CELR1_HUMAN
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 03-AUG-2022, entry version 204.
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 INVOLVEMENT IN LMPHM9, AND VARIANT LMPHM9 1957-TRP--PRO-3014 DEL.
RX PubMed=26855770; DOI=10.1186/s13221-016-0035-5;
RA Gonzalez-Garay M.L., Aldrich M.B., Rasmussen J.C., Guilliod R.,
RA Lapinski P.E., King P.D., Sevick-Muraca E.M.;
RT "A novel mutation in CELSR1 is associated with hereditary lymphedema.";
RL Vasc. Cell 8:1-1(2016).
RN [6]
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).
RN [7]
RP VARIANTS LMPHM9 290-GLU--PRO-3014 DEL; THR-1058; SER-1539; HIS-1883;
RP VAL-2150; TRP-2425; GLY-2709 AND ARG-3001.
RX PubMed=31215153; DOI=10.1002/ajmg.a.61269;
RA Maltese P.E., Michelini S., Ricci M., Maitz S., Fiorentino A., Serrani R.,
RA Lazzerotti A., Bruson A., Paolacci S., Benedetti S., Bertelli M.;
RT "Increasing evidence of hereditary lymphedema caused by CELSR1 loss-of-
RT function variants.";
RL Am. J. Med. Genet. A 179:1718-1724(2019).
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 -!- DISEASE: Lymphatic malformation 9 (LMPHM9) [MIM:619319]: A form of
CC primary lymphedema, a disease characterized by swelling of body parts
CC due to developmental anomalies and functional defects of the lymphatic
CC system. Patients with lymphedema may suffer from recurrent local
CC infections. Impaired lymphatic drainage in the fetus can develop into
CC hydrops fetalis, a severe condition characterized by excessive fluid
CC accumulation in more than two fetal extra-vascular compartments and
CC body cavities, placental enlargement and edema, pericardial or pleural
CC effusion, or ascites. LMPHM9 is an autosomal dominant form with
CC variable expressivity and incomplete penetrance, characterized by the
CC onset of lower-extremity lymphedema in the first decades of life.
CC {ECO:0000269|PubMed:26855770, ECO:0000269|PubMed:31215153}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC 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; 112.
DR IntAct; Q9NYQ6; 15.
DR MINT; Q9NYQ6; -.
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; 193 antibodies from 30 providers.
DR DNASU; 9620; -.
DR Ensembl; ENST00000262738.9; ENSP00000262738.3; ENSG00000075275.18. [Q9NYQ6-1]
DR Ensembl; ENST00000454637.2; ENSP00000414689.2; ENSG00000075275.18. [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; Tissue enhanced (skin).
DR MalaCards; CELSR1; -.
DR MIM; 182940; phenotype.
DR MIM; 604523; gene.
DR MIM; 619319; phenotype.
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 SignaLink; Q9NYQ6; -.
DR BioGRID-ORCS; 9620; 14 hits in 1075 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 145 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 CDD; cd00055; EGF_Lam; 1.
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; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
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; IPR000203; GPS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
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; 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 290..3014
FT /note="Missing (in LMPHM9)"
FT /evidence="ECO:0000269|PubMed:26855770"
FT /id="VAR_085932"
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 1058
FT /note="A -> T (in LMPHM9; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31215153"
FT /id="VAR_085933"
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 1539
FT /note="N -> S (in LMPHM9; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31215153"
FT /id="VAR_085934"
FT VARIANT 1883
FT /note="P -> H (in LMPHM9; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31215153"
FT /id="VAR_085935"
FT VARIANT 1894
FT /note="Y -> H (in dbSNP:rs34467708)"
FT /id="VAR_049466"
FT VARIANT 1957..3014
FT /note="Missing (in LMPHM9)"
FT /evidence="ECO:0000269|PubMed:26855770"
FT /id="VAR_085936"
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 2150
FT /note="G -> V (in LMPHM9; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31215153"
FT /id="VAR_085937"
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 2425
FT /note="G -> W (in LMPHM9; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31215153"
FT /id="VAR_085938"
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 2709
FT /note="R -> G (in LMPHM9; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31215153"
FT /id="VAR_085939"
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 VARIANT 3001
FT /note="T -> R (in LMPHM9; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31215153"
FT /id="VAR_085940"
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
