FAT2_HUMAN
ID FAT2_HUMAN Reviewed; 4349 AA.
AC Q9NYQ8; O75091; Q9NSR7;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Protocadherin Fat 2;
DE Short=hFat2;
DE AltName: Full=Cadherin family member 8;
DE AltName: Full=Multiple epidermal growth factor-like domains protein 1;
DE Short=Multiple EGF-like domains protein 1;
DE Flags: Precursor;
GN Name=FAT2; Synonyms=CDHF8, KIAA0811, MEGF1;
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].
RX PubMed=10716726; DOI=10.1073/pnas.97.7.3124;
RA Wu Q., Maniatis T.;
RT "Large exons encoding multiple ectodomains are a characteristic feature of
RT protocadherin genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3124-3129(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3777-4349, AND VARIANT LEU-4117.
RC TISSUE=Brain;
RX PubMed=9693030; DOI=10.1006/geno.1998.5341;
RA Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
RT "Identification of high-molecular-weight proteins with multiple EGF-like
RT motifs by motif-trap screening.";
RL Genomics 51:27-34(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4142-4349.
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-3904.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [6]
RP 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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17900869; DOI=10.1016/j.jdermsci.2007.07.010;
RA Matsui S., Utani A., Takahashi K., Mukoyama Y., Miyachi Y., Matsuyoshi N.;
RT "Human Fat2 is localized at immature adherens junctions in epidermal
RT keratinocytes.";
RL J. Dermatol. Sci. 48:233-236(2007).
RN [8]
RP FUNCTION.
RX PubMed=18534823; DOI=10.1016/j.jdermsci.2008.04.006;
RA Matsui S., Utani A., Takahashi K., Mukoyama Y., Miyachi Y., Matsuyoshi N.;
RT "Knockdown of Fat2 by siRNA inhibits the migration of human squamous
RT carcinoma cells.";
RL J. Dermatol. Sci. 51:207-210(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP INVOLVEMENT IN SCA45, AND VARIANTS SCA45 ASN-3586 AND GLN-3649.
RX PubMed=29053796; DOI=10.1093/brain/awx251;
RA Nibbeling E.A.R., Duarri A., Verschuuren-Bemelmans C.C., Fokkens M.R.,
RA Karjalainen J.M., Smeets C.J.L.M., de Boer-Bergsma J.J., van der Vries G.,
RA Dooijes D., Bampi G.B., van Diemen C., Brunt E., Ippel E., Kremer B.,
RA Vlak M., Adir N., Wijmenga C., van de Warrenburg B.P.C., Franke L.,
RA Sinke R.J., Verbeek D.S.;
RT "Exome sequencing and network analysis identifies shared mechanisms
RT underlying spinocerebellar ataxia.";
RL Brain 140:2860-2878(2017).
CC -!- FUNCTION: Involved in the regulation of cell migration
CC (PubMed:18534823). May be involved in mediating the organization of the
CC parallel fibers of granule cells during cerebellar development (By
CC similarity). {ECO:0000250|UniProtKB:O88277,
CC ECO:0000269|PubMed:18534823}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Cell junction
CC {ECO:0000269|PubMed:17900869}. Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:O88277}. Note=Localized at adhesion zippers
CC (early state of adherens junctions) of keratinocytes.
CC {ECO:0000269|PubMed:17900869}.
CC -!- TISSUE SPECIFICITY: Expressed in epidermal keratinocytes, infant brain,
CC cerebellum, and also in a variety of tumors, such as pancreatic cancer,
CC diffuse type gastric cancer, ovarian cancer, esophageal cancer, skin
CC squamous cell carcinoma, head and neck cancer. Not expressed in
CC melanoma cell line A375 cells, normal epidermal melanocytes or normal
CC dermal fibroblasts. Expressed in epidermal keratinocytes and squamous
CC cell carcinoma (at protein level). {ECO:0000269|PubMed:16865240,
CC ECO:0000269|PubMed:17900869}.
CC -!- DISEASE: Spinocerebellar ataxia 45 (SCA45) [MIM:617769]: A form of
CC spinocerebellar ataxia, a clinically and genetically heterogeneous
CC group of cerebellar disorders. Patients show progressive incoordination
CC of gait and often poor coordination of hands, speech and eye movements,
CC due to degeneration of the cerebellum with variable involvement of the
CC brainstem and spinal cord. SCA45 is a slowly progressive, autosomal
CC dominant form with onset in adulthood. {ECO:0000269|PubMed:29053796}.
CC Note=The disease may be caused by variants affecting the gene
CC represented in this entry.
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DR EMBL; AF231022; AAF61928.1; -; mRNA.
DR EMBL; AB011535; BAA32463.1; -; mRNA.
DR EMBL; AL157443; CAB75663.1; -; mRNA.
DR EMBL; AC011337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011374; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC034205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS4317.1; -.
DR PIR; T46927; T46927.
DR RefSeq; NP_001438.1; NM_001447.2.
DR RefSeq; XP_006714824.1; XM_006714761.3.
DR RefSeq; XP_011535902.1; XM_011537600.2.
DR RefSeq; XP_011535905.1; XM_011537603.2.
DR RefSeq; XP_016864713.1; XM_017009224.1.
DR RefSeq; XP_016864714.1; XM_017009225.1.
DR SMR; Q9NYQ8; -.
DR BioGRID; 108490; 1.
DR IntAct; Q9NYQ8; 1.
DR STRING; 9606.ENSP00000261800; -.
DR GlyGen; Q9NYQ8; 39 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NYQ8; -.
DR PhosphoSitePlus; Q9NYQ8; -.
DR BioMuta; FAT2; -.
DR DMDM; 296434503; -.
DR EPD; Q9NYQ8; -.
DR MassIVE; Q9NYQ8; -.
DR MaxQB; Q9NYQ8; -.
DR PaxDb; Q9NYQ8; -.
DR PeptideAtlas; Q9NYQ8; -.
DR PRIDE; Q9NYQ8; -.
DR ProteomicsDB; 83267; -.
DR Antibodypedia; 77918; 108 antibodies from 11 providers.
DR DNASU; 2196; -.
DR Ensembl; ENST00000261800.6; ENSP00000261800.5; ENSG00000086570.13.
DR GeneID; 2196; -.
DR KEGG; hsa:2196; -.
DR MANE-Select; ENST00000261800.6; ENSP00000261800.5; NM_001447.3; NP_001438.1.
DR UCSC; uc003lue.5; human.
DR CTD; 2196; -.
DR DisGeNET; 2196; -.
DR GeneCards; FAT2; -.
DR HGNC; HGNC:3596; FAT2.
DR HPA; ENSG00000086570; Tissue enhanced (brain, esophagus, skin).
DR MalaCards; FAT2; -.
DR MIM; 604269; gene.
DR MIM; 617769; phenotype.
DR neXtProt; NX_Q9NYQ8; -.
DR OpenTargets; ENSG00000086570; -.
DR Orphanet; 589527; Spinocerebellar ataxia type 45.
DR PharmGKB; PA28009; -.
DR VEuPathDB; HostDB:ENSG00000086570; -.
DR eggNOG; KOG1219; Eukaryota.
DR GeneTree; ENSGT00940000158507; -.
DR HOGENOM; CLU_000042_2_0_1; -.
DR InParanoid; Q9NYQ8; -.
DR OMA; CFLNEPL; -.
DR OrthoDB; 12779at2759; -.
DR PhylomeDB; Q9NYQ8; -.
DR TreeFam; TF316403; -.
DR PathwayCommons; Q9NYQ8; -.
DR SignaLink; Q9NYQ8; -.
DR BioGRID-ORCS; 2196; 9 hits in 1061 CRISPR screens.
DR GenomeRNAi; 2196; -.
DR Pharos; Q9NYQ8; Tbio.
DR PRO; PR:Q9NYQ8; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9NYQ8; protein.
DR Bgee; ENSG00000086570; Expressed in paraflocculus and 128 other tissues.
DR ExpressionAtlas; Q9NYQ8; baseline and differential.
DR Genevisible; Q9NYQ8; HS.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0031589; P:cell-substrate adhesion; IDA:UniProtKB.
DR GO; GO:0010631; P:epithelial cell migration; IDA:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
DR CDD; cd00110; LamG; 1.
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; IPR001791; Laminin_G.
DR Pfam; PF00028; Cadherin; 29.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 33.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00282; LamG; 1.
DR SUPFAM; SSF49313; SSF49313; 33.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS00232; CADHERIN_1; 14.
DR PROSITE; PS50268; CADHERIN_2; 32.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell junction; Cell membrane; Disease variant;
KW Disulfide bond; EGF-like domain; Glycoprotein; Golgi apparatus; Membrane;
KW Neurodegeneration; Reference proteome; Repeat; Signal;
KW Spinocerebellar ataxia; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..4349
FT /note="Protocadherin Fat 2"
FT /id="PRO_0000004018"
FT TOPO_DOM 19..4048
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 4049..4069
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 4070..4349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..148
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 149..256
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 363..458
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 459..564
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 565..669
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 716..820
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 821..925
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 926..1032
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1033..1137
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1138..1242
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1243..1346
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1350..1448
FT /note="Cadherin 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1449..1555
FT /note="Cadherin 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1556..1660
FT /note="Cadherin 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1661..1758
FT /note="Cadherin 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1759..1872
FT /note="Cadherin 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1969..2070
FT /note="Cadherin 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2071..2171
FT /note="Cadherin 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2172..2272
FT /note="Cadherin 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2273..2379
FT /note="Cadherin 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2380..2481
FT /note="Cadherin 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2482..2585
FT /note="Cadherin 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2586..2691
FT /note="Cadherin 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2692..2797
FT /note="Cadherin 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2798..2906
FT /note="Cadherin 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2907..3011
FT /note="Cadherin 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3012..3113
FT /note="Cadherin 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3114..3218
FT /note="Cadherin 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3219..3321
FT /note="Cadherin 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3322..3426
FT /note="Cadherin 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3427..3531
FT /note="Cadherin 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3532..3642
FT /note="Cadherin 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3773..3944
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 3947..3984
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3986..4022
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 789
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 996
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1904
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1998
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2007
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2368
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 2470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2597
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3772
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3813
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3840
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3873
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3904
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 3989
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 3912..3944
FT /evidence="ECO:0000250"
FT DISULFID 3951..3962
FT /evidence="ECO:0000250"
FT DISULFID 3956..3972
FT /evidence="ECO:0000250"
FT DISULFID 3974..3983
FT /evidence="ECO:0000250"
FT DISULFID 3990..4001
FT /evidence="ECO:0000250"
FT DISULFID 3995..4010
FT /evidence="ECO:0000250"
FT DISULFID 4012..4021
FT /evidence="ECO:0000250"
FT VARIANT 201
FT /note="G -> A (in dbSNP:rs11739693)"
FT /id="VAR_055595"
FT VARIANT 248
FT /note="P -> S (in dbSNP:rs3734061)"
FT /id="VAR_055596"
FT VARIANT 574
FT /note="R -> C (in dbSNP:rs1432862)"
FT /id="VAR_055597"
FT VARIANT 686
FT /note="F -> S (in dbSNP:rs9324700)"
FT /id="VAR_055598"
FT VARIANT 992
FT /note="R -> Q (in dbSNP:rs3734056)"
FT /id="VAR_055599"
FT VARIANT 1004
FT /note="G -> S (in dbSNP:rs3734055)"
FT /id="VAR_055600"
FT VARIANT 1164
FT /note="P -> L (in dbSNP:rs2304053)"
FT /id="VAR_055601"
FT VARIANT 1181
FT /note="Y -> H (in dbSNP:rs6872614)"
FT /id="VAR_061076"
FT VARIANT 1295
FT /note="L -> P (in dbSNP:rs35640822)"
FT /id="VAR_058286"
FT VARIANT 1462
FT /note="V -> M (in dbSNP:rs2278371)"
FT /id="VAR_055602"
FT VARIANT 1515
FT /note="G -> S (in dbSNP:rs2278370)"
FT /id="VAR_055603"
FT VARIANT 1571
FT /note="G -> S (in dbSNP:rs10044879)"
FT /id="VAR_055604"
FT VARIANT 1895
FT /note="R -> W (in dbSNP:rs34464977)"
FT /id="VAR_055605"
FT VARIANT 2054
FT /note="G -> A (in dbSNP:rs34493925)"
FT /id="VAR_055606"
FT VARIANT 2428
FT /note="F -> S (in dbSNP:rs6892335)"
FT /id="VAR_061077"
FT VARIANT 2907
FT /note="A -> T (in dbSNP:rs3734053)"
FT /id="VAR_055607"
FT VARIANT 3318
FT /note="R -> Q (in dbSNP:rs7718054)"
FT /id="VAR_055608"
FT VARIANT 3318
FT /note="R -> W (in dbSNP:rs2304024)"
FT /id="VAR_055609"
FT VARIANT 3514
FT /note="L -> S (in dbSNP:rs2053028)"
FT /id="VAR_055610"
FT VARIANT 3586
FT /note="K -> N (in SCA45; unknown pathological significance;
FT dbSNP:rs770597316)"
FT /evidence="ECO:0000269|PubMed:29053796"
FT /id="VAR_080665"
FT VARIANT 3631
FT /note="M -> I (in dbSNP:rs6650971)"
FT /id="VAR_055611"
FT VARIANT 3649
FT /note="R -> Q (in SCA45; unknown pathological significance;
FT dbSNP:rs201335279)"
FT /evidence="ECO:0000269|PubMed:29053796"
FT /id="VAR_080666"
FT VARIANT 3664
FT /note="A -> G (in dbSNP:rs35963695)"
FT /id="VAR_055612"
FT VARIANT 3953
FT /note="Q -> H (in dbSNP:rs2304029)"
FT /id="VAR_055613"
FT VARIANT 4117
FT /note="P -> L (in dbSNP:rs1105168)"
FT /evidence="ECO:0000269|PubMed:9693030"
FT /id="VAR_055614"
FT CONFLICT 1287
FT /note="D -> Y (in Ref. 1; AAF61928)"
FT /evidence="ECO:0000305"
FT CONFLICT 1303
FT /note="S -> N (in Ref. 1; AAF61928)"
FT /evidence="ECO:0000305"
FT CONFLICT 4160
FT /note="E -> G (in Ref. 2; BAA32463)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4349 AA; 479317 MW; FCEDBB52E252A996 CRC64;
MTIALLGFAI FLLHCATCEK PLEGILSSSA WHFTHSHYNA TIYENSSPKT YVESFEKMGI
YLAEPQWAVR YRIISGDVAN VFKTEEYVVG NFCFLRIRTK SSNTALLNRE VRDSYTLIIQ
ATEKTLELEA LTRVVVHILD QNDLKPLFSP PSYRVTISED MPLKSPICKV TATDADLGQN
AEFYYAFNTR SEMFAIHPTS GVVTVAGKLN VTWRGKHELQ VLAVDRMRKI SEGNGFGSLA
ALVVHVEPAL RKPPAIASVV VTPPDSNDGT TYATVLVDAN SSGAEVESVE VVGGDPGKHF
KAIKSYARSN EFSLVSVKDI NWMEYLHGFN LSLQARSGSG PYFYSQIRGF HLPPSKLSSL
KFEKAVYRVQ LSEFSPPGSR VVMVRVTPAF PNLQYVLKPS SENVGFKLNA RTGLITTTKL
MDFHDRAHYQ LHIRTSPGQA STVVVIDIVD CNNHAPLFNR SSYDGTLDEN IPPGTSVLAV
TATDRDHGEN GYVTYSIAGP KALPFSIDPY LGIISTSKPM DYELMKRIYT FRVRASDWGS
PFRREKEVSI FLQLRNLNDN QPMFEEVNCT GSIRQDWPVG KSIMTMSAID VDELQNLKYE
IVSGNELEYF DLNHFSGVIS LKRPFINLTA GQPTSYSLKI TASDGKNYAS PTTLNITVVK
DPHFEVPVTC DKTGVLTQFT KTILHFIGLQ NQESSDEEFT SLSTYQINHY TPQFEDHFPQ
SIDVLESVPI NTPLARLAAT DPDAGFNGKL VYVIADGNEE GCFDIELETG LLTVAAPLDY
EATNFYILNV TVYDLGTPQK SSWKLLTVNV KDWNDNAPRF PPGGYQLTIS EDTEVGTTIA
ELTTKDADSE DNGRVRYTLL SPTEKFSLHP LTGELVVTGH LDRESEPRYI LKVEARDQPS
KGHQLFSVTD LIITLEDVND NSPQCITEHN RLKVPEDLPP GTVLTFLDAS DPDLGPAGEV
RYVLMDGAHG TFRVDLMTGA LILERELDFE RRAGYNLSLW ASDGGRPLAR RTLCHVEVIV
LDVNENLHPP HFASFVHQGQ VQENSPSGTQ VIVVAAQDDD SGLDGELQYF LRAGTGLAAF
SINQDTGMIQ TLAPLDREFA SYYWLTVLAV DRGSVPLSSV TEVYIEVTDA NDNPPQMSQA
VFYPSIQEDA PVGTSVLQLD AWDPDSSSKG KLTFNITSGN YMGFFMIHPV TGLLSTAQQL
DRENKDEHIL EVTVLDNGEP SLKSTSRVVV GILDVNDNPP IFSHKLFNVR LPERLSPVSP
GPVYRLVASD LDEGLNGRVT YSIEDSDEEA FSIDLVTGVV SSSSTFTAGE YNILTIKATD
SGQPPLSASV RLHIEWIPWP RPSSIPLAFD ETYYSFTVME TDPVNHMVGV ISVEGRPGLF
WFNISGGDKD MDFDIEKTTG SIVIARPLDT RRRSNYNLTV EVTDGSRTIA TQVHIFMIAN
INHHRPQFLE TRYEVRVPQD TVPGVELLRV QAIDQDKGKS LIYTIHGSQD PGSASLFQLD
PSSGVLVTVG KLDLGSGPSQ HTLTVMVRDQ EIPIKRNFVW VTIHVEDGNL HPPRFTQLHY
EASVPDTIAP GTELLQVRAM DADRGVNAEV HYSLLKGNSE GFFNINALLG IITLAQKLDQ
ANHAPHTLTV KAEDQGSPQW HDLATVIIHV YPSDRSAPIF SKSEYFVEIP ESIPVGSPIL
LVSAMSPSEV TYELREGNKD GVFSMNSYSG LISTQKKLDH EKISSYQLKI RGSNMAGAFT
DVMVVVDIID ENDNAPMFLK STFVGQISEA APLYSMIMDK NNNPFVIHAS DSDKEANSLL
VYKILEPEAL KFFKIDPSMG TLTIVSEMDY ESMPSFQFCV YVHDQGSPVL FAPRPAQVII
HVRDVNDSPP RFSEQIYEVA IVGPIHPGME LLMVRASDED SEVNYSIKTG NADEAVTIHP
VTGSISVLNP AFLGLSRKLT IRASDGLYQD TALVKISLTQ VLDKSLQFDQ DVYWAAVKEN
LQDRKALVIL GAQGNHLNDT LSYFLLNGTD MFHMVQSAGV LQTRGVAFDR EQQDTHELAV
EVRDNRTPQR VAQGLVRVSI EDVNDNPPKF KHLPYYTIIQ DGTEPGDVLF QVSATDEDLG
TNGAVTYEFA EDYTYFRIDP YLGDISLKKP FDYQALNKYH LKVIARDGGT PSLQSEEEVL
VTVRNKSNPL FQSPYYKVRV PENITLYTPI LHTQARSPEG LRLIYNIVEE EPLMLFTTDF
KTGVLTVTGP LDYESKTKHV FTVRATDTAL GSFSEATVEV LVEDVNDNPP TFSQLVYTTS
ISEGLPAQTP VIQLLASDQD SGRNRDVSYQ IVEDGSDVSK FFQINGSTGE MSTVQELDYE
AQQHFHVKVR AMDKGDPPLT GETLVVVNVS DINDNPPEFR QPQYEANVSE LATCGHLVLK
VQAIDPDSRD TSRLEYLILS GNQDRHFFIN SSSGIISMFN LCKKHLDSSY NLRVGASDGV
FRATVPVYIN TTNANKYSPE FQQHLYEAEL AENAMVGTKV IDLLAIDKDS GPYGTIDYTI
INKLASEKFS INPNGQIATL QKLDRENSTE RVIAIKVMAR DGGGRVAFCT VKIILTDEND
NPPQFKASEY TVSIQSNVSK DSPVIQVLAY DADEGQNADV TYSVNPEDLV KDVIEINPVT
GVVKVKDSLV GLENQTLDFF IKAQDGGPPH WNSLVPVRLQ VVPKKVSLPK FSEPLYTFSA
PEDLPEGSEI GIVKAVAAQD PVIYSLVRGT TPESNKDGVF SLDPDTGVIK VRKPMDHEST
KLYQIDVMAH CLQNTDVVSL VSVNIQVGDV NDNRPVFEAD PYKAVLTENM PVGTSVIQVT
AIDKDTGRDG QVSYRLSADP GSNVHELFAI DSESGWITTL QELDCETCQT YHFHVVAYDH
GQTIQLSSQA LVQVSITDEN DNAPRFASEE YRGSVVENSE PGELVATLKT LDADISEQNR
QVTCYITEGD PLGQFGISQV GDEWRISSRK TLDREHTAKY LLRVTASDGK FQASVTVEIF
VLDVNDNSPQ CSQLLYTGKV HEDVFPGHFI LKVSATDLDT DTNAQITYSL HGPGAHEFKL
DPHTGELTTL TALDRERKDV FNLVAKATDG GGRSCQADIT LHVEDVNDNA PRFFPSHCAV
AVFDNTTVKT PVAVVFARDP DQGANAQVVY SLPDSAEGHF SIDATTGVIR LEKPLQVRPQ
APLELTVRAS DLGTPIPLST LGTVTVSVVG LEDYLPVFLN TEHSVQVPED APPGTEVLQL
ATLTRPGAEK TGYRVVSGNE QGRFRLDART GILYVNASLD FETSPKYFLS IECSRKSSSS
LSDVTTVMVN ITDVNEHRPQ FPQDPYSTRV LENALVGDVI LTVSATDEDG PLNSDITYSL
IGGNQLGHFT IHPKKGELQV AKALDREQAS SYSLKLRATD SGQPPLHEDT DIAIQVADVN
DNPPRFFQLN YSTTVQENSP IGSKVLQLIL SDPDSPENGP PYSFRITKGN NGSAFRVTPD
GWLVTAEGLS RRAQEWYQLQ IQASDSGIPP LSSLTSVRVH VTEQSHYAPS ALPLEIFITV
GEDEFQGGMV GKIHATDRDP QDTLTYSLAE EETLGRHFSV GAPDGKIIAA QGLPRGHYSF
NVTVSDGTFT TTAGVHVYVW HVGQEALQQA MWMGFYQLTP EELVSDHWRN LQRFLSHKLD
IKRANIHLAS LQPAEAVAGV DVLLVFEGHS GTFYEFQELA SIITHSAKEM EHSVGVQMRS
AMPMVPCQGP TCQGQICHNT VHLDPKVGPT YSTARLSILT PRHHLQRSCS CNGTATRFSG
QSYVRYRAPA ARNWHIHFYL KTLQPQAILL FTNETASVSL KLASGVPQLE YHCLGGFYGN
LSSQRHVNDH EWHSILVEEM DASIRLMVDS MGNTSLVVPE NCRGLRPERH LLLGGLILLH
SSSNVSQGFE GCLDAVVVNE EALDLLAPGK TVAGLLETQA LTQCCLHSDY CSQNTCLNGG
KCSWTHGAGY VCKCPPQFSG KHCEQGRENC TFAPCLEGGT CILSPKGASC NCPHPYTGDR
CEMEARGCSE GHCLVTPEIQ RGDWGQQELL IITVAVAFII ISTVGLLFYC RRCKSHKPVA
MEDPDLLARS VGVDTQAMPA IELNPLSASS CNNLNQPEPS KASVPNELVT FGPNSKQRPV
VCSVPPRLPP AAVPSHSDNE PVIKRTWSSE EMVYPGGAMV WPPTYSRNER WEYPHSEVTQ
GPLPPSAHRH STPVVMPEPN GLYGGFPFPL EMENKRAPLP PRYSNQNLED LMPSRPPSPR
ERLVAPCLNE YTAISYYHSQ FRQGGGGPCL ADGGYKGVGM RLSRAGPSYA VCEVEGAPLA
GQGQPRVPPN YEGSDMVESD YGSCEEVMF
