CELR3_HUMAN
ID CELR3_HUMAN Reviewed; 3312 AA.
AC Q9NYQ7; O75092;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Cadherin EGF LAG seven-pass G-type receptor 3;
DE AltName: Full=Cadherin family member 11;
DE AltName: Full=Epidermal growth factor-like protein 1;
DE Short=EGF-like protein 1;
DE AltName: Full=Flamingo homolog 1;
DE Short=hFmi1;
DE AltName: Full=Multiple epidermal growth factor-like domains protein 2;
DE Short=Multiple EGF-like domains protein 2;
DE Flags: Precursor;
GN Name=CELSR3; Synonyms=CDHF11, EGFL1, FMI1, KIAA0812, MEGF2;
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] (ISOFORM 1).
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1954-3312 (ISOFORM 2).
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP VARIANT ILE-2630.
RX PubMed=23339110; DOI=10.1136/jmedgenet-2012-101223;
RA Edvardson S., Oz S., Abulhijaa F.A., Taher F.B., Shaag A., Zenvirt S.,
RA Dascal N., Elpeleg O.;
RT "Early infantile epileptic encephalopathy associated with a high voltage
RT gated calcium channelopathy.";
RL J. Med. Genet. 50:118-123(2013).
RN [6]
RP VARIANT ASP-2136.
RX PubMed=24358150; DOI=10.1371/journal.pone.0082154;
RA Pippucci T., Parmeggiani A., Palombo F., Maresca A., Angius A.,
RA Crisponi L., Cucca F., Liguori R., Valentino M.L., Seri M., Carelli V.;
RT "A novel null homozygous mutation confirms CACNA2D2 as a gene mutated in
RT epileptic encephalopathy.";
RL PLoS ONE 8:E82154-E82154(2013).
RN [7]
RP VARIANT ARG-1758.
RX PubMed=30410802; DOI=10.1155/2018/6308283;
RA Butler K.M., Holt P.J., Milla S.S., da Silva C., Alexander J.J., Escayg A.;
RT "Epileptic encephalopathy and cerebellar atrophy resulting from compound
RT heterozygous CACNA2D2 variants.";
RL Case Rep. Genet. 2018:6308283-6308283(2018).
CC -!- FUNCTION: Receptor that may have an important role in cell/cell
CC signaling during nervous system formation.
CC -!- INTERACTION:
CC Q9NYQ7; P16333: NCK1; NbExp=2; IntAct=EBI-308417, EBI-389883;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NYQ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NYQ7-2; Sequence=VSP_037125;
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000305}.
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DR EMBL; AF231023; AAF61929.1; -; mRNA.
DR EMBL; AC121252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB011536; BAA32464.1; -; mRNA.
DR CCDS; CCDS2775.1; -. [Q9NYQ7-1]
DR PIR; T00250; T00250.
DR RefSeq; NP_001398.2; NM_001407.2. [Q9NYQ7-1]
DR SMR; Q9NYQ7; -.
DR BioGRID; 108271; 33.
DR IntAct; Q9NYQ7; 32.
DR MINT; Q9NYQ7; -.
DR STRING; 9606.ENSP00000164024; -.
DR GlyGen; Q9NYQ7; 16 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NYQ7; -.
DR PhosphoSitePlus; Q9NYQ7; -.
DR BioMuta; CELSR3; -.
DR DMDM; 229462826; -.
DR EPD; Q9NYQ7; -.
DR jPOST; Q9NYQ7; -.
DR MassIVE; Q9NYQ7; -.
DR MaxQB; Q9NYQ7; -.
DR PaxDb; Q9NYQ7; -.
DR PeptideAtlas; Q9NYQ7; -.
DR PRIDE; Q9NYQ7; -.
DR ProteomicsDB; 83265; -. [Q9NYQ7-1]
DR ProteomicsDB; 83266; -. [Q9NYQ7-2]
DR Antibodypedia; 13269; 319 antibodies from 33 providers.
DR DNASU; 1951; -.
DR Ensembl; ENST00000164024.5; ENSP00000164024.4; ENSG00000008300.17. [Q9NYQ7-1]
DR GeneID; 1951; -.
DR KEGG; hsa:1951; -.
DR MANE-Select; ENST00000164024.5; ENSP00000164024.4; NM_001407.3; NP_001398.2.
DR UCSC; uc003cul.4; human. [Q9NYQ7-1]
DR CTD; 1951; -.
DR DisGeNET; 1951; -.
DR GeneCards; CELSR3; -.
DR HGNC; HGNC:3230; CELSR3.
DR HPA; ENSG00000008300; Tissue enhanced (brain, pituitary gland, retina).
DR MIM; 604264; gene.
DR neXtProt; NX_Q9NYQ7; -.
DR OpenTargets; ENSG00000008300; -.
DR PharmGKB; PA26395; -.
DR VEuPathDB; HostDB:ENSG00000008300; -.
DR eggNOG; KOG4289; Eukaryota.
DR GeneTree; ENSGT00940000160077; -.
DR HOGENOM; CLU_000158_1_0_1; -.
DR InParanoid; Q9NYQ7; -.
DR OMA; WGSPSCG; -.
DR OrthoDB; 23882at2759; -.
DR PhylomeDB; Q9NYQ7; -.
DR TreeFam; TF323983; -.
DR PathwayCommons; Q9NYQ7; -.
DR SignaLink; Q9NYQ7; -.
DR BioGRID-ORCS; 1951; 17 hits in 1073 CRISPR screens.
DR ChiTaRS; CELSR3; human.
DR GeneWiki; CELSR3; -.
DR GenomeRNAi; 1951; -.
DR Pharos; Q9NYQ7; Tbio.
DR PRO; PR:Q9NYQ7; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9NYQ7; protein.
DR Bgee; ENSG00000008300; Expressed in right hemisphere of cerebellum and 144 other tissues.
DR Genevisible; Q9NYQ7; HS.
DR GO; GO:0016021; C:integral component of membrane; TAS:GDB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:GDB.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:GDB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; NAS:ParkinsonsUK-UCL.
DR CDD; cd00055; EGF_Lam; 2.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 4.10.1240.10; -; 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; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF00028; Cadherin; 8.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF00053; Laminin_EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00112; CA; 9.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 5.
DR SMART; SM00180; EGF_Lam; 1.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49313; SSF49313; 9.
DR SUPFAM; SSF49899; SSF49899; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00232; CADHERIN_1; 7.
DR PROSITE; PS50268; CADHERIN_2; 8.
DR PROSITE; PS00022; EGF_1; 6.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 6.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Developmental protein;
KW Disulfide bond; EGF-like domain; G-protein coupled receptor; Glycoprotein;
KW Hydroxylation; Laminin EGF-like domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..3312
FT /note="Cadherin EGF LAG seven-pass G-type receptor 3"
FT /id="PRO_0000012918"
FT TOPO_DOM 33..2540
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2541..2561
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2562..2572
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2573..2593
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2594..2601
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2602..2622
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2623..2643
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2644..2664
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2665..2681
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2682..2702
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2703..2725
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2726..2746
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2747..2753
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2754..2774
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2775..3312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 326..433
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 434..545
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 546..651
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 652..756
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 757..858
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 859..961
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 962..1067
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1068..1169
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1170..1265
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1375..1433
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1435..1471
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1475..1514
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1515..1719
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1722..1758
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1764..1944
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1946..1982
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1983..2020
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2021..2053
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2055..2090
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2077..2124
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2477..2529
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 90..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2361..2399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2888..2927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2978..3006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3086..3243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3256..3312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2366..2391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2979..3000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3109..3123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3162..3177
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3191..3206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3256..3302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1963
FT /note="(3R)-3-hydroxyaspartate"
FT /evidence="ECO:0000255"
FT MOD_RES 2126
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O88278"
FT MOD_RES 3051
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O88278"
FT MOD_RES 3097
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88278"
FT CARBOHYD 632
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 847
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1649
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1713
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1770
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2053
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1379..1390
FT /evidence="ECO:0000250"
FT DISULFID 1384..1421
FT /evidence="ECO:0000250"
FT DISULFID 1423..1432
FT /evidence="ECO:0000250"
FT DISULFID 1439..1450
FT /evidence="ECO:0000250"
FT DISULFID 1444..1459
FT /evidence="ECO:0000250"
FT DISULFID 1461..1470
FT /evidence="ECO:0000250"
FT DISULFID 1479..1490
FT /evidence="ECO:0000250"
FT DISULFID 1484..1500
FT /evidence="ECO:0000250"
FT DISULFID 1502..1513
FT /evidence="ECO:0000250"
FT DISULFID 1693..1719
FT /evidence="ECO:0000250"
FT DISULFID 1726..1737
FT /evidence="ECO:0000250"
FT DISULFID 1731..1746
FT /evidence="ECO:0000250"
FT DISULFID 1748..1757
FT /evidence="ECO:0000250"
FT DISULFID 1915..1944
FT /evidence="ECO:0000250"
FT DISULFID 1950..1961
FT /evidence="ECO:0000250"
FT DISULFID 1955..1970
FT /evidence="ECO:0000250"
FT DISULFID 1972..1981
FT /evidence="ECO:0000250"
FT DISULFID 1985..1996
FT /evidence="ECO:0000250"
FT DISULFID 1990..2008
FT /evidence="ECO:0000250"
FT DISULFID 2010..2019
FT /evidence="ECO:0000250"
FT DISULFID 2027..2040
FT /evidence="ECO:0000250"
FT DISULFID 2042..2052
FT /evidence="ECO:0000250"
FT DISULFID 2059..2074
FT /evidence="ECO:0000250"
FT DISULFID 2061..2077
FT /evidence="ECO:0000250"
FT DISULFID 2079..2089
FT /evidence="ECO:0000250"
FT DISULFID 2098..2107
FT /evidence="ECO:0000250"
FT DISULFID 2110..2122
FT /evidence="ECO:0000250"
FT VAR_SEQ 2158
FT /note="G -> GLRGAG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9693030"
FT /id="VSP_037125"
FT VARIANT 157
FT /note="A -> P (in dbSNP:rs3733085)"
FT /id="VAR_020022"
FT VARIANT 805
FT /note="S -> T (in dbSNP:rs3821875)"
FT /id="VAR_020023"
FT VARIANT 1758
FT /note="Q -> R (in dbSNP:rs12107252)"
FT /evidence="ECO:0000269|PubMed:30410802"
FT /id="VAR_055101"
FT VARIANT 2136
FT /note="G -> D (found in a patient with epileptic
FT encephalopathy; unknown pathological significance;
FT dbSNP:rs587777163)"
FT /evidence="ECO:0000269|PubMed:24358150"
FT /id="VAR_083108"
FT VARIANT 2630
FT /note="M -> I (in dbSNP:rs149614835)"
FT /evidence="ECO:0000269|PubMed:23339110"
FT /id="VAR_083109"
FT CONFLICT 13
FT /note="G -> E (in Ref. 1; AAF61929)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3312 AA; 358185 MW; 9E6B37787A9F0348 CRC64;
MMARRPPWRG LGGRSTPILL LLLLSLFPLS QEELGGGGHQ GWDPGLAATT GPRAHIGGGA
LALCPESSGV REDGGPGLGV REPIFVGLRG RRQSARNSRG PPEQPNEELG IEHGVQPLGS
RERETGQGPG SVLYWRPEVS SCGRTGPLQR GSLSPGALSS GVPGSGNSSP LPSDFLIRHH
GPKPVSSQRN AGTGSRKRVG TARCCGELWA TGSKGQGERA TTSGAERTAP RRNCLPGASG
SGPELDSAPR TARTAPASGS APRESRTAPE PAPKRMRSRG LFRCRFLPQR PGPRPPGLPA
RPEARKVTSA NRARFRRAAN RHPQFPQYNY QTLVPENEAA GTAVLRVVAQ DPDAGEAGRL
VYSLAALMNS RSLELFSIDP QSGLIRTAAA LDRESMERHY LRVTAQDHGS PRLSATTMVA
VTVADRNDHS PVFEQAQYRE TLRENVEEGY PILQLRATDG DAPPNANLRY RFVGPPAARA
AAAAAFEIDP RSGLISTSGR VDREHMESYE LVVEASDQGQ EPGPRSATVR VHITVLDEND
NAPQFSEKRY VAQVREDVRP HTVVLRVTAT DRDKDANGLV HYNIISGNSR GHFAIDSLTG
EIQVVAPLDF EAEREYALRI RAQDAGRPPL SNNTGLASIQ VVDINDHIPI FVSTPFQVSV
LENAPLGHSV IHIQAVDADH GENARLEYSL TGVAPDTPFV INSATGWVSV SGPLDRESVE
HYFFGVEARD HGSPPLSASA SVTVTVLDVN DNRPEFTMKE YHLRLNEDAA VGTSVVSVTA
VDRDANSAIS YQITGGNTRN RFAISTQGGV GLVTLALPLD YKQERYFKLV LTASDRALHD
HCYVHINITD ANTHRPVFQS AHYSVSVNED RPMGSTIVVI SASDDDVGEN ARITYLLEDN
LPQFRIDADS GAITLQAPLD YEDQVTYTLA ITARDNGIPQ KADTTYVEVM VNDVNDNAPQ
FVASHYTGLV SEDAPPFTSV LQISATDRDA HANGRVQYTF QNGEDGDGDF TIEPTSGIVR
TVRRLDREAV SVYELTAYAV DRGVPPLRTP VSIQVMVQDV NDNAPVFPAE EFEVRVKENS
IVGSVVAQIT AVDPDEGPNA HIMYQIVEGN IPELFQMDIF SGELTALIDL DYEARQEYVI
VVQATSAPLV SRATVHVRLV DQNDNSPVLN NFQILFNNYV SNRSDTFPSG IIGRIPAYDP
DVSDHLFYSF ERGNELQLLV VNQTSGELRL SRKLDNNRPL VASMLVTVTD GLHSVTAQCV
LRVVIITEEL LANSLTVRLE NMWQERFLSP LLGRFLEGVA AVLATPAEDV FIFNIQNDTD
VGGTVLNVSF SALAPRGAGA GAAGPWFSSE ELQEQLYVRR AALAARSLLD VLPFDDNVCL
REPCENYMKC VSVLRFDSSA PFLASASTLF RPIQPIAGLR CRCPPGFTGD FCETELDLCY
SNPCRNGGAC ARREGGYTCV CRPRFTGEDC ELDTEAGRCV PGVCRNGGTC TDAPNGGFRC
QCPAGGAFEG PRCEVAARSF PPSSFVMFRG LRQRFHLTLS LSFATVQQSG LLFYNGRLNE
KHDFLALELV AGQVRLTYST GESNTVVSPT VPGGLSDGQW HTVHLRYYNK PRTDALGGAQ
GPSKDKVAVL SVDDCDVAVA LQFGAEIGNY SCAAAGVQTS SKKSLDLTGP LLLGGVPNLP
ENFPVSHKDF IGCMRDLHID GRRVDMAAFV ANNGTMAGCQ AKLHFCDSGP CKNSGFCSER
WGSFSCDCPV GFGGKDCQLT MAHPHHFRGN GTLSWNFGSD MAVSVPWYLG LAFRTRATQG
VLMQVQAGPH STLLCQLDRG LLSVTVTRGS GRASHLLLDQ VTVSDGRWHD LRLELQEEPG
GRRGHHVLMV SLDFSLFQDT MAVGSELQGL KVKQLHVGGL PPGSAEEAPQ GLVGCIQGVW
LGSTPSGSPA LLPPSHRVNA EPGCVVTNAC ASGPCPPHAD CRDLWQTFSC TCQPGYYGPG
CVDACLLNPC QNQGSCRHLP GAPHGYTCDC VGGYFGHHCE HRMDQQCPRG WWGSPTCGPC
NCDVHKGFDP NCNKTNGQCH CKEFHYRPRG SDSCLPCDCY PVGSTSRSCA PHSGQCPCRP
GALGRQCNSC DSPFAEVTAS GCRVLYDACP KSLRSGVWWP QTKFGVLATV PCPRGALGAA
VRLCDEAQGW LEPDLFNCTS PAFRELSLLL DGLELNKTAL DTMEAKKLAQ RLREVTGHTD
HYFSQDVRVT ARLLAHLLAF ESHQQGFGLT ATQDAHFNEN LLWAGSALLA PETGDLWAAL
GQRAPGGSPG SAGLVRHLEE YAATLARNME LTYLNPMGLV TPNIMLSIDR MEHPSSPRGA
RRYPRYHSNL FRGQDAWDPH THVLLPSQSP RPSPSEVLPT SSSIENSTTS SVVPPPAPPE
PEPGISIIIL LVYRTLGGLL PAQFQAERRG ARLPQNPVMN SPVVSVAVFH GRNFLRGILE
SPISLEFRLL QTANRSKAIC VQWDPPGLAE QHGVWTARDC ELVHRNGSHA RCRCSRTGTF
GVLMDASPRE RLEGDLELLA VFTHVVVAVS VAALVLTAAI LLSLRSLKSN VRGIHANVAA
ALGVAELLFL LGIHRTHNQL VCTAVAILLH YFFLSTFAWL FVQGLHLYRM QVEPRNVDRG
AMRFYHALGW GVPAVLLGLA VGLDPEGYGN PDFCWISVHE PLIWSFAGPV VLVIVMNGTM
FLLAARTSCS TGQREAKKTS ALTLRSSFLL LLLVSASWLF GLLAVNHSIL AFHYLHAGLC
GLQGLAVLLL FCVLNADARA AWMPACLGRK AAPEEARPAP GLGPGAYNNT ALFEESGLIR
ITLGASTVSS VSSARSGRTQ DQDSQRGRSY LRDNVLVRHG SAADHTDHSL QAHAGPTDLD
VAMFHRDAGA DSDSDSDLSL EEERSLSIPS SESEDNGRTR GRFQRPLCRA AQSERLLTHP
KDVDGNDLLS YWPALGECEA APCALQTWGS ERRLGLDTSK DAANNNQPDP ALTSGDETSL
GRAQRQRKGI LKNRLQYPLV PQTRGAPELS WCRAATLGHR AVPAASYGRI YAGGGTGSLS
QPASRYSSRE QLDLLLRRQL SRERLEEAPA PVLRPLSRPG SQECMDAAPG RLEPKDRGST
LPRRQPPRDY PGAMAGRFGS RDALDLGAPR EWLSTLPPPR RTRDLDPQPP PLPLSPQRQL
SRDPLLPSRP LDSLSRSSNS REQLDQVPSR HPSREALGPL PQLLRAREDS VSGPSHGPST
EQLDILSSIL ASFNSSALSS VQSSSTPLGP HTTATPSATA SVLGPSTPRS ATSHSISELS
PDSEVPRSEG HS
