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   27-MAR-2024, entry version 204.
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; 36.
DR   IntAct; Q9NYQ7; 31.
DR   MINT; Q9NYQ7; -.
DR   STRING; 9606.ENSP00000164024; -.
DR   GlyCosmos; Q9NYQ7; 16 sites, 1 glycan.
DR   GlyGen; Q9NYQ7; 18 sites, 1 O-linked glycan (3 sites).
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; 9606-ENSP00000164024; -.
DR   PeptideAtlas; Q9NYQ7; -.
DR   ProteomicsDB; 83265; -. [Q9NYQ7-1]
DR   ProteomicsDB; 83266; -. [Q9NYQ7-2]
DR   Antibodypedia; 13269; 350 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   AGR; HGNC:3230; -.
DR   CTD; 1951; -.
DR   DisGeNET; 1951; -.
DR   GeneCards; CELSR3; -.
DR   HGNC; HGNC:3230; CELSR3.
DR   HPA; ENSG00000008300; Tissue enhanced (brain, pituitary gland).
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; ECETRWG; -.
DR   OrthoDB; 4006628at2759; -.
DR   PhylomeDB; Q9NYQ7; -.
DR   TreeFam; TF323983; -.
DR   PathwayCommons; Q9NYQ7; -.
DR   SignaLink; Q9NYQ7; -.
DR   BioGRID-ORCS; 1951; 24 hits in 1153 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 146 other cell types or tissues.
DR   GO; GO:0016020; C: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:0036514; P:dopaminergic neuron axon guidance; ISS:ARUK-UCL.
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:0036515; P:serotonergic neuron axon guidance; ISS:ARUK-UCL.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; NAS:ParkinsonsUK-UCL.
DR   CDD; cd11304; Cadherin_repeat; 9.
DR   CDD; cd00054; EGF_CA; 5.
DR   CDD; cd00055; EGF_Lam; 2.
DR   CDD; cd00110; LamG; 2.
DR   Gene3D; 2.60.120.200; -; 2.
DR   Gene3D; 2.60.220.50; -; 1.
DR   Gene3D; 2.60.40.60; Cadherins; 9.
DR   Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR   Gene3D; 2.10.25.10; Laminin; 7.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 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_7TM.
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   PANTHER; PTHR24026:SF38; CADHERIN EGF LAG SEVEN-PASS G-TYPE RECEPTOR 3; 1.
DR   PANTHER; PTHR24026; FAT ATYPICAL CADHERIN-RELATED; 1.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF00028; Cadherin; 8.
DR   Pfam; PF00008; EGF; 3.
DR   Pfam; PF16489; GAIN; 1.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF02793; HRM; 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; Cadherin-like; 9.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF57196; EGF/Laminin; 4.
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.
DR   Genevisible; Q9NYQ7; HS.
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; uncertain significance; 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
//