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   27-MAR-2024, entry version 200.
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; 121.
DR   IntAct; Q9HCU4; 31.
DR   STRING; 9606.ENSP00000271332; -.
DR   MEROPS; P02.006; -.
DR   GlyConnect; 1055; 9 N-Linked glycans (5 sites).
DR   GlyCosmos; Q9HCU4; 18 sites, 10 glycans.
DR   GlyGen; Q9HCU4; 21 sites, 9 N-linked glycans (5 sites), 3 O-linked glycans (4 sites).
DR   iPTMnet; Q9HCU4; -.
DR   PhosphoSitePlus; Q9HCU4; -.
DR   SwissPalm; Q9HCU4; -.
DR   BioMuta; CELSR2; -.
DR   DMDM; 22095550; -.
DR   EPD; Q9HCU4; -.
DR   jPOST; Q9HCU4; -.
DR   MassIVE; Q9HCU4; -.
DR   MaxQB; Q9HCU4; -.
DR   PaxDb; 9606-ENSP00000271332; -.
DR   PeptideAtlas; Q9HCU4; -.
DR   ProteomicsDB; 81800; -.
DR   Pumba; Q9HCU4; -.
DR   Antibodypedia; 2940; 247 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   AGR; HGNC:3231; -.
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; FTLYIVE; -.
DR   OrthoDB; 4006628at2759; -.
DR   PhylomeDB; Q9HCU4; -.
DR   TreeFam; TF323983; -.
DR   PathwayCommons; Q9HCU4; -.
DR   SignaLink; Q9HCU4; -.
DR   BioGRID-ORCS; 1952; 116 hits in 1156 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 167 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR   GO; GO:0016020; C: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:0006355; P:regulation of DNA-templated transcription; ISS:BHF-UCL.
DR   GO; GO:0032880; P:regulation of protein localization; IEA:Ensembl.
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; cd11304; Cadherin_repeat; 9.
DR   CDD; cd00054; EGF_CA; 5.
DR   CDD; cd00055; EGF_Lam; 1.
DR   CDD; cd00110; LamG; 2.
DR   Gene3D; 1.25.40.610; -; 1.
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; 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_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; IPR000203; GPS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR002049; LE_dom.
DR   PANTHER; PTHR24026:SF32; CADHERIN EGF LAG SEVEN-PASS G-TYPE RECEPTOR 2; 1.
DR   PANTHER; PTHR24026; FAT ATYPICAL CADHERIN-RELATED; 1.
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; 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; 3.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 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.
DR   Genevisible; Q9HCU4; HS.
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; uncertain significance; 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
//