ID   CELR1_HUMAN             Reviewed;        3014 AA.
AC   Q9NYQ6; O95722; Q5TH47; Q9BWQ5; Q9Y506; Q9Y526;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   29-SEP-2021, entry version 201.
DE   RecName: Full=Cadherin EGF LAG seven-pass G-type receptor 1;
DE   AltName: Full=Cadherin family member 9;
DE   AltName: Full=Flamingo homolog 2;
DE            Short=hFmi2;
DE   Flags: Precursor;
GN   Name=CELSR1; Synonyms=CDHF9, FMI2;
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=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 627-3014 (ISOFORM 2), AND
RP   VARIANTS TRP-664 AND ARG-1126.
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2764, AND IDENTIFICATION BY
RP   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   VARIANTS NTD VAL-773; GLN-2438; LEU-2964 AND ALA-2983, VARIANTS PRO-2312
RP   AND THR-2739, CHARACTERIZATION OF VARIANTS NTD VAL-773; GLN-2438; LEU-2964
RP   AND ALA-2983, AND CHARACTERIZATION OF VARIANTS PRO-2312 AND THR-2739.
RX   PubMed=22095531; DOI=10.1002/humu.21662;
RA   Robinson A., Escuin S., Doudney K., Vekemans M., Stevenson R.E.,
RA   Greene N.D., Copp A.J., Stanier P.;
RT   "Mutations in the planar cell polarity genes CELSR1 and SCRIB are
RT   associated with the severe neural tube defect craniorachischisis.";
RL   Hum. Mutat. 33:440-447(2012).
CC   -!- FUNCTION: Receptor that may have an important role in cell/cell
CC       signaling during nervous system formation.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NYQ6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NYQ6-2; Sequence=VSP_002011, VSP_002012;
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC       and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
CC   -!- DISEASE: Neural tube defects (NTD) [MIM:182940]: Congenital
CC       malformations of the central nervous system and adjacent structures
CC       related to defective neural tube closure during the first trimester of
CC       pregnancy. Failure of neural tube closure can occur at any level of the
CC       embryonic axis. Common NTD forms include anencephaly, myelomeningocele
CC       and spina bifida, which result from the failure of fusion in the
CC       cranial and spinal region of the neural tube. NTDs have a
CC       multifactorial etiology encompassing both genetic and environmental
CC       components. {ECO:0000269|PubMed:22095531}. Note=The disease may be
CC       caused by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF231024; AAF61930.1; -; mRNA.
DR   EMBL; AL021392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL031588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL031597; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC000059; AAH00059.2; -; mRNA.
DR   CCDS; CCDS14076.1; -. [Q9NYQ6-1]
DR   RefSeq; NP_055061.1; NM_014246.1. [Q9NYQ6-1]
DR   SMR; Q9NYQ6; -.
DR   BioGRID; 114981; 29.
DR   IntAct; Q9NYQ6; 15.
DR   STRING; 9606.ENSP00000262738; -.
DR   TCDB; 9.A.14.6.4; the g-protein-coupled receptor (gpcr) family.
DR   GlyConnect; 1054; 7 N-Linked glycans (7 sites).
DR   GlyGen; Q9NYQ6; 23 sites, 6 N-linked glycans (6 sites), 3 O-linked glycans (2 sites).
DR   iPTMnet; Q9NYQ6; -.
DR   PhosphoSitePlus; Q9NYQ6; -.
DR   BioMuta; CELSR1; -.
DR   DMDM; 22095551; -.
DR   CPTAC; CPTAC-1482; -.
DR   EPD; Q9NYQ6; -.
DR   jPOST; Q9NYQ6; -.
DR   MassIVE; Q9NYQ6; -.
DR   MaxQB; Q9NYQ6; -.
DR   PaxDb; Q9NYQ6; -.
DR   PeptideAtlas; Q9NYQ6; -.
DR   PRIDE; Q9NYQ6; -.
DR   ProteomicsDB; 83263; -. [Q9NYQ6-1]
DR   ProteomicsDB; 83264; -. [Q9NYQ6-2]
DR   Antibodypedia; 13897; 186 antibodies.
DR   DNASU; 9620; -.
DR   Ensembl; ENST00000262738; ENSP00000262738; ENSG00000075275. [Q9NYQ6-1]
DR   Ensembl; ENST00000454637; ENSP00000414689; ENSG00000075275. [Q9NYQ6-2]
DR   GeneID; 9620; -.
DR   KEGG; hsa:9620; -.
DR   UCSC; uc003bhw.1; human. [Q9NYQ6-1]
DR   CTD; 9620; -.
DR   DisGeNET; 9620; -.
DR   GeneCards; CELSR1; -.
DR   HGNC; HGNC:1850; CELSR1.
DR   HPA; ENSG00000075275; Low tissue specificity.
DR   MalaCards; CELSR1; -.
DR   MIM; 182940; phenotype.
DR   MIM; 604523; gene.
DR   neXtProt; NX_Q9NYQ6; -.
DR   OpenTargets; ENSG00000075275; -.
DR   PharmGKB; PA26393; -.
DR   VEuPathDB; HostDB:ENSG00000075275; -.
DR   eggNOG; KOG4289; Eukaryota.
DR   GeneTree; ENSGT00940000159839; -.
DR   HOGENOM; CLU_000158_1_0_1; -.
DR   InParanoid; Q9NYQ6; -.
DR   OrthoDB; 23882at2759; -.
DR   PhylomeDB; Q9NYQ6; -.
DR   TreeFam; TF323983; -.
DR   PathwayCommons; Q9NYQ6; -.
DR   BioGRID-ORCS; 9620; 7 hits in 1013 CRISPR screens.
DR   ChiTaRS; CELSR1; human.
DR   GeneWiki; CELSR1; -.
DR   GenomeRNAi; 9620; -.
DR   Pharos; Q9NYQ6; Tbio.
DR   PRO; PR:Q9NYQ6; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; Q9NYQ6; protein.
DR   Bgee; ENSG00000075275; Expressed in ventricular zone and 173 other tissues.
DR   ExpressionAtlas; Q9NYQ6; baseline and differential.
DR   Genevisible; Q9NYQ6; HS.
DR   GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0045176; P:apical protein localization; ISS:UniProtKB.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0007417; P:central nervous system development; TAS:UniProtKB.
DR   GO; GO:0048105; P:establishment of body hair planar orientation; ISS:UniProtKB.
DR   GO; GO:0001736; P:establishment of planar polarity; ISS:UniProtKB.
DR   GO; GO:0042249; P:establishment of planar polarity of embryonic epithelium; ISS:UniProtKB.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   GO; GO:0060490; P:lateral sprouting involved in lung morphogenesis; ISS:UniProtKB.
DR   GO; GO:0001843; P:neural tube closure; ISS:UniProtKB.
DR   GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR   GO; GO:0060488; P:orthogonal dichotomous subdivision of terminal units involved in lung branching morphogenesis; ISS:UniProtKB.
DR   GO; GO:0060489; P:planar dichotomous subdivision of terminal units involved in lung branching morphogenesis; ISS:UniProtKB.
DR   GO; GO:0090251; P:protein localization involved in establishment of planar polarity; ISS:UniProtKB.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0007266; P:Rho protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; NAS:ParkinsonsUK-UCL.
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; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR032471; GAIN_dom_N.
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; IPR000203; GPS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR002049; Laminin_EGF.
DR   InterPro; IPR001791; Laminin_G.
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; 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; 4.
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   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS00232; CADHERIN_1; 7.
DR   PROSITE; PS50268; CADHERIN_2; 9.
DR   PROSITE; PS00022; EGF_1; 6.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 6.
DR   PROSITE; PS01248; EGF_LAM_1; 1.
DR   PROSITE; PS50027; EGF_LAM_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   Disease variant; Disulfide bond; EGF-like domain;
KW   G-protein coupled receptor; Glycoprotein; Hydroxylation;
KW   Laminin EGF-like domain; Membrane; Phosphoprotein; Receptor;
KW   Reference proteome; Repeat; Signal; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..3014
FT                   /note="Cadherin EGF LAG seven-pass G-type receptor 1"
FT                   /id="PRO_0000012914"
FT   TOPO_DOM        22..2469
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2470..2490
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2491..2501
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2502..2522
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2523..2527
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2528..2548
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2549..2572
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2573..2593
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2594..2611
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2612..2632
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2633..2655
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2656..2676
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2677..2683
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2684..2704
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2705..3014
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          246..353
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          354..459
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          460..565
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          566..687
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          688..789
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          790..892
FT                   /note="Cadherin 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          893..999
FT                   /note="Cadherin 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          1000..1101
FT                   /note="Cadherin 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          1106..1224
FT                   /note="Cadherin 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          1303..1361
FT                   /note="EGF-like 1; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1363..1399
FT                   /note="EGF-like 2; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1403..1441
FT                   /note="EGF-like 3; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1442..1646
FT                   /note="Laminin G-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          1649..1685
FT                   /note="EGF-like 4; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1689..1870
FT                   /note="Laminin G-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          1872..1907
FT                   /note="EGF-like 5; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1908..1946
FT                   /note="EGF-like 6; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1947..1979
FT                   /note="EGF-like 7; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1981..2016
FT                   /note="EGF-like 8; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          2003..2050
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          2408..2460
FT                   /note="GPS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT   REGION          204..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2291..2328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2777..2939
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2954..3014
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..224
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2812..2828
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2829..2844
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2872..2903
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2959..2973
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1666
FT                   /note="(3R)-3-hydroxyasparagine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1889
FT                   /note="(3R)-3-hydroxyaspartate"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2761
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O35161"
FT   MOD_RES         2764
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         2871
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O35161"
FT   MOD_RES         2873
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O35161"
FT   CARBOHYD        403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        546
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        634
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        778
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1213
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1249
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1576
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1623
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1640
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1979
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2415
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2437
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2523
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        1307..1318
FT                   /evidence="ECO:0000250"
FT   DISULFID        1312..1349
FT                   /evidence="ECO:0000250"
FT   DISULFID        1351..1360
FT                   /evidence="ECO:0000250"
FT   DISULFID        1367..1378
FT                   /evidence="ECO:0000250"
FT   DISULFID        1372..1387
FT                   /evidence="ECO:0000250"
FT   DISULFID        1389..1398
FT                   /evidence="ECO:0000250"
FT   DISULFID        1407..1418
FT                   /evidence="ECO:0000250"
FT   DISULFID        1412..1428
FT                   /evidence="ECO:0000250"
FT   DISULFID        1430..1440
FT                   /evidence="ECO:0000250"
FT   DISULFID        1620..1646
FT                   /evidence="ECO:0000250"
FT   DISULFID        1653..1664
FT                   /evidence="ECO:0000250"
FT   DISULFID        1658..1673
FT                   /evidence="ECO:0000250"
FT   DISULFID        1675..1684
FT                   /evidence="ECO:0000250"
FT   DISULFID        1840..1870
FT                   /evidence="ECO:0000250"
FT   DISULFID        1876..1887
FT                   /evidence="ECO:0000250"
FT   DISULFID        1881..1896
FT                   /evidence="ECO:0000250"
FT   DISULFID        1898..1907
FT                   /evidence="ECO:0000250"
FT   DISULFID        1911..1922
FT                   /evidence="ECO:0000250"
FT   DISULFID        1916..1934
FT                   /evidence="ECO:0000250"
FT   DISULFID        1936..1945
FT                   /evidence="ECO:0000250"
FT   DISULFID        1953..1966
FT                   /evidence="ECO:0000250"
FT   DISULFID        1968..1978
FT                   /evidence="ECO:0000250"
FT   DISULFID        1985..2000
FT                   /evidence="ECO:0000250"
FT   DISULFID        1987..2003
FT                   /evidence="ECO:0000250"
FT   DISULFID        2005..2015
FT                   /evidence="ECO:0000250"
FT   DISULFID        2024..2033
FT                   /evidence="ECO:0000250"
FT   DISULFID        2036..2048
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1395..1397
FT                   /note="GEH -> EIS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_002011"
FT   VAR_SEQ         1398..3014
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_002012"
FT   VARIANT         587
FT                   /note="I -> V (in dbSNP:rs34141466)"
FT                   /id="VAR_049464"
FT   VARIANT         664
FT                   /note="S -> W (in dbSNP:rs4823850)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_016094"
FT   VARIANT         773
FT                   /note="A -> V (in NTD; shows significantly reduced protein
FT                   localization to the cell membrane; dbSNP:rs12170597)"
FT                   /evidence="ECO:0000269|PubMed:22095531"
FT                   /id="VAR_067213"
FT   VARIANT         1126
FT                   /note="C -> R (in dbSNP:rs4823561)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_016095"
FT   VARIANT         1242
FT                   /note="V -> I (in dbSNP:rs6008842)"
FT                   /id="VAR_049465"
FT   VARIANT         1894
FT                   /note="Y -> H (in dbSNP:rs34467708)"
FT                   /id="VAR_049466"
FT   VARIANT         1994
FT                   /note="L -> P (in dbSNP:rs6008795)"
FT                   /id="VAR_049467"
FT   VARIANT         1995
FT                   /note="L -> P (in dbSNP:rs6008794)"
FT                   /id="VAR_049468"
FT   VARIANT         2045
FT                   /note="T -> M (in dbSNP:rs12169391)"
FT                   /id="VAR_049469"
FT   VARIANT         2107
FT                   /note="I -> V (in dbSNP:rs4044210)"
FT                   /id="VAR_024479"
FT   VARIANT         2219
FT                   /note="R -> H (in dbSNP:rs34267201)"
FT                   /id="VAR_049470"
FT   VARIANT         2268
FT                   /note="T -> A (in dbSNP:rs6007897)"
FT                   /id="VAR_024480"
FT   VARIANT         2312
FT                   /note="R -> P (does not affect protein localization to the
FT                   cell membrane; dbSNP:rs7287089)"
FT                   /evidence="ECO:0000269|PubMed:22095531"
FT                   /id="VAR_067214"
FT   VARIANT         2438
FT                   /note="R -> Q (in NTD; shows reduced protein localization
FT                   to the cell membrane; dbSNP:rs199688538)"
FT                   /evidence="ECO:0000269|PubMed:22095531"
FT                   /id="VAR_067215"
FT   VARIANT         2739
FT                   /note="N -> T (does not affect protein localization to the
FT                   cell membrane; dbSNP:rs148905592)"
FT                   /evidence="ECO:0000269|PubMed:22095531"
FT                   /id="VAR_067216"
FT   VARIANT         2797
FT                   /note="C -> S (in dbSNP:rs12165943)"
FT                   /id="VAR_049471"
FT   VARIANT         2903
FT                   /note="E -> Q (in dbSNP:rs9615351)"
FT                   /id="VAR_049472"
FT   VARIANT         2948
FT                   /note="G -> S (in dbSNP:rs35364389)"
FT                   /id="VAR_049473"
FT   VARIANT         2964
FT                   /note="S -> L (in NTD; shows reduced protein localization
FT                   to the cell membrane; dbSNP:rs6008777)"
FT                   /evidence="ECO:0000269|PubMed:22095531"
FT                   /id="VAR_067217"
FT   VARIANT         2983
FT                   /note="P -> A (in NTD; shows reduced protein localization
FT                   to the cell membrane; dbSNP:rs61741871)"
FT                   /evidence="ECO:0000269|PubMed:22095531"
FT                   /id="VAR_067218"
FT   CONFLICT        651
FT                   /note="E -> D (in Ref. 3; AAH00059)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   3014 AA;  329486 MW;  C34691AD3A1DFF3A CRC64;
     MAPPPPPVLP VLLLLAAAAA LPAMGLRAAA WEPRVPGGTR AFALRPGCTY AVGAACTPRA
     PRELLDVGRD GRLAGRRRVS GAGRPLPLQV RLVARSAPTA LSRRLRARTH LPGCGARARL
     CGTGARLCGA LCFPVPGGCA AAQHSALAAP TTLPACRCPP RPRPRCPGRP ICLPPGGSVR
     LRLLCALRRA AGAVRVGLAL EAATAGTPSA SPSPSPPLPP NLPEARAGPA RRARRGTSGR
     GSLKFPMPNY QVALFENEPA GTLILQLHAH YTIEGEEERV SYYMEGLFDE RSRGYFRIDS
     ATGAVSTDSV LDRETKETHV LRVKAVDYST PPRSATTYIT VLVKDTNDHS PVFEQSEYRE
     RVRENLEVGY EVLTIRASDR DSPINANLRY RVLGGAWDVF QLNESSGVVS TRAVLDREEA
     AEYQLLVEAN DQGRNPGPLS ATATVYIEVE DENDNYPQFS EQNYVVQVPE DVGLNTAVLR
     VQATDRDQGQ NAAIHYSILS GNVAGQFYLH SLSGILDVIN PLDFEDVQKY SLSIKAQDGG
     RPPLINSSGV VSVQVLDVND NEPIFVSSPF QATVLENVPL GYPVVHIQAV DADSGENARL
     HYRLVDTAST FLGGGSAGPK NPAPTPDFPF QIHNSSGWIT VCAELDREEV EHYSFGVEAV
     DHGSPPMSSS TSVSITVLDV NDNDPVFTQP TYELRLNEDA AVGSSVLTLQ ARDRDANSVI
     TYQLTGGNTR NRFALSSQRG GGLITLALPL DYKQEQQYVL AVTASDGTRS HTAHVLINVT
     DANTHRPVFQ SSHYTVSVSE DRPVGTSIAT LSANDEDTGE NARITYVIQD PVPQFRIDPD
     SGTMYTMMEL DYENQVAYTL TIMAQDNGIP QKSDTTTLEI LILDANDNAP QFLWDFYQGS
     IFEDAPPSTS ILQVSATDRD SGPNGRLLYT FQGGDDGDGD FYIEPTSGVI RTQRRLDREN
     VAVYNLWALA VDRGSPTPLS ASVEIQVTIL DINDNAPMFE KDELELFVEE NNPVGSVVAK
     IRANDPDEGP NAQIMYQIVE GDMRHFFQLD LLNGDLRAMV ELDFEVRREY VLVVQATSAP
     LVSRATVHIL LVDQNDNPPV LPDFQILFNN YVTNKSNSFP TGVIGCIPAH DPDVSDSLNY
     TFVQGNELRL LLLDPATGEL QLSRDLDNNR PLEALMEVSV SDGIHSVTAF CTLRVTIITD
     DMLTNSITVR LENMSQEKFL SPLLALFVEG VAAVLSTTKD DVFVFNVQND TDVSSNILNV
     TFSALLPGGV RGQFFPSEDL QEQIYLNRTL LTTISTQRVL PFDDNICLRE PCENYMKCVS
     VLRFDSSAPF LSSTTVLFRP IHPINGLRCR CPPGFTGDYC ETEIDLCYSD PCGANGRCRS
     REGGYTCECF EDFTGEHCEV DARSGRCANG VCKNGGTCVN LLIGGFHCVC PPGEYERPYC
     EVTTRSFPPQ SFVTFRGLRQ RFHFTISLTF ATQERNGLLL YNGRFNEKHD FIALEIVDEQ
     VQLTFSAGET TTTVAPKVPS GVSDGRWHSV QVQYYNKPNI GHLGLPHGPS GEKMAVVTVD
     DCDTTMAVRF GKDIGNYSCA AQGTQTGSKK SLDLTGPLLL GGVPNLPEDF PVHNRQFVGC
     MRNLSVDGKN VDMAGFIANN GTREGCAARR NFCDGRRCQN GGTCVNRWNM YLCECPLRFG
     GKNCEQAMPH PQLFSGESVV SWSDLNIIIS VPWYLGLMFR TRKEDSVLME ATSGGPTSFR
     LQILNNYLQF EVSHGPSDVE SVMLSGLRVT DGEWHHLLIE LKNVKEDSEM KHLVTMTLDY
     GMDQNKADIG GMLPGLTVRS VVVGGASEDK VSVRRGFRGC MQGVRMGGTP TNVATLNMNN
     ALKVRVKDGC DVDDPCTSSP CPPNSRCHDA WEDYSCVCDK GYLGINCVDA CHLNPCENMG
     ACVRSPGSPQ GYVCECGPSH YGPYCENKLD LPCPRGWWGN PVCGPCHCAV SKGFDPDCNK
     TNGQCQCKEN YYKLLAQDTC LPCDCFPHGS HSRTCDMATG QCACKPGVIG RQCNRCDNPF
     AEVTTLGCEV IYNGCPKAFE AGIWWPQTKF GQPAAVPCPK GSVGNAVRHC SGEKGWLPPE
     LFNCTTISFV DLRAMNEKLS RNETQVDGAR ALQLVRALRS ATQHTGTLFG NDVRTAYQLL
     GHVLQHESWQ QGFDLAATQD ADFHEDVIHS GSALLAPATR AAWEQIQRSE GGTAQLLRRL
     EGYFSNVARN VRRTYLRPFV IVTANMILAV DIFDKFNFTG ARVPRFDTIH EEFPRELESS
     VSFPADFFRP PEEKEGPLLR PAGRRTTPQT TRPGPGTERE APISRRRRHP DDAGQFAVAL
     VIIYRTLGQL LPERYDPDRR SLRLPHRPII NTPMVSTLVY SEGAPLPRPL ERPVLVEFAL
     LEVEERTKPV CVFWNHSLAV GGTGGWSARG CELLSRNRTH VACQCSHTAS FAVLMDISRR
     ENGEVLPLKI VTYAAVSLSL AALLVAFVLL SLVRMLRSNL HSIHKHLAVA LFLSQLVFVI
     GINQTENPFL CTVVAILLHY IYMSTFAWTL VESLHVYRML TEVRNIDTGP MRFYYVVGWG
     IPAIVTGLAV GLDPQGYGNP DFCWLSLQDT LIWSFAGPIG AVIIINTVTS VLSAKVSCQR
     KHHYYGKKGI VSLLRTAFLL LLLISATWLL GLLAVNRDAL SFHYLFAIFS GLQGPFVLLF
     HCVLNQEVRK HLKGVLGGRK LHLEDSATTR ATLLTRSLNC NTTFGDGPDM LRTDLGESTA
     SLDSIVRDEG IQKLGVSSGL VRGSHGEPDA SLMPRSCKDP PGHDSDSDSE LSLDEQSSSY
     ASSHSSDSED DGVGAEEKWD PARGAVHSTP KGDAVANHVP AGWPDQSLAE SDSEDPSGKP
     RLKVETKVSV ELHREEQGSH RGEYPPDQES GGAARLASSQ PPEQRKGILK NKVTYPPPLT
     LTEQTLKGRL REKLADCEQS PTSSRTSSLG SGGPDCAITV KSPGREPGRD HLNGVAMNVR
     TGSAQADGSD SEKP
//