FAT4_HUMAN
ID FAT4_HUMAN Reviewed; 4981 AA.
AC Q6V0I7; A8K5Z6; B5MDG4; Q3LIA6; Q8TCK7; Q9H5T6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Protocadherin Fat 4;
DE Short=hFat4;
DE AltName: Full=Cadherin family member 14;
DE AltName: Full=FAT tumor suppressor homolog 4;
DE AltName: Full=Fat-like cadherin protein FAT-J;
DE Flags: Precursor;
GN Name=FAT4; Synonyms=CDHF14, FATJ; ORFNames=Nbla00548;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=15003449; DOI=10.1016/j.jmb.2004.01.026;
RA Hoeng J.C., Ivanov N.V., Hodor P., Xia M., Wei N., Blevins R., Gerhold D.,
RA Borodovsky M., Liu Y.;
RT "Identification of new human cadherin genes using a combination of protein
RT motif search and gene finding methods.";
RL J. Mol. Biol. 337:307-317(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2709-3364 (ISOFORM 1).
RC TISSUE=Neuroblastoma;
RX PubMed=12880961; DOI=10.1016/s0304-3835(03)00085-5;
RA Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S.,
RA Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S.,
RA Hirato J., Nakagawara A.;
RT "Neuroblastoma oligo-capping cDNA project: toward the understanding of the
RT genesis and biology of neuroblastoma.";
RL Cancer Lett. 197:63-68(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3819-4981 (ISOFORM 3), AND
RP VARIANTS ASN-3873 AND SER-4972.
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4859-4981.
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=16865240;
RA Katoh Y., Katoh M.;
RT "Comparative integromics on FAT1, FAT2, FAT3 and FAT4.";
RL Int. J. Mol. Med. 18:523-528(2006).
RN [7]
RP DEVELOPMENTAL STAGE, AND VARIANTS VMLDS2 LYS-2375; PHE-4159 AND TYR-4398.
RX PubMed=24056717; DOI=10.1038/ng.2765;
RA Cappello S., Gray M.J., Badouel C., Lange S., Einsiedler M., Srour M.,
RA Chitayat D., Hamdan F.F., Jenkins Z.A., Morgan T., Preitner N., Uster T.,
RA Thomas J., Shannon P., Morrison V., Di Donato N., Van Maldergem L.,
RA Neuhann T., Newbury-Ecob R., Swinkells M., Terhal P., Wilson L.C.,
RA Zwijnenburg P.J., Sutherland-Smith A.J., Black M.A., Markie D.,
RA Michaud J.L., Simpson M.A., Mansour S., McNeill H., Goetz M.,
RA Robertson S.P.;
RT "Mutations in genes encoding the cadherin receptor-ligand pair DCHS1 and
RT FAT4 disrupt cerebral cortical development.";
RL Nat. Genet. 45:1300-1308(2013).
RN [8]
RP INVOLVEMENT IN HKLLS2, AND VARIANTS HKLLS2 LEU-475; GLN-486; LYS-2375 AND
RP PHE-4282.
RX PubMed=24913602; DOI=10.1007/s00439-014-1456-y;
RA Alders M., Al-Gazali L., Cordeiro I., Dallapiccola B., Garavelli L.,
RA Tuysuz B., Salehi F., Haagmans M.A., Mook O.R., Majoie C.B., Mannens M.M.,
RA Hennekam R.C.;
RT "Hennekam syndrome can be caused by FAT4 mutations and be allelic to Van
RT Maldergem syndrome.";
RL Hum. Genet. 133:1161-1167(2014).
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. FAT4
CC plays a role in the maintenance of planar cell polarity as well as in
CC inhibition of YAP1-mediated neuroprogenitor cell proliferation and
CC differentiation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterophilic interaction with DCHS1; this interaction affects
CC their respective protein levels. Interacts (via cytoplasmic domain)
CC with MPDZ. Forms a complex with PALS1 and MPDZ. {ECO:0000250}.
CC -!- INTERACTION:
CC Q6V0I7; Q9H2K2: TNKS2; NbExp=2; IntAct=EBI-948985, EBI-4398527;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Note=In the kidney, localizes to
CC primary cilia. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6V0I7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6V0I7-2; Sequence=VSP_032334, VSP_032335, VSP_032336,
CC VSP_032337;
CC Name=3;
CC IsoId=Q6V0I7-3; Sequence=VSP_032338;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in fetal brain, infant
CC brain, brain tumor and colorectal cancer. {ECO:0000269|PubMed:15003449,
CC ECO:0000269|PubMed:16865240}.
CC -!- DEVELOPMENTAL STAGE: In embryos at 9 weeks the strongest expression is
CC detected in the apical neuroepithelium, with weaker staining being
CC present in the subventricular zone and within the cortical plate.
CC {ECO:0000269|PubMed:24056717}.
CC -!- DISEASE: Van Maldergem syndrome 2 (VMLDS2) [MIM:615546]: An autosomal
CC recessive disorder characterized by intellectual disability, typical
CC craniofacial features, auditory malformations resulting in hearing
CC loss, and skeletal and limb malformations. Some patients have renal
CC hypoplasia. Brain MRI typically shows periventricular nodular
CC heterotopia. {ECO:0000269|PubMed:24056717}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- DISEASE: Hennekam lymphangiectasia-lymphedema syndrome 2 (HKLLS2)
CC [MIM:616006]: A form of Hennekam lymphangiectasia-lymphedema syndrome,
CC a generalized lymph-vessels dysplasia characterized by intestinal
CC lymphangiectasia with severe lymphedema of the limbs, genitalia and
CC face. In addition, affected individuals have unusual facies and some
CC manifest intellectual disability. HKLLS2 individuals have
CC lymphangiectasia variably affecting the gut, pericardium, lungs,
CC kidneys, and genitalia. Other features include camptodactyly and rare
CC syndactyly. HKLLS2 inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:24913602}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15534.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15534.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAF84150.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY356402; AAR13653.1; -; mRNA.
DR EMBL; AC079835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092629; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC098865; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB075518; BAE45762.1; -; mRNA.
DR EMBL; AK026709; BAB15534.1; ALT_SEQ; mRNA.
DR EMBL; AK291461; BAF84150.1; ALT_INIT; mRNA.
DR EMBL; AL713715; CAD28510.1; -; mRNA.
DR CCDS; CCDS3732.3; -. [Q6V0I7-1]
DR RefSeq; NP_001278214.1; NM_001291285.1.
DR RefSeq; NP_001278232.1; NM_001291303.1.
DR RefSeq; NP_078858.4; NM_024582.4. [Q6V0I7-1]
DR SMR; Q6V0I7; -.
DR BioGRID; 122763; 67.
DR ELM; Q6V0I7; -.
DR IntAct; Q6V0I7; 26.
DR MINT; Q6V0I7; -.
DR STRING; 9606.ENSP00000377862; -.
DR CarbonylDB; Q6V0I7; -.
DR GlyGen; Q6V0I7; 38 sites.
DR iPTMnet; Q6V0I7; -.
DR PhosphoSitePlus; Q6V0I7; -.
DR BioMuta; FAT4; -.
DR DMDM; 172046149; -.
DR EPD; Q6V0I7; -.
DR jPOST; Q6V0I7; -.
DR MassIVE; Q6V0I7; -.
DR MaxQB; Q6V0I7; -.
DR PaxDb; Q6V0I7; -.
DR PeptideAtlas; Q6V0I7; -.
DR PRIDE; Q6V0I7; -.
DR ProteomicsDB; 67701; -. [Q6V0I7-1]
DR ProteomicsDB; 67702; -. [Q6V0I7-2]
DR ProteomicsDB; 67703; -. [Q6V0I7-3]
DR Antibodypedia; 62649; 119 antibodies from 17 providers.
DR DNASU; 79633; -.
DR Ensembl; ENST00000335110.5; ENSP00000335169.5; ENSG00000196159.14. [Q6V0I7-2]
DR GeneID; 79633; -.
DR KEGG; hsa:79633; -.
DR UCSC; uc003ifj.5; human. [Q6V0I7-1]
DR CTD; 79633; -.
DR DisGeNET; 79633; -.
DR GeneCards; FAT4; -.
DR HGNC; HGNC:23109; FAT4.
DR HPA; ENSG00000196159; Low tissue specificity.
DR MalaCards; FAT4; -.
DR MIM; 612411; gene.
DR MIM; 615546; phenotype.
DR MIM; 616006; phenotype.
DR neXtProt; NX_Q6V0I7; -.
DR OpenTargets; ENSG00000196159; -.
DR Orphanet; 314679; Cerebrofacioarticular syndrome.
DR Orphanet; 2136; Hennekam syndrome.
DR PharmGKB; PA134954366; -.
DR VEuPathDB; HostDB:ENSG00000196159; -.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000155719; -.
DR HOGENOM; CLU_000042_1_0_1; -.
DR InParanoid; Q6V0I7; -.
DR OrthoDB; 34489at2759; -.
DR PhylomeDB; Q6V0I7; -.
DR TreeFam; TF331335; -.
DR PathwayCommons; Q6V0I7; -.
DR SignaLink; Q6V0I7; -.
DR BioGRID-ORCS; 79633; 12 hits in 1067 CRISPR screens.
DR ChiTaRS; FAT4; human.
DR GeneWiki; FAT4; -.
DR GenomeRNAi; 79633; -.
DR Pharos; Q6V0I7; Tbio.
DR PRO; PR:Q6V0I7; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q6V0I7; protein.
DR Bgee; ENSG00000196159; Expressed in calcaneal tendon and 160 other tissues.
DR ExpressionAtlas; Q6V0I7; baseline and differential.
DR Genevisible; Q6V0I7; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0021987; P:cerebral cortex development; ISS:UniProtKB.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR GO; GO:0035329; P:hippo signaling; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0022008; P:neurogenesis; ISS:UniProtKB.
DR CDD; cd00110; LamG; 2.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF00028; Cadherin; 32.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 34.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 5.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49313; SSF49313; 34.
DR SUPFAM; SSF49899; SSF49899; 2.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS00232; CADHERIN_1; 23.
DR PROSITE; PS50268; CADHERIN_2; 34.
DR PROSITE; PS00022; EGF_1; 7.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 6.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Deafness; Disease variant;
KW Disulfide bond; EGF-like domain; Glycoprotein; Intellectual disability;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..4981
FT /note="Protocadherin Fat 4"
FT /id="PRO_0000324637"
FT TOPO_DOM 39..4504
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 4505..4525
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 4526..4981
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 43..135
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 136..250
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 251..353
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 359..475
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 476..582
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 584..689
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 690..793
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 794..893
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 894..996
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 997..1100
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1101..1210
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1211..1315
FT /note="Cadherin 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1316..1420
FT /note="Cadherin 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1421..1529
FT /note="Cadherin 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1529..1629
FT /note="Cadherin 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1630..1740
FT /note="Cadherin 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1741..1841
FT /note="Cadherin 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1842..1944
FT /note="Cadherin 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1945..2051
FT /note="Cadherin 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2051..2154
FT /note="Cadherin 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2155..2259
FT /note="Cadherin 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2260..2364
FT /note="Cadherin 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2365..2466
FT /note="Cadherin 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2467..2567
FT /note="Cadherin 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2568..2669
FT /note="Cadherin 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2670..2773
FT /note="Cadherin 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2773..2872
FT /note="Cadherin 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2873..2983
FT /note="Cadherin 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2984..3089
FT /note="Cadherin 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3090..3194
FT /note="Cadherin 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3195..3298
FT /note="Cadherin 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3299..3404
FT /note="Cadherin 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3405..3510
FT /note="Cadherin 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3509..3620
FT /note="Cadherin 34"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3802..3860
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3862..3898
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3900..3936
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3938..3974
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3975..4159
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 4162..4198
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4217..4398
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 4426..4463
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 4534..4584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4680..4713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4706..4795
FT /note="Necessary and sufficient for interaction with MPDZ"
FT /evidence="ECO:0000250"
FT REGION 4752..4856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4869..4911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4957..4981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4534..4555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4811..4825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4873..4889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4876
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2PZL6"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 721
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 825
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 880
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 946
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1085
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1828
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1899
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1967
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2921
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2937
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3036
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3706
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3758
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4017
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 3806..3817
FT /evidence="ECO:0000250"
FT DISULFID 3811..3848
FT /evidence="ECO:0000250"
FT DISULFID 3850..3859
FT /evidence="ECO:0000250"
FT DISULFID 3866..3877
FT /evidence="ECO:0000250"
FT DISULFID 3871..3886
FT /evidence="ECO:0000250"
FT DISULFID 3888..3897
FT /evidence="ECO:0000250"
FT DISULFID 3904..3915
FT /evidence="ECO:0000250"
FT DISULFID 3909..3924
FT /evidence="ECO:0000250"
FT DISULFID 3926..3935
FT /evidence="ECO:0000250"
FT DISULFID 3942..3953
FT /evidence="ECO:0000250"
FT DISULFID 3947..3962
FT /evidence="ECO:0000250"
FT DISULFID 3964..3973
FT /evidence="ECO:0000250"
FT DISULFID 4133..4159
FT /evidence="ECO:0000250"
FT DISULFID 4166..4177
FT /evidence="ECO:0000250"
FT DISULFID 4171..4186
FT /evidence="ECO:0000250"
FT DISULFID 4188..4197
FT /evidence="ECO:0000250"
FT DISULFID 4365..4398
FT /evidence="ECO:0000250"
FT DISULFID 4430..4441
FT /evidence="ECO:0000250"
FT DISULFID 4435..4451
FT /evidence="ECO:0000250"
FT DISULFID 4453..4462
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..1702
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15003449"
FT /id="VSP_032334"
FT VAR_SEQ 1703..1725
FT /note="CLYLVDVYAIEKSTAFPRTQRAE -> MVTTVVAVGDTLAQPLAAAEVFI
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15003449"
FT /id="VSP_032335"
FT VAR_SEQ 3932..3966
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15003449"
FT /id="VSP_032336"
FT VAR_SEQ 4159..4200
FT /note="CPRLEGACTRSPCQHGGTCMDYWSWQQCHCKEGLTGKYCEKS -> YGDFIS
FT YCFKEKKCKKVCFT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15003449"
FT /id="VSP_032337"
FT VAR_SEQ 4360
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032338"
FT VARIANT 453
FT /note="Q -> L (in dbSNP:rs6847454)"
FT /id="VAR_048580"
FT VARIANT 475
FT /note="F -> L (in HKLLS2)"
FT /evidence="ECO:0000269|PubMed:24913602"
FT /id="VAR_071948"
FT VARIANT 486
FT /note="E -> Q (in HKLLS2)"
FT /evidence="ECO:0000269|PubMed:24913602"
FT /id="VAR_071949"
FT VARIANT 807
FT /note="A -> V (in dbSNP:rs1039808)"
FT /id="VAR_048581"
FT VARIANT 2375
FT /note="E -> K (in VMLDS2 and HKLLS2; dbSNP:rs398122955)"
FT /evidence="ECO:0000269|PubMed:24056717,
FT ECO:0000269|PubMed:24913602"
FT /id="VAR_070925"
FT VARIANT 2826
FT /note="D -> N (in dbSNP:rs1485569217)"
FT /id="VAR_039860"
FT VARIANT 3524
FT /note="G -> D (in dbSNP:rs1567047)"
FT /id="VAR_039861"
FT VARIANT 3828
FT /note="K -> E (in dbSNP:rs17009684)"
FT /id="VAR_039862"
FT VARIANT 3873
FT /note="S -> N (in dbSNP:rs12650153)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_039863"
FT VARIANT 4159
FT /note="C -> F (in VMLDS2; dbSNP:rs398122953)"
FT /evidence="ECO:0000269|PubMed:24056717"
FT /id="VAR_070926"
FT VARIANT 4282
FT /note="S -> F (in HKLLS2; dbSNP:rs199682210)"
FT /evidence="ECO:0000269|PubMed:24913602"
FT /id="VAR_071950"
FT VARIANT 4374
FT /note="E -> K (in dbSNP:rs11942361)"
FT /id="VAR_039864"
FT VARIANT 4398
FT /note="C -> Y (in VMLDS2; dbSNP:rs398122954)"
FT /evidence="ECO:0000269|PubMed:24056717"
FT /id="VAR_070927"
FT VARIANT 4972
FT /note="P -> S (in dbSNP:rs1014867)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_039865"
FT VARIANT 4977
FT /note="A -> T (in dbSNP:rs17009858)"
FT /id="VAR_039866"
FT CONFLICT 3363..3364
FT /note="RE -> QK (in Ref. 3; BAE45762)"
FT /evidence="ECO:0000305"
FT CONFLICT 4868
FT /note="P -> S (in Ref. 4; BAB15534)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4981 AA; 542687 MW; 588ED3CC4612A6DA CRC64;
MDLAPDRATG RPWLPLHTLS VSQLLRVFWL LSLLPGQAWV HGAEPRQVFQ VLEEQPPGTL
VGTIQTRPGF TYRLSESHAL FAINSSTGAL YTTSTIDRES LPSDVINLVV LSSAPTYPTE
VRVLVRDLND NAPVFPDPSI VVTFKEDSSS GRQVILDTAT DSDIGSNGVD HRSYRIIRGN
EAGRFRLDIT LNPSGEGAFL HLVSKGGLDR EVTPQYQLLV EVEDKGEPKR RGYLQVNVTV
QDINDNPPVF GSSHYQAGVP EDAVVGSSVL QVAAADADEG TNADIRYRLQ DEGTPFQMDP
ETGLITVREP LDFEARRQYS LTVQAMDRGV PSLTGRAEAL IQLLDVNDND PVVKFRYFPA
TSRYASVDEN AQVGTVVALL TVTDADSPAA NGNISVQILG GNEQRHFEVQ SSKVPNLSLI
KVASALDRER IPSYNLTVSV SDNYGAPPGA AVQARSSVAS LVIFVNDIND HPPVFSQQVY
RVNLSEEAPP GSYVSGISAT DGDSGLNANL RYSIVSGNGL GWFHISEHSG LVTTGSSGGL
DRELASQIVL NISARDQGVH PKVSYAQLVV TLLDVNDEKP VFSQPEGYDV SVVENAPTGT
ELLMLRATDG DLGDNGTVRF SLQEAETDRR SFRLDPVSGR LSTISSLDRE EQAFYSLLVL
ATDLGSPPQS SMARINVSLL DINDNSPVFY PVQYFAHIKE NEPGGSYITT VSATDPDLGT
NGTVKYSISA GDRSRFQVNA QSGVISTRMA LDREEKTAYQ LQIVATDGGN LQSPNQAIVT
ITVLDTQDNP PVFSQVAYSF VVFENVALGY HVGSVSASTM DLNSNISYLI TTGDQKGMFA
INQVTGQLTT ANVIDREEQS FYQLKVVASG GTVTGDTMVN ITVKDLNDNS PHFLQAIESV
NVVENWQAGH SIFQAKAVDP DEGVNGMVLY SLKQNPKNLF AINEKNGTIS LLGPLDVHAG
SYQIEILASD MGVPQLSSSV ILTVYVHDVN DNSPVFDQLS YEVTLSESEP VNSRFFKVQA
SDKDSGANGE IAYTIAEGNT GDAFGIFPDG QLYIKSELDR ELQDRYVLMV VASDRAVEPL
SATVNVTVIL EDVNDNRPLF NSTNYTFYFE EEQRAGSFVG KVSAVDKDFG PNGEVRYSFE
MVQPDFELHA ISGEITNTHQ FDRESLMRRR GTAVFSFTVI ATDQGIPQPL KDQATVHVYM
KDINDNAPKF LKDFYQATIS ESAANLTQVL RVSASDVDEG NNGLIHYSII KGNEERQFAI
DSTSGQVTLI GKLDYEATPA YSLVIQAVDS GTIPLNSTCT LNIDILDEND NTPSFPKSTL
FVDVLENMRI GELVSSVTAT DSDSGDNADL YYSITGTNNH GTFSISPNTG SIFLAKKLDF
ETQSLYKLNI TAKDQGRPPR SSTMSVVIHV RDFNDNPPSF PPGDIFKSIV ENIPIGTSVI
SVTAHDPDAD INGQLSYTII QQMPRGNHFT IDEVKGTIYT NAEIDREFAN LFELTVKAND
QAVPIETRRY ALKNVTILVT DLNDNVPMFI SQNALAADPS AVIGSVLTTI MAADPDEGAN
GEIEYEIING DTDTFIVDRY SGDLRVASAL VPSQLIYNLI VSATDLGPER RKSTTELTII
LQGLDGPVFT QPKYITILKE GEPIGTNVIS IEAASPRGSE APVEYYIVSV RCEEKTVGRL
FTIGRHTGII QTAAILDREQ GACLYLVDVY AIEKSTAFPR TQRAEVEITL QDINDNPPVF
PTDMLDLTVE ENIGDGSKIM QLTAMDADEG ANALVTYTII SGADDSFRID PESGDLIATR
RLDRERRSKY SLLVRADDGL QSSDMRINIT VSDVNDHTPK FSRPVYSFDI PEDTIPGSLV
AAILATDDDS GVNGEITYIV NEDDEDGIFF LNPITGVFNL TRLLDYEVQQ YYILTVRAED
GGGQFTTIRV YFNILDVNDN PPIFSLNSYS TSLMENLPVG STVLVFNVTD ADDGINSQLT
YSIASGDSLG QFTVDKNGVL KVLKALDRES QSFYNLVVQV HDLPQIPASR FTSTAQVSII
LLDVNDNPPT FLSPKLTYIP ENTPIDTVVF KAQATDPDSG PNSYIEYTLL NPLGNKFSIG
TIDGEVRLTG ELDREEVSNY TLTVVATDKG QPSLSSSTEV VVMVLDINDN NPIFAQALYK
VEINENTLTG TDIIQVFAAD GDEGTNGQVR YGIVNGNTNQ EFRIDSVTGA ITVAKPLDRE
KTPTYHLTVQ ATDRGSTPRT DTSTVSIVLL DINDFVPVFE LSPYSVNVPE NLGTLPRTIL
QVVARDDDRG SNSKLSYVLF GGNEDNAFTL SASGELGVTQ SLDRETKERF VLMITATDSG
SPALTGTGTI NVIVDDVNDN VPTFASKAYF TTIPEDAPTG TDVLLVNASD ADASKNAVIR
IIGGNSQFTI NPSTGQIITS ALLDRETKDN YTLVVVCSDA GSPEPLSSST SVLVTVTDVN
DNPPRFQHHP YVTHIPSPTL PGSFVFAVTV TDADIGPNSE LHYSLSGRNS EKFHIDPLRG
AIMAAGPLNG ASEVTFSVHV KDGGSFPKTD STTVTVRFVN KADFPKVRAK EQTFMFPENQ
PVSSLVTTIT GSSLRGEPMS YYIASGNLGN TFQIDQLTGQ VSISQPLDFE KIQKYVVWIE
ARDGGFPPFS SYEKLDITVL DVNDNAPIFK EDPFISEILE NLSPRKILTV SAMDKDSGPN
GQLDYEIVNG NMENSFSINH ATGEIRSVRP LDREKVSHYV LTIKSSDKGS PSQSTSVKVM
INILDENDNA PRFSQIFSAH VPENSPLGYT VTRVTTSDED IGINAISRYS IMDASLPFTI
NPSTGDIVIS RPLNREDTDR YRIRVSAHDS GWTVSTDVTI FVTDINDNAP RFSRTSYYLD
CPELTEIGSK VTQVFATDPD EGSNGQVFYF IKSQSEYFRI NATTGEIFNK QILKYQNVTG
FSNVNINRHS FIVTSSDRGK PSLISETTVT INIVDSNDNA PQFLKSKYFT PVTKNVKVGT
KLIRVTAIDD KDFGLNSEVE YFISNDNHLG KFKLDNDTGW ISVASSLISD LNQNFFITVT
AKDKGNPPLS SQATVHITVT EENYHTPEFS QSHMSATIPE SHSIGSIVRT VSARDRDAAM
NGLIKYSISS GNEEGIFAIN SSTGILTLAK ALDYELCQKH EMTISAIDGG WVARTGYCSV
TVNVIDVNDN SPVFLSDDYF PTVLENAPSG TTVIHLNATD ADSGTNAVIA YTVQSSDSDL
FVIDPNTGVI TTQGFLDFET KQSYHLTVKA FNVPDEERCS FATVNIQLKG TNEYVPRFVS
KLYYFEISEA APKGTIVGEV FASDRDLGTD GEVHYLIFGN SRKKGFQINK KTGQIYVSGI
LDREKEERVS LKVLAKNFGS IRGADIDEVT VNVTVLDAND PPIFTLNIYS VQISEGVPIG
THVTFVSAFD SDSIPSWSRF SYFIGSGNEN GAFSINPQTG QITVTAELDR ETLPIYNLSV
LAVDSGTPSA TGSASLLVTL EDINDNGPML TVSEGEVMEN KRPGTLVMTL QSTDPDLPPN
QGPFTYYLLS TGPATSYFSL STAGVLSTTR EIDREQIADF YLSVVTKDSG VPQMSSTGTV
HITVIDQNDN PSQSRTVEIF VNYYGNLFPG GILGSVKPQD PDVLDSFHCS LTSGVTSLFS
IPGGTCDLNS QPRSTDGTFD LTVLSNDGVH STVTSNIRVF FAGFSNATVD NSILLRLGVP
TVKDFLTNHY LHFLRIASSQ LTGLGTAVQL YSAYEENNRT FLLAAVKRNH NQYVNPSGVA
TFFESIKEIL LRQSGVKVES VDHDSCVHGP CQNGGSCLRR LAVSSVLKSR ESLPVIIVAN
EPLQPFLCKC LPGYAGSWCE IDIDECLPSP CHSGGTCHNL VGGFSCSCPD GFTGRACERD
INECLQSPCK NGAICQNFPG SFNCVCKTGY TGKMCESSVN YCECNPCFNG GSCQSGVDSY
YCHCPFGVFG KHCELNSYGF EELSYMEFPS LDPNNNYIYV KFATIKSHAL LLYNYDNQTG
DRAEFLALEI AEERLRFSYN LGSGTYKLTT MKKVSDGHFH TVIARRAGMA ASLTVDSCSE
NQEPGYCTVS NVAVSDDWTL DVQPNRVTVG GIRSLEPILQ RRGHVESHDF VGCIMEFAVN
GRPLEPSQAL AAQGILDQCP RLEGACTRSP CQHGGTCMDY WSWQQCHCKE GLTGKYCEKS
VTPDTALSLE GKGRLDYHMS QNEKREYLLR QSLRGAMLEP FGVNSLEVKF RTRSENGVLI
HIQESSNYTT VKIKNGKVYF TSDAGIAGKV ERNIPEVYVA DGHWHTFLIG KNGTATVLSV
DRIYNRDIIH PTQDFGGLDV LTISLGGIPP NQAHRDAQTA GFDGCIASMW YGGESLPFSG
KHSLASISKT DPSVKIGCRG PNICASNPCW GDLLCINQWY AYRCVPPGDC ASHPCQNGGS
CEPGLHSGFT CSCPDSHTGR TCEMVVACLG VLCPQGKVCK AGSPAGHVCV LSQGPEEISL
PLWAVPAIVG SCATVLALLV LSLILCNQCR GKKAKNPKEE KKPKEKKKKG SENVAFDDPD
NIPPYGDDMT VRKQPEGNPK PDIIERENPY LIYDETDIPH NSETIPSAPL ASPEQEIEHY
DIDNASSIAP SDADIIQHYK QFRSHTPKFS IQRHSPLGFA RQSPMPLGAS SLTYQPSYGQ
GLRTSSLSHS ACPTPNPLSR HSPAPFSKSS TFYRNSPARE LHLPIRDGNT LEMHGDTCQP
GIFNYATRLG RRSKSPQAMA SHGSRPGSRL KQPIGQIPLE SSPPVGLSIE EVERLNTPRP
RNPSICSADH GRSSSEEDCR RPLSRTRNPA DGIPAPESSS DSDSHESFTC SEMEYDREKP
MVYTSRMPKL SQVNESDADD EDNYGARLKP RRYHGRRAEG GPVGTQAAAP GTADNTLPMK
LGQQAGTFNW DNLLNWGPGF GHYVDVFKDL ASLPEKAAAN EEGKAGTTKP VPKDGEAEQY
V
