CAD11_HUMAN
ID CAD11_HUMAN Reviewed; 796 AA.
AC P55287; A8K5D6; A8MZC8; B7WP28; Q15065; Q15066; Q9UQ93; Q9UQ94;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Cadherin-11;
DE AltName: Full=OSF-4;
DE AltName: Full=Osteoblast cadherin;
DE Short=OB-cadherin;
DE Flags: Precursor;
GN Name=CDH11;
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 1).
RC TISSUE=Brain;
RX PubMed=7982033; DOI=10.3109/15419069409014199;
RA Tanihara H., Sano K., Heimark R.L., St John T., Suzuki S.;
RT "Cloning of five human cadherins clarifies characteristic features of
RT cadherin extracellular domain and provides further evidence for two
RT structurally different types of cadherin.";
RL Cell Adhes. Commun. 2:15-26(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS ILE-275 AND
RP ALA-373.
RC TISSUE=Osteosarcoma;
RX PubMed=8163513; DOI=10.1016/s0021-9258(17)32685-6;
RA Okazaki M., Takeshita S., Kawai S., Kikuno R., Tsujimura A., Kudo A.,
RA Amann E.;
RT "Molecular cloning and characterization of OB-cadherin, a new member of
RT cadherin family expressed in osteoblasts.";
RL J. Biol. Chem. 269:12092-12098(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-373.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 269-796 (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=2059658; DOI=10.1091/mbc.2.4.261;
RA Suzuki S., Sano K., Tanihara H.;
RT "Diversity of the cadherin family: evidence for eight new cadherins in
RT nervous tissue.";
RL Cell Regul. 2:261-270(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 600-668.
RA Kools P.F.J., Hogendoorn P.C.W., Bovee J.V.M.G., van Roy F.;
RT "Alternative cadherin-11 transcripts encoding truncated adhesion molecules
RT are detectable in both human cancer and normal cells.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP CHROMOSOMAL TRANSLOCATION WITH USP6.
RX PubMed=15026324; DOI=10.1158/0008-5472.can-03-2827;
RA Oliveira A.M., Hsi B.L., Weremowicz S., Rosenberg A.E., Dal Cin P.,
RA Joseph N., Bridge J.A., Perez-Atayde A.R., Fletcher J.A.;
RT "USP6 (Tre2) fusion oncogenes in aneurysmal bone cyst.";
RL Cancer Res. 64:1920-1923(2004).
RN [8]
RP INVOLVEMENT IN ESWS.
RX PubMed=28988429; DOI=10.1002/ajmg.a.38495;
RA Taskiran E.Z., Karaosmanoglu B., Kosukcu C., Dogan O.A.,
RA Taylan-Sekeroglu H., Simsek-Kiper P.O., Utine E.G., Boduroglu K.,
RA Alikasifoglu M.;
RT "Homozygous indel mutation in CDH11 as the probable cause of Elsahy-Waters
RT syndrome.";
RL Am. J. Med. Genet. A 173:3143-3152(2017).
RN [9]
RP INVOLVEMENT IN ESWS, AND VARIANT ESWS 232-TYR--SER-796 DEL.
RX PubMed=29271567; DOI=10.1002/ajmg.a.38568;
RA Harms F.L., Nampoothiri S., Anazi S., Yesodharan D., Alawi M., Kutsche K.,
RA Alkuraya F.S.;
RT "Elsahy-Waters syndrome is caused by biallelic mutations in CDH11.";
RL Am. J. Med. Genet. A 176:477-482(2018).
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They
CC preferentially interact with themselves in a homophilic manner in
CC connecting cells; cadherins may thus contribute to the sorting of
CC heterogeneous cell types.
CC -!- SUBUNIT: Interacts with PCDH8. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P55287-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P55287-2; Sequence=VSP_000640, VSP_000641;
CC -!- TISSUE SPECIFICITY: Expressed mainly in brain but also found in other
CC tissues. Expressed in neuroblasts.
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC cadherin domain and rigidify the connections, imparting a strong
CC curvature to the full-length ectodomain. {ECO:0000250}.
CC -!- DISEASE: Note=A chromosomal aberration involving CDH11 is a common
CC genetic feature of aneurysmal bone cyst, a benign osseous neoplasm.
CC Translocation t(16;17)(q22;p13) with USP6. The translocation generates
CC a fusion gene in which the strong CDH11 promoter is fused to the entire
CC USP6 coding sequence, resulting in USP6 transcriptional up-regulation.
CC -!- DISEASE: Elsahy-Waters syndrome (ESWS) [MIM:211380]: An autosomal
CC recessive syndrome characterized by moderate intellectual disability,
CC hypospadias and characteristic craniofacial morphology, which includes
CC brachycephaly, facial asymmetry, exotropia, hypertelorism, telechantus,
CC broad nose, concave nasal ridge, underdeveloped mid-face, prognathism,
CC and radicular dentin dysplasia. {ECO:0000269|PubMed:28988429,
CC ECO:0000269|PubMed:29271567}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; L34056; AAA35622.1; -; mRNA.
DR EMBL; D21254; BAA04798.1; -; mRNA.
DR EMBL; D21255; BAA04799.1; -; mRNA.
DR EMBL; AK291251; BAF83940.1; -; mRNA.
DR EMBL; AC010533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF060370; AAD27755.1; -; Genomic_DNA.
DR EMBL; AF060369; AAD27755.1; JOINED; Genomic_DNA.
DR EMBL; AF060370; AAD27756.1; -; Genomic_DNA.
DR EMBL; AF060369; AAD27756.1; JOINED; Genomic_DNA.
DR CCDS; CCDS10803.1; -. [P55287-1]
DR CCDS; CCDS81993.1; -. [P55287-2]
DR PIR; A38992; A38992.
DR RefSeq; NP_001295321.1; NM_001308392.1. [P55287-2]
DR RefSeq; NP_001788.2; NM_001797.3. [P55287-1]
DR RefSeq; XP_005255818.1; XM_005255761.3.
DR RefSeq; XP_005255819.1; XM_005255762.2. [P55287-1]
DR RefSeq; XP_005255820.1; XM_005255763.2. [P55287-1]
DR RefSeq; XP_011521105.1; XM_011522803.2. [P55287-1]
DR AlphaFoldDB; P55287; -.
DR SMR; P55287; -.
DR BioGRID; 107444; 8.
DR CORUM; P55287; -.
DR IntAct; P55287; 5.
DR MINT; P55287; -.
DR STRING; 9606.ENSP00000268603; -.
DR GlyGen; P55287; 4 sites.
DR iPTMnet; P55287; -.
DR PhosphoSitePlus; P55287; -.
DR BioMuta; CDH11; -.
DR DMDM; 146345381; -.
DR jPOST; P55287; -.
DR MassIVE; P55287; -.
DR MaxQB; P55287; -.
DR PaxDb; P55287; -.
DR PeptideAtlas; P55287; -.
DR PRIDE; P55287; -.
DR ProteomicsDB; 56837; -. [P55287-1]
DR ProteomicsDB; 56838; -. [P55287-2]
DR ABCD; P55287; 16 sequenced antibodies.
DR Antibodypedia; 4584; 822 antibodies from 38 providers.
DR DNASU; 1009; -.
DR Ensembl; ENST00000268603.9; ENSP00000268603.4; ENSG00000140937.14. [P55287-1]
DR Ensembl; ENST00000394156.7; ENSP00000377711.3; ENSG00000140937.14. [P55287-2]
DR GeneID; 1009; -.
DR KEGG; hsa:1009; -.
DR MANE-Select; ENST00000268603.9; ENSP00000268603.4; NM_001797.4; NP_001788.2.
DR UCSC; uc002eoi.4; human. [P55287-1]
DR CTD; 1009; -.
DR DisGeNET; 1009; -.
DR GeneCards; CDH11; -.
DR HGNC; HGNC:1750; CDH11.
DR HPA; ENSG00000140937; Tissue enhanced (ovary, placenta).
DR MalaCards; CDH11; -.
DR MIM; 211380; phenotype.
DR MIM; 600023; gene.
DR neXtProt; NX_P55287; -.
DR OpenTargets; ENSG00000140937; -.
DR Orphanet; 1299; Branchioskeletogenital syndrome.
DR PharmGKB; PA26284; -.
DR VEuPathDB; HostDB:ENSG00000140937; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000153691; -.
DR HOGENOM; CLU_005284_4_3_1; -.
DR InParanoid; P55287; -.
DR OMA; ERYFVIN; -.
DR OrthoDB; 188978at2759; -.
DR PhylomeDB; P55287; -.
DR TreeFam; TF329887; -.
DR PathwayCommons; P55287; -.
DR Reactome; R-HSA-418990; Adherens junctions interactions.
DR SignaLink; P55287; -.
DR SIGNOR; P55287; -.
DR BioGRID-ORCS; 1009; 14 hits in 1068 CRISPR screens.
DR ChiTaRS; CDH11; human.
DR GeneWiki; CDH11; -.
DR GenomeRNAi; 1009; -.
DR Pharos; P55287; Tbio.
DR PRO; PR:P55287; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P55287; protein.
DR Bgee; ENSG00000140937; Expressed in periodontal ligament and 193 other tissues.
DR ExpressionAtlas; P55287; baseline and differential.
DR Genevisible; P55287; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0034332; P:adherens junction organization; IBA:GO_Central.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR GO; GO:0021957; P:corticospinal tract morphogenesis; IEA:Ensembl.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0001503; P:ossification; NAS:UniProtKB.
DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR Gene3D; 4.10.900.10; -; 1.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR InterPro; IPR027397; Catenin-bd_sf.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR Pfam; PF00028; Cadherin; 4.
DR Pfam; PF01049; Cadherin_C; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SUPFAM; SSF49313; SSF49313; 5.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Chromosomal rearrangement; Cleavage on pair of basic residues; Deafness;
KW Disease variant; Glycoprotein; Intellectual disability; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..53
FT /evidence="ECO:0000255"
FT /id="PRO_0000003785"
FT CHAIN 54..796
FT /note="Cadherin-11"
FT /id="PRO_0000003786"
FT TOPO_DOM 54..617
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 618..640
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 641..796
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 54..159
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 160..268
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 269..383
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 384..486
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 487..612
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT MOD_RES 788
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55288"
FT MOD_RES 791
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P55288"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 632..693
FT /note="VIVVLFVTLRRQKKEPLIVFEEEDVRENIITYDDEGGGEEDTEAFDIATLQN
FT PDGINGFIPR -> GCPSLMEPPSPREDMRLLYLGFQLMLFSYVKVNRRFCLLGVFIKL
FT PFLYVVATESPTTLTSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8163513"
FT /id="VSP_000640"
FT VAR_SEQ 694..796
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8163513"
FT /id="VSP_000641"
FT VARIANT 232..796
FT /note="Missing (in ESWS)"
FT /evidence="ECO:0000269|PubMed:29271567"
FT /id="VAR_080481"
FT VARIANT 255
FT /note="T -> M (in dbSNP:rs35195)"
FT /id="VAR_031945"
FT VARIANT 275
FT /note="M -> I (in dbSNP:rs1130821)"
FT /evidence="ECO:0000269|PubMed:8163513"
FT /id="VAR_031946"
FT VARIANT 373
FT /note="S -> A (in dbSNP:rs35213)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:8163513"
FT /id="VAR_031947"
FT CONFLICT 271..272
FT /note="SV -> RL (in Ref. 1; AAA35622 and 5; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="K -> E (in Ref. 1; AAA35622 and 5; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="K -> Q (in Ref. 1; AAA35622 and 5; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 796 AA; 87965 MW; E17090EC95C59936 CRC64;
MKENYCLQAA LVCLGMLCHS HAFAPERRGH LRPSFHGHHE KGKEGQVLQR SKRGWVWNQF
FVIEEYTGPD PVLVGRLHSD IDSGDGNIKY ILSGEGAGTI FVIDDKSGNI HATKTLDREE
RAQYTLMAQA VDRDTNRPLE PPSEFIVKVQ DINDNPPEFL HETYHANVPE RSNVGTSVIQ
VTASDADDPT YGNSAKLVYS ILEGQPYFSV EAQTGIIRTA LPNMDREAKE EYHVVIQAKD
MGGHMGGLSG TTKVTITLTD VNDNPPKFPQ SVYQMSVSEA AVPGEEVGRV KAKDPDIGEN
GLVTYNIVDG DGMESFEITT DYETQEGVIK LKKPVDFETK RAYSLKVEAA NVHIDPKFIS
NGPFKDTVTV KISVEDADEP PMFLAPSYIH EVQENAAAGT VVGRVHAKDP DAANSPIRYS
IDRHTDLDRF FTINPEDGFI KTTKPLDREE TAWLNITVFA AEIHNRHQEA KVPVAIRVLD
VNDNAPKFAA PYEGFICESD QTKPLSNQPI VTISADDKDD TANGPRFIFS LPPEIIHNPN
FTVRDNRDNT AGVYARRGGF SRQKQDLYLL PIVISDGGIP PMSSTNTLTI KVCGCDVNGA
LLSCNAEAYI LNAGLSTGAL IAILACIVIL LVIVVLFVTL RRQKKEPLIV FEEEDVRENI
ITYDDEGGGE EDTEAFDIAT LQNPDGINGF IPRKDIKPEY QYMPRPGLRP APNSVDVDDF
INTRIQEADN DPTAPPYDSI QIYGYEGRGS VAGSLSSLES ATTDSDLDYD YLQNWGPRFK
KLADLYGSKD TFDDDS
