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 05-FEB-2025, entry version 206. 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. 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; 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; 4. DR IntAct; Q9NYQ8; 1. DR STRING; 9606.ENSP00000261800; -. DR GlyCosmos; Q9NYQ8; 38 sites, No reported glycans. DR GlyGen; Q9NYQ8; 40 sites, 2 O-linked glycans (2 sites). DR iPTMnet; Q9NYQ8; -. DR PhosphoSitePlus; Q9NYQ8; -. DR BioMuta; FAT2; -. DR DMDM; 296434503; -. DR jPOST; Q9NYQ8; -. DR MassIVE; Q9NYQ8; -. DR PaxDb; 9606-ENSP00000261800; -. DR PeptideAtlas; Q9NYQ8; -. DR ProteomicsDB; 83267; -. DR Antibodypedia; 77918; 120 antibodies from 13 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 AGR; HGNC:3596; -. DR CTD; 2196; -. DR DisGeNET; 2196; -. DR GeneCards; FAT2; -. DR HGNC; HGNC:3596; FAT2. DR HPA; ENSG00000086570; Tissue enriched (brain). 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; QRRENCT; -. DR OrthoDB; 6252479at2759; -. DR PhylomeDB; Q9NYQ8; -. DR TreeFam; TF316403; -. DR PathwayCommons; Q9NYQ8; -. DR SignaLink; Q9NYQ8; -. DR BioGRID-ORCS; 2196; 11 hits in 1139 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 129 other cell types or tissues. DR ExpressionAtlas; Q9NYQ8; baseline and differential. 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: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; cd11304; Cadherin_repeat; 33. DR CDD; cd00054; EGF_CA; 2. DR CDD; cd00110; LamG; 1. DR FunFam; 2.60.40.60:FF:000116; Dachsous cadherin-related 2; 1. DR FunFam; 2.60.40.60:FF:000015; FAT atypical cadherin 1; 1. DR FunFam; 2.60.40.60:FF:000021; FAT atypical cadherin 1; 2. DR FunFam; 2.60.40.60:FF:000026; FAT atypical cadherin 1; 2. DR FunFam; 2.60.40.60:FF:000032; FAT atypical cadherin 1; 1. DR FunFam; 2.60.40.60:FF:000033; FAT atypical cadherin 1; 1. DR FunFam; 2.60.40.60:FF:000037; FAT atypical cadherin 1; 2. DR FunFam; 2.60.40.60:FF:000041; FAT atypical cadherin 1; 1. DR FunFam; 2.60.40.60:FF:000051; FAT atypical cadherin 1; 1. DR FunFam; 2.60.40.60:FF:000065; FAT atypical cadherin 1; 1. DR FunFam; 2.60.40.60:FF:000066; FAT atypical cadherin 1; 1. DR FunFam; 2.60.40.60:FF:000071; FAT atypical cadherin 1; 1. DR FunFam; 2.60.40.60:FF:000075; FAT atypical cadherin 1; 1. DR FunFam; 2.60.40.60:FF:000079; FAT atypical cadherin 1; 1. DR FunFam; 2.60.40.60:FF:000080; FAT atypical cadherin 1; 1. DR FunFam; 2.60.40.60:FF:000089; FAT atypical cadherin 1; 1. DR FunFam; 2.60.120.200:FF:000139; FAT atypical cadherin 2; 1. DR FunFam; 2.60.40.60:FF:000186; FAT atypical cadherin 2; 1. DR FunFam; 2.60.40.60:FF:000194; FAT atypical cadherin 2; 1. DR FunFam; 2.60.40.60:FF:000197; FAT atypical cadherin 2; 1. DR FunFam; 2.60.40.60:FF:000207; FAT atypical cadherin 2; 1. DR FunFam; 2.60.40.60:FF:000210; FAT atypical cadherin 2; 1. DR FunFam; 2.60.40.60:FF:000215; FAT atypical cadherin 2; 1. DR FunFam; 2.60.40.60:FF:000024; FAT atypical cadherin 3; 1. DR FunFam; 2.60.40.60:FF:000039; FAT atypical cadherin 3; 1. DR FunFam; 2.60.40.60:FF:000053; FAT atypical cadherin 3; 1. DR FunFam; 2.60.40.60:FF:000058; FAT atypical cadherin 3; 1. DR FunFam; 2.60.40.60:FF:000059; FAT atypical cadherin 3; 1. DR FunFam; 2.60.40.60:FF:000061; FAT atypical cadherin 3; 1. DR FunFam; 2.10.25.10:FF:000057; protocadherin Fat 1 isoform X2; 2. DR FunFam; 2.60.40.60:FF:000178; Protocadherin Fat 2; 1. DR FunFam; 2.60.40.60:FF:000198; Protocadherin Fat 2; 1. DR Gene3D; 2.60.120.200; -; 1. DR Gene3D; 2.60.40.60; Cadherins; 33. DR Gene3D; 2.10.25.10; Laminin; 2. 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; IPR001791; Laminin_G. DR PANTHER; PTHR24027:SF438; CADHERIN 23; 1. DR PANTHER; PTHR24027; CADHERIN-23; 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; 33. DR SMART; SM00181; EGF; 2. DR SMART; SM00179; EGF_CA; 2. 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; 2. 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; Proteomics identification; Reference proteome; Repeat; KW Signal; 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; uncertain 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; uncertain 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 //