FAT1_HUMAN
ID FAT1_HUMAN Reviewed; 4588 AA.
AC Q14517;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Protocadherin Fat 1;
DE AltName: Full=Cadherin family member 7;
DE AltName: Full=Cadherin-related tumor suppressor homolog;
DE AltName: Full=Protein fat homolog;
DE Contains:
DE RecName: Full=Protocadherin Fat 1, nuclear form;
DE Flags: Precursor;
GN Name=FAT1; Synonyms=CDHF7, FAT;
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].
RC TISSUE=Lymphocyte;
RX PubMed=8586420; DOI=10.1006/geno.1995.9884;
RA Dunne J., Hanby A.M., Poulsom R., Jones T.A., Sheer D., Chin W.G., Da S.M.,
RA Zhao Q., Beverley P.C.L., Owen M.J.;
RT "Molecular cloning and tissue expression of FAT, the human homologue of the
RT Drosophila fat gene that is located on chromosome 4q34-q35 and encodes a
RT putative adhesion molecule.";
RL Genomics 30:207-223(1995).
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 SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=15922730; DOI=10.1016/j.yexcr.2005.03.006;
RA Magg T., Schreiner D., Solis G.P., Bade E.G., Hofer H.W.;
RT "Processing of the human protocadherin Fat1 and translocation of its
RT cytoplasmic domain to the nucleus.";
RL Exp. Cell Res. 307:100-108(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [5]
RP INTERACTION WITH ATN1 AND RERE.
RX PubMed=19131340; DOI=10.1074/jbc.m809333200;
RA Hou R., Sibinga N.E.;
RT "Atrophin proteins interact with the Fat1 cadherin and regulate migration
RT and orientation in vascular smooth muscle cells.";
RL J. Biol. Chem. 284:6955-6965(2009).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-3422 AND ASN-3716.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-3716.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [8]
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 [9]
RP VARIANTS SER-902; VAL-1393 AND SER-3732.
RX PubMed=26566883; DOI=10.1136/jmedgenet-2015-103179;
RA Rafiullah R., Aslamkhan M., Paramasivam N., Thiel C., Mustafa G.,
RA Wiemann S., Schlesner M., Wade R.C., Rappold G.A., Berkel S.;
RT "Homozygous missense mutation in the LMAN2L gene segregates with
RT intellectual disability in a large consanguineous Pakistani family.";
RL J. Med. Genet. 53:138-144(2016).
RN [10]
RP VARIANTS LEU-546; ASP-1147; HIS-1930 AND MET-4422.
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: [Protocadherin Fat 1]: Plays an essential role for cellular
CC polarization, directed cell migration and modulating cell-cell contact.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via the C-terminus 4300-4400 AA) with ATN1
CC (PubMed:19131340). Interacts with RERE (PubMed:19131340).
CC {ECO:0000269|PubMed:19131340}.
CC -!- INTERACTION:
CC Q14517; Q8N8S7: ENAH; NbExp=2; IntAct=EBI-1171918, EBI-2834410;
CC Q14517; Q9NSC5: HOMER3; NbExp=4; IntAct=EBI-1171918, EBI-748420;
CC Q14517; Q99JP6: Homer3; Xeno; NbExp=2; IntAct=EBI-1171918, EBI-6272061;
CC -!- SUBCELLULAR LOCATION: [Protocadherin Fat 1]: Cell membrane
CC {ECO:0000269|PubMed:15922730}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:15922730}.
CC -!- SUBCELLULAR LOCATION: [Protocadherin Fat 1, nuclear form]: Nucleus
CC {ECO:0000269|PubMed:15922730}.
CC -!- TISSUE SPECIFICITY: Expressed in many epithelial and some endothelial
CC and smooth muscle cells.
CC -!- DOMAIN: A PTB-like motif (DNXYH sequence) is required for the targeting
CC to the leading edge. This motif represents a minimal protein-protein
CC interaction core motif that is not regulated by tyrosine
CC phosphorylation (By similarity). {ECO:0000250}.
CC -!- PTM: Undergoes proteolytic cleavage. The extracellular domain is
CC cleaved off and the cytoplasmic domain (about 400 AA) shuttles to the
CC nucleus. {ECO:0000269|PubMed:15922730}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FAT1ID40533ch4q35.html";
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DR EMBL; X87241; CAA60685.1; -; mRNA.
DR EMBL; AC107050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS47177.1; -.
DR RefSeq; NP_005236.2; NM_005245.3.
DR RefSeq; XP_006714202.1; XM_006714139.2.
DR SMR; Q14517; -.
DR BioGRID; 108489; 153.
DR IntAct; Q14517; 47.
DR MINT; Q14517; -.
DR STRING; 9606.ENSP00000406229; -.
DR GlyGen; Q14517; 22 sites.
DR iPTMnet; Q14517; -.
DR PhosphoSitePlus; Q14517; -.
DR BioMuta; FAT1; -.
DR DMDM; 334302792; -.
DR EPD; Q14517; -.
DR jPOST; Q14517; -.
DR MassIVE; Q14517; -.
DR MaxQB; Q14517; -.
DR PaxDb; Q14517; -.
DR PeptideAtlas; Q14517; -.
DR PRIDE; Q14517; -.
DR ProteomicsDB; 60019; -.
DR Antibodypedia; 964; 176 antibodies from 26 providers.
DR DNASU; 2195; -.
DR Ensembl; ENST00000441802.7; ENSP00000406229.2; ENSG00000083857.15.
DR GeneID; 2195; -.
DR KEGG; hsa:2195; -.
DR MANE-Select; ENST00000441802.7; ENSP00000406229.2; NM_005245.4; NP_005236.2.
DR UCSC; uc003izf.4; human.
DR CTD; 2195; -.
DR DisGeNET; 2195; -.
DR GeneCards; FAT1; -.
DR HGNC; HGNC:3595; FAT1.
DR HPA; ENSG00000083857; Tissue enhanced (choroid).
DR MIM; 600976; gene.
DR neXtProt; NX_Q14517; -.
DR OpenTargets; ENSG00000083857; -.
DR PharmGKB; PA164719952; -.
DR VEuPathDB; HostDB:ENSG00000083857; -.
DR eggNOG; KOG1219; Eukaryota.
DR GeneTree; ENSGT00940000157733; -.
DR HOGENOM; CLU_000042_2_0_1; -.
DR InParanoid; Q14517; -.
DR OrthoDB; 12779at2759; -.
DR PhylomeDB; Q14517; -.
DR TreeFam; TF316403; -.
DR PathwayCommons; Q14517; -.
DR SignaLink; Q14517; -.
DR BioGRID-ORCS; 2195; 6 hits in 1075 CRISPR screens.
DR ChiTaRS; FAT1; human.
DR GeneWiki; FAT_(gene); -.
DR GenomeRNAi; 2195; -.
DR Pharos; Q14517; Tbio.
DR PRO; PR:Q14517; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q14517; protein.
DR Bgee; ENSG00000083857; Expressed in choroid plexus epithelium and 201 other tissues.
DR ExpressionAtlas; Q14517; baseline and differential.
DR Genevisible; Q14517; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IEA:Ensembl.
DR GO; GO:0003412; P:establishment of epithelial cell apical/basal polarity involved in camera-type eye morphogenesis; IEA:Ensembl.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
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; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
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; 34.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00282; LamG; 1.
DR SUPFAM; SSF49313; SSF49313; 33.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00232; CADHERIN_1; 17.
DR PROSITE; PS50268; CADHERIN_2; 33.
DR PROSITE; PS00022; EGF_1; 4.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell membrane; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Nucleus; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..4588
FT /note="Protocadherin Fat 1"
FT /id="PRO_0000004017"
FT CHAIN ?..4588
FT /note="Protocadherin Fat 1, nuclear form"
FT /id="PRO_0000408559"
FT TOPO_DOM 22..4181
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 4182..4202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 4203..4588
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..149
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 150..257
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 368..463
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 464..569
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 570..673
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 718..822
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 823..927
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 928..1034
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1035..1139
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1140..1245
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1246..1357
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1359..1456
FT /note="Cadherin 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1457..1562
FT /note="Cadherin 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1563..1667
FT /note="Cadherin 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1668..1765
FT /note="Cadherin 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1766..1879
FT /note="Cadherin 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1880..1979
FT /note="Cadherin 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1980..2081
FT /note="Cadherin 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2082..2182
FT /note="Cadherin 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2183..2283
FT /note="Cadherin 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2284..2390
FT /note="Cadherin 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2391..2492
FT /note="Cadherin 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2493..2596
FT /note="Cadherin 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2597..2703
FT /note="Cadherin 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2704..2809
FT /note="Cadherin 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2810..2918
FT /note="Cadherin 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2919..3023
FT /note="Cadherin 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3024..3125
FT /note="Cadherin 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3126..3230
FT /note="Cadherin 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3231..3335
FT /note="Cadherin 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3336..3440
FT /note="Cadherin 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3441..3545
FT /note="Cadherin 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3546..3647
FT /note="Cadherin 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3790..3827
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3829..4009
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 4013..4050
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4052..4088
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4089..4125
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4127..4163
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 4255..4275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4303..4327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4343..4376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4435..4479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4565..4588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 4204..4214
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 4378..4382
FT /note="PTB-like motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 4255..4273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4356..4376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4435..4450
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 660
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 740
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 791
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 998
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1748
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1864
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1902
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1940
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1991
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 2464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 3444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3613
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3716
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 4152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 3794..3805
FT /evidence="ECO:0000250"
FT DISULFID 3799..3816
FT /evidence="ECO:0000250"
FT DISULFID 3818..3826
FT /evidence="ECO:0000250"
FT DISULFID 3976..4009
FT /evidence="ECO:0000250"
FT DISULFID 4017..4028
FT /evidence="ECO:0000250"
FT DISULFID 4022..4038
FT /evidence="ECO:0000250"
FT DISULFID 4040..4049
FT /evidence="ECO:0000250"
FT DISULFID 4056..4067
FT /evidence="ECO:0000250"
FT DISULFID 4061..4076
FT /evidence="ECO:0000250"
FT DISULFID 4078..4087
FT /evidence="ECO:0000250"
FT DISULFID 4093..4104
FT /evidence="ECO:0000250"
FT DISULFID 4098..4113
FT /evidence="ECO:0000250"
FT DISULFID 4115..4124
FT /evidence="ECO:0000250"
FT DISULFID 4131..4142
FT /evidence="ECO:0000250"
FT DISULFID 4136..4151
FT /evidence="ECO:0000250"
FT DISULFID 4153..4162
FT /evidence="ECO:0000250"
FT VARIANT 131
FT /note="A -> V (in dbSNP:rs3733415)"
FT /id="VAR_055590"
FT VARIANT 546
FT /note="P -> L (found in a patient with spinocerebellar
FT ataxia; unknown pathological significance;
FT dbSNP:rs1373737710)"
FT /evidence="ECO:0000269|PubMed:29053796"
FT /id="VAR_080732"
FT VARIANT 902
FT /note="R -> S (in dbSNP:rs555992573)"
FT /evidence="ECO:0000269|PubMed:26566883"
FT /id="VAR_076441"
FT VARIANT 1147
FT /note="E -> D (found in a patient with spinocerebellar
FT ataxia; unknown pathological significance;
FT dbSNP:rs1383300308)"
FT /evidence="ECO:0000269|PubMed:29053796"
FT /id="VAR_080733"
FT VARIANT 1330
FT /note="N -> S (in dbSNP:rs874111)"
FT /id="VAR_055591"
FT VARIANT 1393
FT /note="I -> V (in dbSNP:rs753226094)"
FT /evidence="ECO:0000269|PubMed:26566883"
FT /id="VAR_076442"
FT VARIANT 1564
FT /note="A -> T (in dbSNP:rs2304867)"
FT /id="VAR_055592"
FT VARIANT 1605
FT /note="N -> D (in dbSNP:rs6836935)"
FT /id="VAR_055593"
FT VARIANT 1930
FT /note="D -> H (found in a patient with spinocerebellar
FT ataxia; unknown pathological significance;
FT dbSNP:rs748622474)"
FT /evidence="ECO:0000269|PubMed:29053796"
FT /id="VAR_080734"
FT VARIANT 3732
FT /note="N -> S (in dbSNP:rs373241719)"
FT /evidence="ECO:0000269|PubMed:26566883"
FT /id="VAR_076443"
FT VARIANT 3800
FT /note="P -> H (in dbSNP:rs11731738)"
FT /id="VAR_055594"
FT VARIANT 4422
FT /note="T -> M (found in a patient with spinocerebellar
FT ataxia; unknown pathological significance;
FT dbSNP:rs1409256573)"
FT /evidence="ECO:0000269|PubMed:29053796"
FT /id="VAR_080735"
FT CONFLICT 322
FT /note="G -> D (in Ref. 1; CAA60685)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="S -> R (in Ref. 1; CAA60685)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="V -> I (in Ref. 1; CAA60685)"
FT /evidence="ECO:0000305"
FT CONFLICT 614
FT /note="F -> L (in Ref. 1; CAA60685)"
FT /evidence="ECO:0000305"
FT CONFLICT 862
FT /note="V -> L (in Ref. 1; CAA60685)"
FT /evidence="ECO:0000305"
FT CONFLICT 1064
FT /note="R -> G (in Ref. 1; CAA60685)"
FT /evidence="ECO:0000305"
FT CONFLICT 1273
FT /note="H -> R (in Ref. 1; CAA60685)"
FT /evidence="ECO:0000305"
FT CONFLICT 1351
FT /note="P -> Q (in Ref. 1; CAA60685)"
FT /evidence="ECO:0000305"
FT CONFLICT 1526..1529
FT /note="HQHT -> SPAH (in Ref. 1; CAA60685)"
FT /evidence="ECO:0000305"
FT CONFLICT 1604
FT /note="G -> GNIG (in Ref. 1; CAA60685)"
FT /evidence="ECO:0000305"
FT CONFLICT 2006
FT /note="N -> S (in Ref. 1; CAA60685)"
FT /evidence="ECO:0000305"
FT CONFLICT 2054
FT /note="T -> I (in Ref. 1; CAA60685)"
FT /evidence="ECO:0000305"
FT CONFLICT 2385
FT /note="D -> G (in Ref. 1; CAA60685)"
FT /evidence="ECO:0000305"
FT CONFLICT 2618..2619
FT /note="VL -> S (in Ref. 1; CAA60685)"
FT /evidence="ECO:0000305"
FT CONFLICT 2718
FT /note="I -> V (in Ref. 1; CAA60685)"
FT /evidence="ECO:0000305"
FT CONFLICT 3113
FT /note="L -> V (in Ref. 1; CAA60685)"
FT /evidence="ECO:0000305"
FT CONFLICT 4059
FT /note="K -> N (in Ref. 1; CAA60685)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4588 AA; 506273 MW; 1896223E46E3B892 CRC64;
MGRHLALLLL LLLLFQHFGD SDGSQRLEQT PLQFTHLEYN VTVQENSAAK TYVGHPVKMG
VYITHPAWEV RYKIVSGDSE NLFKAEEYIL GDFCFLRIRT KGGNTAILNR EVKDHYTLIV
KALEKNTNVE ARTKVRVQVL DTNDLRPLFS PTSYSVSLPE NTAIRTSIAR VSATDADIGT
NGEFYYSFKD RTDMFAIHPT SGVIVLTGRL DYLETKLYEM EILAADRGMK LYGSSGISSM
AKLTVHIEQA NECAPVITAV TLSPSELDRD PAYAIVTVDD CDQGANGDIA SLSIVAGDLL
QQFRTVRSFP GSKEYKVKAI GGIDWDSHPF GYNLTLQAKD KGTPPQFSSV KVIHVTSPQF
KAGPVKFEKD VYRAEISEFA PPNTPVVMVK AIPAYSHLRY VFKSTPGKAK FSLNYNTGLI
SILEPVKRQQ AAHFELEVTT SDRKASTKVL VKVLGANSNP PEFTQTAYKA AFDENVPIGT
TVMSLSAVDP DEGENGYVTY SIANLNHVPF AIDHFTGAVS TSENLDYELM PRVYTLRIRA
SDWGLPYRRE VEVLATITLN NLNDNTPLFE KINCEGTIPR DLGVGEQITT VSAIDADELQ
LVQYQIEAGN ELDFFSLNPN SGVLSLKRSL MDGLGAKVSF HSLRITATDG ENFATPLYIN
ITVAASHKLV NLQCEETGVA KMLAEKLLQA NKLHNQGEVE DIFFDSHSVN AHIPQFRSTL
PTGIQVKENQ PVGSSVIFMN STDLDTGFNG KLVYAVSGGN EDSCFMIDME TGMLKILSPL
DRETTDKYTL NITVYDLGIP QKAAWRLLHV VVVDANDNPP EFLQESYFVE VSEDKEVHSE
IIQVEATDKD LGPNGHVTYS IVTDTDTFSI DSVTGVVNIA RPLDRELQHE HSLKIEARDQ
AREEPQLFST VVVKVSLEDV NDNPPTFIPP NYRVKVREDL PEGTVIMWLE AHDPDLGQSG
QVRYSLLDHG EGNFDVDKLS GAVRIVQQLD FEKKQVYNLT VRAKDKGKPV SLSSTCYVEV
EVVDVNENLH PPVFSSFVEK GTVKEDAPVG SLVMTVSAHD EDARRDGEIR YSIRDGSGVG
VFKIGEETGV IETSDRLDRE STSHYWLTVF ATDQGVVPLS SFIEIYIEVE DVNDNAPQTS
EPVYYPEIME NSPKDVSVVQ IEAFDPDSSS NDKLMYKITS GNPQGFFSIH PKTGLITTTS
RKLDREQQDE HILEVTVTDN GSPPKSTIAR VIVKILDEND NKPQFLQKFY KIRLPEREKP
DRERNARREP LYHVIATDKD EGPNAEISYS IEDGNEHGKF FIEPKTGVVS SKRFSAAGEY
DILSIKAVDN GRPQKSSTTR LHIEWISKPK PSLEPISFEE SFFTFTVMES DPVAHMIGVI
SVEPPGIPLW FDITGGNYDS HFDVDKGTGT IIVAKPLDAE QKSNYNLTVE ATDGTTTILT
QVFIKVIDTN DHRPQFSTSK YEVVIPEDTA PETEILQISA VDQDEKNKLI YTLQSSRDPL
SLKKFRLDPA TGSLYTSEKL DHEAVHQHTL TVMVRDQDVP VKRNFARIVV NVSDTNDHAP
WFTASSYKGR VYESAAVGSV VLQVTALDKD KGKNAEVLYS IESGNIGNSF MIDPVLGSIK
TAKELDRSNQ AEYDLMVKAT DKGSPPMSEI TSVRIFVTIA DNASPKFTSK EYSVELSETV
SIGSFVGMVT AHSQSSVVYE IKDGNTGDAF DINPHSGTII TQKALDFETL PIYTLIIQGT
NMAGLSTNTT VLVHLQDEND NAPVFMQAEY TGLISESASI NSVVLTDRNV PLVIRAADAD
KDSNALLVYH IVEPSVHTYF AIDSSTGAIH TVLSLDYEET SIFHFTVQVH DMGTPRLFAE
YAANVTVHVI DINDCPPVFA KPLYEASLLL PTYKGVKVIT VNATDADSSA FSQLIYSITE
GNIGEKFSMD YKTGALTVQN TTQLRSRYEL TVRASDGRFA GLTSVKINVK ESKESHLKFT
QDVYSAVVKE NSTEAETLAV ITAIGNPINE PLFYHILNPD RRFKISRTSG VLSTTGTPFD
REQQEAFDVV VEVTEEHKPS AVAHVVVKVI VEDQNDNAPV FVNLPYYAVV KVDTEVGHVI
RYVTAVDRDS GRNGEVHYYL KEHHEHFQIG PLGEISLKKQ FELDTLNKEY LVTVVAKDGG
NPAFSAEVIV PITVMNKAMP VFEKPFYSAE IAESIQVHSP VVHVQANSPE GLKVFYSITD
GDPFSQFTIN FNTGVINVIA PLDFEAHPAY KLSIRATDSL TGAHAEVFVD IIVDDINDNP
PVFAQQSYAV TLSEASVIGT SVVQVRATDS DSEPNRGISY QMFGNHSKSH DHFHVDSSTG
LISLLRTLDY EQSRQHTIFV RAVDGGMPTL SSDVIVTVDV TDLNDNPPLF EQQIYEARIS
EHAPHGHFVT CVKAYDADSS DIDKLQYSIL SGNDHKHFVI DSATGIITLS NLHRHALKPF
YSLNLSVSDG VFRSSTQVHV TVIGGNLHSP AFLQNEYEVE LAENAPLHTL VMEVKTTDGD
SGIYGHVTYH IVNDFAKDRF YINERGQIFT LEKLDRETPA EKVISVRLMA KDAGGKVAFC
TVNVILTDDN DNAPQFRATK YEVNIGSSAA KGTSVVKVLA SDADEGSNAD ITYAIEADSE
SVKENLEINK LSGVITTKES LIGLENEFFT FFVRAVDNGS PSKESVVLVY VKILPPEMQL
PKFSEPFYTF TVSEDVPIGT EIDLIRAEHS GTVLYSLVKG NTPESNRDES FVIDRQSGRL
KLEKSLDHET TKWYQFSILA RCTQDDHEMV ASVDVSIQVK DANDNSPVFE SSPYEAFIVE
NLPGGSRVIQ IRASDADSGT NGQVMYSLDQ SQSVEVIESF AINMETGWIT TLKELDHEKR
DNYQIKVVAS DHGEKIQLSS TAIVDVTVTD VNDSPPRFTA EIYKGTVSED DPQGGVIAIL
STTDADSEEI NRQVTYFITG GDPLGQFAVE TIQNEWKVYV KKPLDREKRD NYLLTITATD
GTFSSKAIVE VKVLDANDNS PVCEKTLYSD TIPEDVLPGK LIMQISATDA DIRSNAEITY
TLLGSGAEKF KLNPDTGELK TSTPLDREEQ AVYHLLVRAT DGGGRFCQAS IVLTLEDVND
NAPEFSADPY AITVFENTEP GTLLTRVQAT DADAGLNRKI LYSLIDSADG QFSINELSGI
IQLEKPLDRE LQAVYTLSLK AVDQGLPRRL TATGTVIVSV LDINDNPPVF EYREYGATVS
EDILVGTEVL QVYAASRDIE ANAEITYSII SGNEHGKFSI DSKTGAVFII ENLDYESSHE
YYLTVEATDG GTPSLSDVAT VNVNVTDIND NTPVFSQDTY TTVISEDAVL EQSVITVMAD
DADGPSNSHI HYSIIDGNQG SSFTIDPVRG EVKVTKLLDR ETISGYTLTV QASDNGSPPR
VNTTTVNIDV SDVNDNAPVF SRGNYSVIIQ ENKPVGFSVL QLVVTDEDSS HNGPPFFFTI
VTGNDEKAFE VNPQGVLLTS SAIKRKEKDH YLLQVKVADN GKPQLSSLTY IDIRVIEESI
YPPAILPLEI FITSSGEEYS GGVIGKIHAT DQDVYDTLTY SLDPQMDNLF SVSSTGGKLI
AHKKLDIGQY LLNVSVTDGK FTTVADITVH IRQVTQEMLN HTIAIRFANL TPEEFVGDYW
RNFQRALRNI LGVRRNDIQI VSLQSSEPHP HLDVLLFVEK PGSAQISTKQ LLHKINSSVT
DIEEIIGVRI LNVFQKLCAG LDCPWKFCDE KVSVDESVMS THSTARLSFV TPRHHRAAVC
LCKEGRCPPV HHGCEDDPCP EGSECVSDPW EEKHTCVCPS GRFGQCPGSS SMTLTGNSYV
KYRLTENENK LEMKLTMRLR TYSTHAVVMY ARGTDYSILE IHHGRLQYKF DCGSGPGIVS
VQSIQVNDGQ WHAVALEVNG NYARLVLDQV HTASGTAPGT LKTLNLDNYV FFGGHIRQQG
TRHGRSPQVG NGFRGCMDSI YLNGQELPLN SKPRSYAHIE ESVDVSPGCF LTATEDCASN
PCQNGGVCNP SPAGGYYCKC SALYIGTHCE ISVNPCSSKP CLYGGTCVVD NGGFVCQCRG
LYTGQRCQLS PYCKDEPCKN GGTCFDSLDG AVCQCDSGFR GERCQSDIDE CSGNPCLHGA
LCENTHGSYH CNCSHEYRGR HCEDAAPNQY VSTPWNIGLA EGIGIVVFVA GIFLLVVVFV
LCRKMISRKK KHQAEPKDKH LGPATAFLQR PYFDSKLNKN IYSDIPPQVP VRPISYTPSI
PSDSRNNLDR NSFEGSAIPE HPEFSTFNPE SVHGHRKAVA VCSVAPNLPP PPPSNSPSDS
DSIQKPSWDF DYDTKVVDLD PCLSKKPLEE KPSQPYSARE SLSEVQSLSS FQSESCDDNG
YHWDTSDWMP SVPLPDIQEF PNYEVIDEQT PLYSADPNAI DTDYYPGGYD IESDFPPPPE
DFPAADELPP LPPEFSNQFE SIHPPRDMPA AGSLGSSSRN RQRFNLNQYL PNFYPLDMSE
PQTKGTGENS TCREPHAPYP PGYQRHFEAP AVESMPMSVY ASTASCSDVS ACCEVESEVM
MSDYESGDDG HFEEVTIPPL DSQQHTEV
