GenomeNet

Database: UniProt
Entry: Q14517
LinkDB: Q14517
Original site: Q14517 
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   13-FEB-2019, entry version 183.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Da S.M., Zhao Q., Beverley P.C.L., Owen M.J.;
RT   "Molecular cloning and tissue expression of FAT, the human homologue
RT   of the Drosophila fat gene that is located on chromosome 4q34-q35 and
RT   encodes a 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.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   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.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   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.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 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.,
RA   Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT   efficient 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
RT   migration 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
RT   multiple 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-
RT   linked 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.,
RA   Buerckstuemmer T., 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.,
RA   van der Vries G., Dooijes D., Bampi G.B., van Diemen C., Brunt E.,
RA   Ippel E., Kremer B., Vlak M., Adir N., Wijmenga C.,
RA   van de Warrenburg B.P.C., Franke L., 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: Plays an essential role for cellular polarization,
CC       directed cell migration and modulating cell-cell contact.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (via the C-terminus 4300-4400 AA) with ATN1.
CC       Interacts with RERE. Interacts (via EVH1 domains) with ENAH (By
CC       similarity). Interacts (via cytoplasmic domain) with CTNNB1 (By
CC       similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q8N8S7:ENAH; NbExp=2; IntAct=EBI-1171918, EBI-2834410;
CC       Q9NSC5:HOMER3; NbExp=4; IntAct=EBI-1171918, EBI-748420;
CC       Q99JP6:Homer3 (xeno); NbExp=2; IntAct=EBI-1171918, EBI-6272061;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15922730};
CC       Single-pass type I membrane protein {ECO:0000269|PubMed:15922730}.
CC       Nucleus {ECO:0000269|PubMed:15922730}. Cytoplasm, perinuclear
CC       region {ECO:0000269|PubMed:15922730}.
CC   -!- TISSUE SPECIFICITY: Expressed in many epithelial and some
CC       endothelial and smooth muscle cells.
CC   -!- DOMAIN: A PTB-like motif (DNXYH sequence) is required for the
CC       targeting to the leading edge. This motif represents a minimal
CC       protein-protein interaction core motif that is not regulated by
CC       tyrosine 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
CC       the nucleus. {ECO:0000269|PubMed:15922730}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/FAT1ID40533ch4q35.html";
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   UniGene; Hs.481371; -.
DR   ProteinModelPortal; Q14517; -.
DR   SMR; Q14517; -.
DR   BioGrid; 108489; 56.
DR   IntAct; Q14517; 24.
DR   MINT; Q14517; -.
DR   STRING; 9606.ENSP00000406229; -.
DR   iPTMnet; Q14517; -.
DR   PhosphoSitePlus; Q14517; -.
DR   BioMuta; FAT1; -.
DR   DMDM; 334302792; -.
DR   EPD; Q14517; -.
DR   jPOST; Q14517; -.
DR   MaxQB; Q14517; -.
DR   PaxDb; Q14517; -.
DR   PeptideAtlas; Q14517; -.
DR   PRIDE; Q14517; -.
DR   ProteomicsDB; 60019; -.
DR   Ensembl; ENST00000441802; ENSP00000406229; ENSG00000083857.
DR   GeneID; 2195; -.
DR   KEGG; hsa:2195; -.
DR   UCSC; uc003izf.4; human.
DR   CTD; 2195; -.
DR   DisGeNET; 2195; -.
DR   EuPathDB; HostDB:ENSG00000083857.13; -.
DR   GeneCards; FAT1; -.
DR   HGNC; HGNC:3595; FAT1.
DR   HPA; HPA001869; -.
DR   HPA; HPA023882; -.
DR   MIM; 600976; gene.
DR   neXtProt; NX_Q14517; -.
DR   OpenTargets; ENSG00000083857; -.
DR   PharmGKB; PA164719952; -.
DR   eggNOG; KOG1219; Eukaryota.
DR   eggNOG; ENOG410XPEI; LUCA.
DR   GeneTree; ENSGT00940000157733; -.
DR   HOGENOM; HOG000046499; -.
DR   HOVERGEN; HBG005641; -.
DR   InParanoid; Q14517; -.
DR   KO; K16506; -.
DR   OrthoDB; 12779at2759; -.
DR   TreeFam; TF316403; -.
DR   ChiTaRS; FAT1; human.
DR   GeneWiki; FAT_(gene); -.
DR   GenomeRNAi; 2195; -.
DR   PRO; PR:Q14517; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   Bgee; ENSG00000083857; Expressed in 229 organ(s), highest expression level in epithelium of mammary gland.
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:0048593; P:camera-type eye morphogenesis; IEA:Ensembl.
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:0007163; P:establishment or maintenance of cell polarity; ISS:UniProtKB.
DR   GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IEA:Ensembl.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
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; IPR013032; EGF-like_CS.
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; Complete proteome; Cytoplasm;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Nucleus;
KW   Polymorphism; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22   4588       Protocadherin Fat 1.
FT                                /FTId=PRO_0000004017.
FT   CHAIN         ?   4588       Protocadherin Fat 1, nuclear form.
FT                                /FTId=PRO_0000408559.
FT   TOPO_DOM     22   4181       Extracellular. {ECO:0000255}.
FT   TRANSMEM   4182   4202       Helical. {ECO:0000255}.
FT   TOPO_DOM   4203   4588       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       35    149       Cadherin 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      150    257       Cadherin 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      368    463       Cadherin 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      464    569       Cadherin 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      570    673       Cadherin 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      718    822       Cadherin 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      823    927       Cadherin 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      928   1034       Cadherin 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1035   1139       Cadherin 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1140   1245       Cadherin 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1246   1357       Cadherin 11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1359   1456       Cadherin 12. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1457   1562       Cadherin 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1563   1667       Cadherin 14. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1668   1765       Cadherin 15. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1766   1879       Cadherin 16. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1880   1979       Cadherin 17. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1980   2081       Cadherin 18. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2082   2182       Cadherin 19. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2183   2283       Cadherin 20. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2284   2390       Cadherin 21. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2391   2492       Cadherin 22. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2493   2596       Cadherin 23. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2597   2703       Cadherin 24. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2704   2809       Cadherin 25. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2810   2918       Cadherin 26. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2919   3023       Cadherin 27. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     3024   3125       Cadherin 28. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     3126   3230       Cadherin 29. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     3231   3335       Cadherin 30. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     3336   3440       Cadherin 31. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     3441   3545       Cadherin 32. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     3546   3647       Cadherin 33. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     3790   3827       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     3829   4009       Laminin G-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     4013   4050       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     4052   4088       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     4089   4125       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     4127   4163       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   MOTIF      4204   4214       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOTIF      4378   4382       PTB-like motif. {ECO:0000250}.
FT   CARBOHYD     40     40       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    333    333       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    660    660       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    740    740       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    791    791       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    998    998       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1426   1426       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1551   1551       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1748   1748       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1864   1864       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1902   1902       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1940   1940       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1991   1991       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2325   2325       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2464   2464       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3324   3324       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3422   3422       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   3444   3444       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3613   3613       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3640   3640       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3716   3716       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218,
FT                                ECO:0000269|PubMed:19349973}.
FT   CARBOHYD   4152   4152       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID   3794   3805       {ECO:0000250}.
FT   DISULFID   3799   3816       {ECO:0000250}.
FT   DISULFID   3818   3826       {ECO:0000250}.
FT   DISULFID   3976   4009       {ECO:0000250}.
FT   DISULFID   4017   4028       {ECO:0000250}.
FT   DISULFID   4022   4038       {ECO:0000250}.
FT   DISULFID   4040   4049       {ECO:0000250}.
FT   DISULFID   4056   4067       {ECO:0000250}.
FT   DISULFID   4061   4076       {ECO:0000250}.
FT   DISULFID   4078   4087       {ECO:0000250}.
FT   DISULFID   4093   4104       {ECO:0000250}.
FT   DISULFID   4098   4113       {ECO:0000250}.
FT   DISULFID   4115   4124       {ECO:0000250}.
FT   DISULFID   4131   4142       {ECO:0000250}.
FT   DISULFID   4136   4151       {ECO:0000250}.
FT   DISULFID   4153   4162       {ECO:0000250}.
FT   VARIANT     131    131       A -> V (in dbSNP:rs3733415).
FT                                /FTId=VAR_055590.
FT   VARIANT     546    546       P -> L (found in a patient with
FT                                spinocerebellar ataxia; unknown
FT                                pathological significance;
FT                                dbSNP:rs1373737710).
FT                                {ECO:0000269|PubMed:29053796}.
FT                                /FTId=VAR_080732.
FT   VARIANT     902    902       R -> S (in dbSNP:rs555992573).
FT                                {ECO:0000269|PubMed:26566883}.
FT                                /FTId=VAR_076441.
FT   VARIANT    1147   1147       E -> D (found in a patient with
FT                                spinocerebellar ataxia; unknown
FT                                pathological significance;
FT                                dbSNP:rs1383300308).
FT                                {ECO:0000269|PubMed:29053796}.
FT                                /FTId=VAR_080733.
FT   VARIANT    1330   1330       N -> S (in dbSNP:rs874111).
FT                                /FTId=VAR_055591.
FT   VARIANT    1393   1393       I -> V (in dbSNP:rs753226094).
FT                                {ECO:0000269|PubMed:26566883}.
FT                                /FTId=VAR_076442.
FT   VARIANT    1564   1564       A -> T (in dbSNP:rs2304867).
FT                                /FTId=VAR_055592.
FT   VARIANT    1605   1605       N -> D (in dbSNP:rs6836935).
FT                                /FTId=VAR_055593.
FT   VARIANT    1930   1930       D -> H (found in a patient with
FT                                spinocerebellar ataxia; unknown
FT                                pathological significance;
FT                                dbSNP:rs748622474).
FT                                {ECO:0000269|PubMed:29053796}.
FT                                /FTId=VAR_080734.
FT   VARIANT    3732   3732       N -> S (in dbSNP:rs373241719).
FT                                {ECO:0000269|PubMed:26566883}.
FT                                /FTId=VAR_076443.
FT   VARIANT    3800   3800       P -> H (in dbSNP:rs11731738).
FT                                /FTId=VAR_055594.
FT   VARIANT    4422   4422       T -> M (found in a patient with
FT                                spinocerebellar ataxia; unknown
FT                                pathological significance;
FT                                dbSNP:rs1409256573).
FT                                {ECO:0000269|PubMed:29053796}.
FT                                /FTId=VAR_080735.
FT   CONFLICT    322    322       G -> D (in Ref. 1; CAA60685).
FT                                {ECO:0000305}.
FT   CONFLICT    404    404       S -> R (in Ref. 1; CAA60685).
FT                                {ECO:0000305}.
FT   CONFLICT    482    482       V -> I (in Ref. 1; CAA60685).
FT                                {ECO:0000305}.
FT   CONFLICT    614    614       F -> L (in Ref. 1; CAA60685).
FT                                {ECO:0000305}.
FT   CONFLICT    862    862       V -> L (in Ref. 1; CAA60685).
FT                                {ECO:0000305}.
FT   CONFLICT   1064   1064       R -> G (in Ref. 1; CAA60685).
FT                                {ECO:0000305}.
FT   CONFLICT   1273   1273       H -> R (in Ref. 1; CAA60685).
FT                                {ECO:0000305}.
FT   CONFLICT   1351   1351       P -> Q (in Ref. 1; CAA60685).
FT                                {ECO:0000305}.
FT   CONFLICT   1526   1529       HQHT -> SPAH (in Ref. 1; CAA60685).
FT                                {ECO:0000305}.
FT   CONFLICT   1604   1604       G -> GNIG (in Ref. 1; CAA60685).
FT                                {ECO:0000305}.
FT   CONFLICT   2006   2006       N -> S (in Ref. 1; CAA60685).
FT                                {ECO:0000305}.
FT   CONFLICT   2054   2054       T -> I (in Ref. 1; CAA60685).
FT                                {ECO:0000305}.
FT   CONFLICT   2385   2385       D -> G (in Ref. 1; CAA60685).
FT                                {ECO:0000305}.
FT   CONFLICT   2618   2619       VL -> S (in Ref. 1; CAA60685).
FT                                {ECO:0000305}.
FT   CONFLICT   2718   2718       I -> V (in Ref. 1; CAA60685).
FT                                {ECO:0000305}.
FT   CONFLICT   3113   3113       L -> V (in Ref. 1; CAA60685).
FT                                {ECO:0000305}.
FT   CONFLICT   4059   4059       K -> N (in Ref. 1; CAA60685).
FT                                {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
//
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