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 27-MAR-2024, entry version 209. 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="https://atlasgeneticsoncology.org/gene/40533/FAT1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 163. DR IntAct; Q14517; 49. DR MINT; Q14517; -. DR STRING; 9606.ENSP00000406229; -. DR GlyCosmos; Q14517; 22 sites, No reported glycans. DR GlyGen; Q14517; 31 sites, 3 O-linked glycans (9 sites). DR iPTMnet; Q14517; -. DR PhosphoSitePlus; Q14517; -. DR SwissPalm; Q14517; -. DR BioMuta; FAT1; -. DR DMDM; 334302792; -. DR EPD; Q14517; -. DR jPOST; Q14517; -. DR MassIVE; Q14517; -. DR MaxQB; Q14517; -. DR PaxDb; 9606-ENSP00000406229; -. DR PeptideAtlas; Q14517; -. DR ProteomicsDB; 60019; -. DR Pumba; Q14517; -. DR Antibodypedia; 964; 214 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 AGR; HGNC:3595; -. DR CTD; 2195; -. DR DisGeNET; 2195; -. DR GeneCards; FAT1; -. DR HGNC; HGNC:3595; FAT1. DR HPA; ENSG00000083857; Tissue enhanced (choroid). DR MalaCards; FAT1; -. 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; 2961370at2759; -. DR PhylomeDB; Q14517; -. DR TreeFam; TF316403; -. DR PathwayCommons; Q14517; -. DR SignaLink; Q14517; -. DR BioGRID-ORCS; 2195; 7 hits in 1164 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 203 other cell types or tissues. DR ExpressionAtlas; Q14517; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl. DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. 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: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:1904385; P:cellular response to angiotensin; IEA:Ensembl. 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 GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IEA:Ensembl. DR CDD; cd11304; Cadherin_repeat; 33. DR CDD; cd00054; EGF_CA; 4. DR CDD; cd00110; LamG; 1. DR Gene3D; 2.60.120.200; -; 1. DR Gene3D; 2.60.40.60; Cadherins; 33. DR Gene3D; 2.10.25.10; Laminin; 4. DR InterPro; IPR039808; Cadherin. 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 PANTHER; PTHR24027; CADHERIN-23; 1. DR PANTHER; PTHR24027:SF422; NEURAL-CADHERIN 2-RELATED; 1. 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; Cadherin-like; 33. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR SUPFAM; SSF57196; EGF/Laminin; 4. 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. DR Genevisible; Q14517; HS. 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; uncertain significance; 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; uncertain significance; 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; uncertain significance; 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; uncertain significance; 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 //