CELR2_HUMAN
ID CELR2_HUMAN Reviewed; 2923 AA.
AC Q9HCU4; Q5T2Y7; Q92566;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Cadherin EGF LAG seven-pass G-type receptor 2 {ECO:0000305};
DE AltName: Full=Cadherin family member 10;
DE AltName: Full=Epidermal growth factor-like protein 2;
DE Short=EGF-like protein 2;
DE AltName: Full=Flamingo homolog 3;
DE AltName: Full=Multiple epidermal growth factor-like domains protein 3;
DE Short=Multiple EGF-like domains protein 3;
DE Flags: Precursor;
GN Name=CELSR2 {ECO:0000312|HGNC:HGNC:3231};
GN Synonyms=CDHF10, EGFL2, KIAA0279, MEGF3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10907856; DOI=10.1093/dnares/7.3.233;
RA Vincent J.B., Skaug J., Scherer S.W.;
RT "The human homologue of flamingo, EGFL2, encodes a brain-expressed large
RT cadherin-like protein with epidermal growth factor-like domains, and maps
RT to chromosome 1p13.3-p21.1.";
RL DNA Res. 7:233-235(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT "Genome-wide discovery and analysis of human seven transmembrane helix
RT receptor genes.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 70-2923, AND VARIANT HIS-1639.
RC TISSUE=Brain;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [5]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Nomura N.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP VARIANT TRP-2812.
RX PubMed=29983323; DOI=10.1016/j.neuron.2018.06.019;
RA Furey C.G., Choi J., Jin S.C., Zeng X., Timberlake A.T.,
RA Nelson-Williams C., Mansuri M.S., Lu Q., Duran D., Panchagnula S.,
RA Allocco A., Karimy J.K., Khanna A., Gaillard J.R., DeSpenza T., Antwi P.,
RA Loring E., Butler W.E., Smith E.R., Warf B.C., Strahle J.M., Limbrick D.D.,
RA Storm P.B., Heuer G., Jackson E.M., Iskandar B.J., Johnston J.M.,
RA Tikhonova I., Castaldi C., Lopez-Giraldez F., Bjornson R.D., Knight J.R.,
RA Bilguvar K., Mane S., Alper S.L., Haider S., Guclu B., Bayri Y., Sahin Y.,
RA Apuzzo M.L.J., Duncan C.C., DiLuna M.L., Guenel M., Lifton R.P.,
RA Kahle K.T.;
RT "De Novo Mutation in Genes Regulating Neural Stem Cell Fate in Human
RT Congenital Hydrocephalus.";
RL Neuron 99:302-314.e4(2018).
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 -!- TISSUE SPECIFICITY: Highest expression in brain and testis.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000305}.
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DR EMBL; AF234887; AAG00080.1; -; mRNA.
DR EMBL; AB065955; BAC06168.1; -; Genomic_DNA.
DR EMBL; AL390252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D87469; BAA13407.2; -; mRNA.
DR CCDS; CCDS796.1; -.
DR RefSeq; NP_001399.1; NM_001408.2.
DR SMR; Q9HCU4; -.
DR BioGRID; 108272; 117.
DR IntAct; Q9HCU4; 31.
DR STRING; 9606.ENSP00000271332; -.
DR MEROPS; P02.006; -.
DR GlyConnect; 1055; 9 N-Linked glycans (5 sites).
DR GlyGen; Q9HCU4; 18 sites, 9 N-linked glycans (5 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q9HCU4; -.
DR PhosphoSitePlus; Q9HCU4; -.
DR BioMuta; CELSR2; -.
DR DMDM; 22095550; -.
DR EPD; Q9HCU4; -.
DR jPOST; Q9HCU4; -.
DR MassIVE; Q9HCU4; -.
DR MaxQB; Q9HCU4; -.
DR PaxDb; Q9HCU4; -.
DR PeptideAtlas; Q9HCU4; -.
DR PRIDE; Q9HCU4; -.
DR ProteomicsDB; 81800; -.
DR Antibodypedia; 2940; 223 antibodies from 30 providers.
DR DNASU; 1952; -.
DR Ensembl; ENST00000271332.4; ENSP00000271332.3; ENSG00000143126.8.
DR GeneID; 1952; -.
DR KEGG; hsa:1952; -.
DR MANE-Select; ENST00000271332.4; ENSP00000271332.3; NM_001408.3; NP_001399.1.
DR UCSC; uc001dxa.5; human.
DR CTD; 1952; -.
DR DisGeNET; 1952; -.
DR GeneCards; CELSR2; -.
DR HGNC; HGNC:3231; CELSR2.
DR HPA; ENSG00000143126; Tissue enhanced (brain, skin).
DR MIM; 604265; gene.
DR neXtProt; NX_Q9HCU4; -.
DR OpenTargets; ENSG00000143126; -.
DR PharmGKB; PA26394; -.
DR VEuPathDB; HostDB:ENSG00000143126; -.
DR eggNOG; KOG4289; Eukaryota.
DR GeneTree; ENSGT00940000157493; -.
DR HOGENOM; CLU_000158_1_0_1; -.
DR InParanoid; Q9HCU4; -.
DR OMA; GCPTKKN; -.
DR OrthoDB; 23882at2759; -.
DR PhylomeDB; Q9HCU4; -.
DR TreeFam; TF323983; -.
DR PathwayCommons; Q9HCU4; -.
DR SignaLink; Q9HCU4; -.
DR BioGRID-ORCS; 1952; 115 hits in 1077 CRISPR screens.
DR ChiTaRS; CELSR2; human.
DR GeneWiki; CELSR2; -.
DR GenomeRNAi; 1952; -.
DR Pharos; Q9HCU4; Tbio.
DR PRO; PR:Q9HCU4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9HCU4; protein.
DR Bgee; ENSG00000143126; Expressed in ganglionic eminence and 165 other tissues.
DR Genevisible; Q9HCU4; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; NAS:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0033326; P:cerebrospinal fluid secretion; IEA:Ensembl.
DR GO; GO:0060271; P:cilium assembly; IEA:Ensembl.
DR GO; GO:0003341; P:cilium movement; IEA:Ensembl.
DR GO; GO:0048813; P:dendrite morphogenesis; ISS:BHF-UCL.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:BHF-UCL.
DR GO; GO:0097475; P:motor neuron migration; IEA:Ensembl.
DR GO; GO:0021999; P:neural plate anterior/posterior regionalization; ISS:BHF-UCL.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; ISS:BHF-UCL.
DR GO; GO:0032880; P:regulation of protein localization; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:BHF-UCL.
DR GO; GO:0021591; P:ventricular system development; IEA:Ensembl.
DR GO; GO:0016055; P:Wnt signaling pathway; ISS:BHF-UCL.
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; IPR013032; EGF-like_CS.
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; 1.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF12661; hEGF; 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 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; 4.
DR PROSITE; PS50026; EGF_3; 6.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 2.
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 Calcium; Cell membrane; Developmental protein; Disulfide bond;
KW EGF-like domain; G-protein coupled receptor; Glycoprotein; Hydroxylation;
KW Laminin EGF-like domain; Membrane; Receptor; Reference proteome; Repeat;
KW Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..2923
FT /note="Cadherin EGF LAG seven-pass G-type receptor 2"
FT /id="PRO_0000012916"
FT TOPO_DOM 32..2380
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2381..2401
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2402..2416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2417..2437
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2438
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2439..2459
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2460..2480
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2481..2501
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2502..2519
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2520..2540
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2541..2560
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2561..2581
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2582..2591
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2592..2612
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2613..2923
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 182..289
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 290..399
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 400..505
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 506..610
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 611..712
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 713..815
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 816..921
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 922..1023
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1028..1146
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1228..1286
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1288..1324
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1328..1366
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1367..1571
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1574..1610
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1614..1791
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1793..1828
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1829..1867
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1883..1922
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1924..1971
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2316..2368
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 154..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2213..2238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2688..2838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2854..2888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2741..2756
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2854..2872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1591
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000255"
FT MOD_RES 1810
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 701
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1036
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1076
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 1212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1827
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1900
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2024
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2043
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2061
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1232..1243
FT /evidence="ECO:0000250"
FT DISULFID 1237..1274
FT /evidence="ECO:0000250"
FT DISULFID 1276..1285
FT /evidence="ECO:0000250"
FT DISULFID 1292..1303
FT /evidence="ECO:0000250"
FT DISULFID 1297..1312
FT /evidence="ECO:0000250"
FT DISULFID 1314..1323
FT /evidence="ECO:0000250"
FT DISULFID 1332..1343
FT /evidence="ECO:0000250"
FT DISULFID 1337..1353
FT /evidence="ECO:0000250"
FT DISULFID 1355..1365
FT /evidence="ECO:0000250"
FT DISULFID 1545..1571
FT /evidence="ECO:0000250"
FT DISULFID 1578..1589
FT /evidence="ECO:0000250"
FT DISULFID 1583..1598
FT /evidence="ECO:0000250"
FT DISULFID 1600..1609
FT /evidence="ECO:0000250"
FT DISULFID 1761..1791
FT /evidence="ECO:0000250"
FT DISULFID 1797..1808
FT /evidence="ECO:0000250"
FT DISULFID 1802..1817
FT /evidence="ECO:0000250"
FT DISULFID 1819..1828
FT /evidence="ECO:0000250"
FT DISULFID 1832..1843
FT /evidence="ECO:0000250"
FT DISULFID 1837..1855
FT /evidence="ECO:0000250"
FT DISULFID 1857..1866
FT /evidence="ECO:0000250"
FT DISULFID 1887..1899
FT /evidence="ECO:0000250"
FT DISULFID 1889..1906
FT /evidence="ECO:0000250"
FT DISULFID 1908..1921
FT /evidence="ECO:0000250"
FT DISULFID 1924..1936
FT /evidence="ECO:0000250"
FT DISULFID 1926..1943
FT /evidence="ECO:0000250"
FT DISULFID 1945..1954
FT /evidence="ECO:0000250"
FT DISULFID 1957..1969
FT /evidence="ECO:0000250"
FT VARIANT 1066
FT /note="R -> Q (in dbSNP:rs12083590)"
FT /id="VAR_049474"
FT VARIANT 1639
FT /note="Y -> H (in dbSNP:rs653635)"
FT /evidence="ECO:0000269|PubMed:9039502"
FT /id="VAR_024481"
FT VARIANT 1992
FT /note="G -> R (in dbSNP:rs12567377)"
FT /id="VAR_049475"
FT VARIANT 2387
FT /note="T -> A (in dbSNP:rs17035649)"
FT /id="VAR_049476"
FT VARIANT 2812
FT /note="R -> W (found in a patient with congenital
FT hydrocephalus; unknown pathological significance;
FT dbSNP:rs149683589)"
FT /evidence="ECO:0000269|PubMed:29983323"
FT /id="VAR_083430"
SQ SEQUENCE 2923 AA; 317453 MW; 382757D315158ED8 CRC64;
MRSPATGVPL PTPPPPLLLL LLLLLPPPLL GDQVGPCRSL GSRGRGSSGA CAPMGWLCPS
SASNLWLYTS RCRDAGTELT GHLVPHHDGL RVWCPESEAH IPLPPAPEGC PWSCRLLGIG
GHLSPQGKLT LPEEHPCLKA PRLRCQSCKL AQAPGLRAGE RSPEESLGGR RKRNVNTAPQ
FQPPSYQATV PENQPAGTPV ASLRAIDPDE GEAGRLEYTM DALFDSRSNQ FFSLDPVTGA
VTTAEELDRE TKSTHVFRVT AQDHGMPRRS ALATLTILVT DTNDHDPVFE QQEYKESLRE
NLEVGYEVLT VRATDGDAPP NANILYRLLE GSGGSPSEVF EIDPRSGVIR TRGPVDREEV
ESYQLTVEAS DQGRDPGPRS TTAAVFLSVE DDNDNAPQFS EKRYVVQVRE DVTPGAPVLR
VTASDRDKGS NAVVHYSIMS GNARGQFYLD AQTGALDVVS PLDYETTKEY TLRVRAQDGG
RPPLSNVSGL VTVQVLDIND NAPIFVSTPF QATVLESVPL GYLVLHVQAI DADAGDNARL
EYRLAGVGHD FPFTINNGTG WISVAAELDR EEVDFYSFGV EARDHGTPAL TASASVSVTV
LDVNDNNPTF TQPEYTVRLN EDAAVGTSVV TVSAVDRDAH SVITYQITSG NTRNRFSITS
QSGGGLVSLA LPLDYKLERQ YVLAVTASDG TRQDTAQIVV NVTDANTHRP VFQSSHYTVN
VNEDRPAGTT VVLISATDED TGENARITYF MEDSIPQFRI DADTGAVTTQ AELDYEDQVS
YTLAITARDN GIPQKSDTTY LEILVNDVND NAPQFLRDSY QGSVYEDVPP FTSVLQISAT
DRDSGLNGRV FYTFQGGDDG DGDFIVESTS GIVRTLRRLD RENVAQYVLR AYAVDKGMPP
ARTPMEVTVT VLDVNDNPPV FEQDEFDVFV EENSPIGLAV ARVTATDPDE GTNAQIMYQI
VEGNIPEVFQ LDIFSGELTA LVDLDYEDRP EYVLVIQATS APLVSRATVH VRLLDRNDNP
PVLGNFEILF NNYVTNRSSS FPGGAIGRVP AHDPDISDSL TYSFERGNEL SLVLLNASTG
ELKLSRALDN NRPLEAIMSV LVSDGVHSVT AQCALRVTII TDEMLTHSIT LRLEDMSPER
FLSPLLGLFI QAVAATLATP PDHVVVFNVQ RDTDAPGGHI LNVSLSVGQP PGPGGGPPFL
PSEDLQERLY LNRSLLTAIS AQRVLPFDDN ICLREPCENY MRCVSVLRFD SSAPFIASSS
VLFRPIHPVG GLRCRCPPGF TGDYCETEVD LCYSRPCGPH GRCRSREGGY TCLCRDGYTG
EHCEVSARSG RCTPGVCKNG GTCVNLLVGG FKCDCPSGDF EKPYCQVTTR SFPAHSFITF
RGLRQRFHFT LALSFATKER DGLLLYNGRF NEKHDFVALE VIQEQVQLTF SAGESTTTVS
PFVPGGVSDG QWHTVQLKYY NKPLLGQTGL PQGPSEQKVA VVTVDGCDTG VALRFGSVLG
NYSCAAQGTQ GGSKKSLDLT GPLLLGGVPD LPESFPVRMR QFVGCMRNLQ VDSRHIDMAD
FIANNGTVPG CPAKKNVCDS NTCHNGGTCV NQWDAFSCEC PLGFGGKSCA QEMANPQHFL
GSSLVAWHGL SLPISQPWYL SLMFRTRQAD GVLLQAITRG RSTITLQLRE GHVMLSVEGT
GLQASSLRLE PGRANDGDWH HAQLALGASG GPGHAILSFD YGQQRAEGNL GPRLHGLHLS
NITVGGIPGP AGGVARGFRG CLQGVRVSDT PEGVNSLDPS HGESINVEQG CSLPDPCDSN
PCPANSYCSN DWDSYSCSCD PGYYGDNCTN VCDLNPCEHQ SVCTRKPSAP HGYTCECPPN
YLGPYCETRI DQPCPRGWWG HPTCGPCNCD VSKGFDPDCN KTSGECHCKE NHYRPPGSPT
CLLCDCYPTG SLSRVCDPED GQCPCKPGVI GRQCDRCDNP FAEVTTNGCE VNYDSCPRAI
EAGIWWPRTR FGLPAAAPCP KGSFGTAVRH CDEHRGWLPP NLFNCTSITF SELKGFAERL
QRNESGLDSG RSQQLALLLR NATQHTAGYF GSDVKVAYQL ATRLLAHEST QRGFGLSATQ
DVHFTENLLR VGSALLDTAN KRHWELIQQT EGGTAWLLQH YEAYASALAQ NMRHTYLSPF
TIVTPNIVIS VVRLDKGNFA GAKLPRYEAL RGEQPPDLET TVILPESVFR ETPPVVRPAG
PGEAQEPEEL ARRQRRHPEL SQGEAVASVI IYRTLAGLLP HNYDPDKRSL RVPKRPIINT
PVVSISVHDD EELLPRALDK PVTVQFRLLE TEERTKPICV FWNHSILVSG TGGWSARGCE
VVFRNESHVS CQCNHMTSFA VLMDVSRREN GEILPLKTLT YVALGVTLAA LLLTFFFLTL
LRILRSNQHG IRRNLTAALG LAQLVFLLGI NQADLPFACT VIAILLHFLY LCTFSWALLE
ALHLYRALTE VRDVNTGPMR FYYMLGWGVP AFITGLAVGL DPEGYGNPDF CWLSIYDTLI
WSFAGPVAFA VSMSVFLYIL AARASCAAQR QGFEKKGPVS GLQPSFAVLL LLSATWLLAL
LSVNSDTLLF HYLFATCNCI QGPFIFLSYV VLSKEVRKAL KLACSRKPSP DPALTTKSTL
TSSYNCPSPY ADGRLYQPYG DSAGSLHSTS RSGKSQPSYI PFLLREESAL NPGQGPPGLG
DPGSLFLEGQ DQQHDPDTDS DSDLSLEDDQ SGSYASTHSS DSEEEEEEEE EEAAFPGEQG
WDSLLGPGAE RLPLHSTPKD GGPGPGKAPW PGDFGTTAKE SSGNGAPEER LRENGDALSR
EGSLGPLPGS SAQPHKGILK KKCLPTISEK SSLLRLPLEQ CTGSSRGSSA SEGSRGGPPP
RPPPRQSLQE QLNGVMPIAM SIKAGTVDED SSGSEFLFFN FLH
