ID AGRB3_HUMAN Reviewed; 1522 AA. AC O60242; B7Z1K0; O60297; Q2NKN6; Q5VY37; Q9BX54; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2010, sequence version 2. DT 13-FEB-2019, entry version 169. DE RecName: Full=Adhesion G protein-coupled receptor B3 {ECO:0000303|PubMed:25713288}; DE AltName: Full=Brain-specific angiogenesis inhibitor 3; DE Flags: Precursor; GN Name=ADGRB3 {ECO:0000312|HGNC:HGNC:945}; Synonyms=BAI3, KIAA0550; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-503, AND TISSUE RP SPECIFICITY. RC TISSUE=Fetal brain; RX PubMed=9533023; RA Shiratsuchi T., Nishimori H., Ichise H., Nakamura Y., Tokino T.; RT "Cloning and characterization of BAI2 and BAI3, novel genes homologous RT to brain-specific angiogenesis inhibitor 1 (BAI1)."; RL Cytogenet. Cell Genet. 79:103-108(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP SER-503. RC TISSUE=Brain; RX PubMed=9628581; DOI=10.1093/dnares/5.1.31; RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., RA Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. IX. RT The complete sequences of 100 new cDNA clones from brain which can RT code for large proteins in vitro."; RL DNA Res. 5:31-39(1998). RN [3] RP SEQUENCE REVISION TO 643-665 AND C-TERMINUS. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Cerebellum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP SER-503. 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, AND IDENTIFICATION RP 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 [9] RP SUBCELLULAR LOCATION, AND INTERACTION WITH C1QL1; C1QL2; C1QL3 AND RP C1QL4. RX PubMed=21262840; DOI=10.1073/pnas.1019577108; RA Bolliger M.F., Martinelli D.C., Sudhof T.C.; RT "The cell-adhesion G protein-coupled receptor BAI3 is a high-affinity RT receptor for C1q-like proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 108:2534-2539(2011). RN [10] RP FUNCTION, AND INTERACTION WITH ELMO1; ELMO2 AND ELMO3. RX PubMed=24567399; DOI=10.1073/pnas.1313886111; RA Hamoud N., Tran V., Croteau L.P., Kania A., Cote J.F.; RT "G-protein coupled receptor BAI3 promotes myoblast fusion in RT vertebrates."; RL Proc. Natl. Acad. Sci. U.S.A. 111:3745-3750(2014). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 498-868, PROTEOLYTIC RP PROCESSING, GLYCOSYLATION AT ASN-540 AND ASN-625, DISULFIDE BONDS, AND RP SUBCELLULAR LOCATION. RX PubMed=22333914; DOI=10.1038/emboj.2012.26; RA Arac D., Boucard A.A., Bolliger M.F., Nguyen J., Soltis S.M., RA Sudhof T.C., Brunger A.T.; RT "A novel evolutionarily conserved domain of cell-adhesion GPCRs RT mediates autoproteolysis."; RL EMBO J. 31:1364-1378(2012). RN [12] RP NOMENCLATURE. RX PubMed=25713288; DOI=10.1124/pr.114.009647; RA Hamann J., Aust G., Arac D., Engel F.B., Formstone C., Fredriksson R., RA Hall R.A., Harty B.L., Kirchhoff C., Knapp B., Krishnan A., RA Liebscher I., Lin H.H., Martinelli D.C., Monk K.R., Peeters M.C., RA Piao X., Promel S., Schoneberg T., Schwartz T.W., Singer K., RA Stacey M., Ushkaryov Y.A., Vallon M., Wolfrum U., Wright M.W., Xu L., RA Langenhan T., Schioth H.B.; RT "International union of basic and clinical pharmacology. XCIV. RT Adhesion G protein-coupled receptors."; RL Pharmacol. Rev. 67:338-367(2015). CC -!- FUNCTION: Receptor that plays a role in the regulation of CC synaptogenesis and dendritic spine formation at least partly via CC interaction with ELMO1 and RAC1 activity (By similarity). Promotes CC myoblast fusion through ELMO/DOCK1 (PubMed:24567399). CC {ECO:0000250|UniProtKB:Q80ZF8, ECO:0000269|PubMed:24567399}. CC -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular CC region non-covalently linked to a seven-transmembrane moiety. CC Interacts (via TSP N-terminal domains) with C1QL1, C1QL2, C1QL3 CC and C1QL4 (PubMed:21262840). Interacts with ELMO1, ELMO2 AND ELMO3 CC (PubMed:24567399). {ECO:0000269|PubMed:21262840, CC ECO:0000269|PubMed:24567399}. CC -!- INTERACTION: CC Q9ESN4:C1ql3 (xeno); NbExp=4; IntAct=EBI-2682765, EBI-15907894; CC Q8N954:GPATCH11; NbExp=3; IntAct=EBI-2682765, EBI-2555378; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21262840, CC ECO:0000269|PubMed:22333914}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O60242-1; Sequence=Displayed; CC Name=2; CC IsoId=O60242-2; Sequence=VSP_056939; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Strongly expressed in brain. Also detected in CC heart. Reduced expression in some glioblastoma cell lines. CC {ECO:0000269|PubMed:9533023}. CC -!- PTM: The endogenous protein is proteolytically cleaved into 2 CC subunits, an extracellular subunit and a seven-transmembrane CC subunit. {ECO:0000269|PubMed:22333914}. CC -!- MISCELLANEOUS: Autoproteolysis appears to be cell specific, does CC not readily undergo proteolytic cleavage in HEK293T cells. CC {ECO:0000269|PubMed:25713288}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. CC Adhesion G-protein coupled receptor (ADGR) subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA25476.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AB005299; BAA25363.1; -; mRNA. DR EMBL; AB011122; BAA25476.2; ALT_INIT; mRNA. DR EMBL; AK293560; BAH11536.1; -; mRNA. DR EMBL; AL035469; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL078598; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL589875; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL133378; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL158051; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL160401; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL356117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL359714; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL391807; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471051; EAW48837.1; -; Genomic_DNA. DR EMBL; BC111720; AAI11721.1; -; mRNA. DR CCDS; CCDS4968.1; -. [O60242-1] DR PIR; T00028; T00028. DR PIR; T00326; T00326. DR RefSeq; NP_001695.1; NM_001704.2. DR RefSeq; XP_005248809.1; XM_005248752.2. [O60242-1] DR UniGene; Hs.13261; -. DR PDB; 4DLO; X-ray; 2.30 A; A/B=498-868. DR PDBsum; 4DLO; -. DR ProteinModelPortal; O60242; -. DR SMR; O60242; -. DR BioGrid; 107053; 3. DR DIP; DIP-56121N; -. DR IntAct; O60242; 9. DR STRING; 9606.ENSP00000359630; -. DR MEROPS; P02.027; -. DR TCDB; 9.A.14.6.7; the g-protein-coupled receptor (gpcr) family. DR iPTMnet; O60242; -. DR PhosphoSitePlus; O60242; -. DR BioMuta; ADGRB3; -. DR jPOST; O60242; -. DR PaxDb; O60242; -. DR PeptideAtlas; O60242; -. DR PRIDE; O60242; -. DR ProteomicsDB; 49275; -. DR Ensembl; ENST00000370598; ENSP00000359630; ENSG00000135298. [O60242-1] DR Ensembl; ENST00000546190; ENSP00000441821; ENSG00000135298. [O60242-1] DR GeneID; 577; -. DR KEGG; hsa:577; -. DR UCSC; uc003pev.5; human. [O60242-1] DR CTD; 577; -. DR DisGeNET; 577; -. DR EuPathDB; HostDB:ENSG00000135298.13; -. DR GeneCards; ADGRB3; -. DR HGNC; HGNC:945; ADGRB3. DR MIM; 602684; gene. DR neXtProt; NX_O60242; -. DR OpenTargets; ENSG00000135298; -. DR PharmGKB; PA25249; -. DR eggNOG; ENOG410IEA0; Eukaryota. DR eggNOG; ENOG4111FBM; LUCA. DR GeneTree; ENSGT00940000155081; -. DR HOGENOM; HOG000230916; -. DR HOVERGEN; HBG004813; -. DR InParanoid; O60242; -. DR KO; K04598; -. DR OMA; WERRIRT; -. DR OrthoDB; 27621at2759; -. DR PhylomeDB; O60242; -. DR TreeFam; TF331634; -. DR ChiTaRS; ADGRB3; human. DR GeneWiki; Brain-specific_angiogenesis_inhibitor_3; -. DR GenomeRNAi; 577; -. DR PRO; PR:O60242; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000135298; Expressed in 137 organ(s), highest expression level in middle temporal gyrus. DR ExpressionAtlas; O60242; baseline and differential. DR Genevisible; O60242; HS. DR GO; GO:0016021; C:integral component of membrane; TAS:GDB. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IPI:UniProtKB. DR GO; GO:0098794; C:postsynapse; IBA:GO_Central. DR GO; GO:0043083; C:synaptic cleft; IBA:GO_Central. DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central. DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:GDB. DR GO; GO:0099558; P:maintenance of synapse structure; IEA:Ensembl. DR GO; GO:0061743; P:motor learning; IEA:Ensembl. DR GO; GO:0007520; P:myoblast fusion; IDA:UniProtKB. DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:InterPro. DR GO; GO:0016322; P:neuron remodeling; IBA:GO_Central. DR GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl. DR GO; GO:0048814; P:regulation of dendrite morphogenesis; ISS:UniProtKB. DR Gene3D; 2.20.100.10; -; 4. DR Gene3D; 4.10.1240.10; -; 1. DR InterPro; IPR000859; CUB_dom. DR InterPro; IPR032471; GAIN_dom_N. DR InterPro; IPR017981; GPCR_2-like. DR InterPro; IPR008077; GPCR_2_brain_angio_inhib. DR InterPro; IPR036445; GPCR_2_extracell_dom_sf. DR InterPro; IPR001879; GPCR_2_extracellular_dom. DR InterPro; IPR000832; GPCR_2_secretin-like. DR InterPro; IPR017983; GPCR_2_secretin-like_CS. DR InterPro; IPR000203; GPS. DR InterPro; IPR000884; TSP1_rpt. DR InterPro; IPR036383; TSP1_rpt_sf. DR Pfam; PF00002; 7tm_2; 1. DR Pfam; PF16489; GAIN; 1. DR Pfam; PF01825; GPS; 1. DR Pfam; PF02793; HRM; 1. DR Pfam; PF00090; TSP_1; 4. DR PRINTS; PR01694; BAIPRECURSOR. DR PRINTS; PR00249; GPCRSECRETIN. DR SMART; SM00303; GPS; 1. DR SMART; SM00008; HormR; 1. DR SMART; SM00209; TSP1; 4. DR SUPFAM; SSF82895; SSF82895; 4. DR PROSITE; PS01180; CUB; 1. DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1. DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. DR PROSITE; PS50221; GPS; 1. DR PROSITE; PS50092; TSP1; 4. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Complete proteome; KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane; KW Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat; KW Signal; Transducer; Transmembrane; Transmembrane helix. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 1522 Adhesion G protein-coupled receptor B3. FT /FTId=PRO_0000012865. FT TOPO_DOM 25 880 Extracellular. {ECO:0000305}. FT TRANSMEM 881 901 Helical; Name=1. {ECO:0000255}. FT TOPO_DOM 902 910 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 911 931 Helical; Name=2. {ECO:0000255}. FT TOPO_DOM 932 939 Extracellular. {ECO:0000305}. FT TRANSMEM 940 960 Helical; Name=3. {ECO:0000255}. FT TOPO_DOM 961 981 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 982 1002 Helical; Name=4. {ECO:0000255}. FT TOPO_DOM 1003 1023 Extracellular. {ECO:0000305}. FT TRANSMEM 1024 1044 Helical; Name=5. {ECO:0000255}. FT TOPO_DOM 1045 1098 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 1099 1119 Helical; Name=6. {ECO:0000255}. FT TOPO_DOM 1120 1125 Extracellular. {ECO:0000305}. FT TRANSMEM 1126 1146 Helical; Name=7. {ECO:0000255}. FT TOPO_DOM 1147 1522 Cytoplasmic. {ECO:0000305}. FT DOMAIN 30 159 CUB. {ECO:0000255|PROSITE- FT ProRule:PRU00059}. FT DOMAIN 291 343 TSP type-1 1. {ECO:0000255|PROSITE- FT ProRule:PRU00210}. FT DOMAIN 345 398 TSP type-1 2. {ECO:0000255|PROSITE- FT ProRule:PRU00210}. FT DOMAIN 400 453 TSP type-1 3. {ECO:0000255|PROSITE- FT ProRule:PRU00210}. FT DOMAIN 455 508 TSP type-1 4. {ECO:0000255|PROSITE- FT ProRule:PRU00210}. FT DOMAIN 816 868 GPS. {ECO:0000255|PROSITE- FT ProRule:PRU00098}. FT COMPBIAS 942 945 Poly-Thr. FT COMPBIAS 1173 1176 Poly-Ser. FT MOD_RES 619 619 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1220 1220 Phosphoserine. FT {ECO:0000250|UniProtKB:Q80ZF8}. FT MOD_RES 1411 1411 Phosphoserine. FT {ECO:0000250|UniProtKB:Q80ZF8}. FT CARBOHYD 51 51 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 54 54 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 82 82 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 105 105 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 241 241 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 337 337 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 418 418 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 540 540 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:22333914}. FT CARBOHYD 625 625 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:22333914}. FT CARBOHYD 779 779 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 812 812 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 828 828 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 937 937 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 30 55 {ECO:0000255|PROSITE-ProRule:PRU00059}. FT DISULFID 303 336 {ECO:0000255|PROSITE-ProRule:PRU00210}. FT DISULFID 307 342 {ECO:0000255|PROSITE-ProRule:PRU00210}. FT DISULFID 318 326 {ECO:0000255|PROSITE-ProRule:PRU00210}. FT DISULFID 357 392 {ECO:0000255|PROSITE-ProRule:PRU00210}. FT DISULFID 361 397 {ECO:0000255|PROSITE-ProRule:PRU00210}. FT DISULFID 372 382 {ECO:0000255|PROSITE-ProRule:PRU00210}. FT DISULFID 412 447 {ECO:0000255|PROSITE-ProRule:PRU00210}. FT DISULFID 416 452 {ECO:0000255|PROSITE-ProRule:PRU00210}. FT DISULFID 427 437 {ECO:0000255|PROSITE-ProRule:PRU00210}. FT DISULFID 467 502 {ECO:0000255|PROSITE-ProRule:PRU00210}. FT DISULFID 471 507 {ECO:0000255|PROSITE-ProRule:PRU00210}. FT DISULFID 482 492 {ECO:0000255|PROSITE-ProRule:PRU00210}. FT DISULFID 514 549 {ECO:0000269|PubMed:22333914}. FT DISULFID 537 567 {ECO:0000269|PubMed:22333914}. FT DISULFID 819 851 {ECO:0000269|PubMed:22333914}. FT DISULFID 839 853 {ECO:0000269|PubMed:22333914}. FT VAR_SEQ 1 1036 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_056939. FT VARIANT 503 503 N -> S (in dbSNP:rs1932618). FT {ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:9533023, FT ECO:0000269|PubMed:9628581}. FT /FTId=VAR_046525. FT TURN 502 504 {ECO:0000244|PDB:4DLO}. FT TURN 519 521 {ECO:0000244|PDB:4DLO}. FT STRAND 532 535 {ECO:0000244|PDB:4DLO}. FT STRAND 541 551 {ECO:0000244|PDB:4DLO}. FT STRAND 557 559 {ECO:0000244|PDB:4DLO}. FT STRAND 563 569 {ECO:0000244|PDB:4DLO}. FT HELIX 570 583 {ECO:0000244|PDB:4DLO}. FT HELIX 589 608 {ECO:0000244|PDB:4DLO}. FT HELIX 613 632 {ECO:0000244|PDB:4DLO}. FT HELIX 639 652 {ECO:0000244|PDB:4DLO}. FT HELIX 655 657 {ECO:0000244|PDB:4DLO}. FT HELIX 658 664 {ECO:0000244|PDB:4DLO}. FT TURN 665 667 {ECO:0000244|PDB:4DLO}. FT HELIX 670 687 {ECO:0000244|PDB:4DLO}. FT STRAND 694 698 {ECO:0000244|PDB:4DLO}. FT STRAND 700 710 {ECO:0000244|PDB:4DLO}. FT STRAND 718 721 {ECO:0000244|PDB:4DLO}. FT HELIX 730 734 {ECO:0000244|PDB:4DLO}. FT STRAND 738 741 {ECO:0000244|PDB:4DLO}. FT HELIX 743 746 {ECO:0000244|PDB:4DLO}. FT STRAND 759 769 {ECO:0000244|PDB:4DLO}. FT HELIX 770 772 {ECO:0000244|PDB:4DLO}. FT STRAND 781 783 {ECO:0000244|PDB:4DLO}. FT STRAND 787 794 {ECO:0000244|PDB:4DLO}. FT STRAND 803 808 {ECO:0000244|PDB:4DLO}. FT STRAND 815 823 {ECO:0000244|PDB:4DLO}. FT STRAND 833 835 {ECO:0000244|PDB:4DLO}. FT STRAND 839 845 {ECO:0000244|PDB:4DLO}. FT STRAND 848 855 {ECO:0000244|PDB:4DLO}. FT STRAND 857 864 {ECO:0000244|PDB:4DLO}. SQ SEQUENCE 1522 AA; 171518 MW; D22D0A5CF59E811F CRC64; MKAVRNLLIY IFSTYLLVMF GFNAAQDFWC STLVKGVIYG SYSVSEMFPK NFTNCTWTLE NPDPTKYSIY LKFSKKDLSC SNFSLLAYQF DHFSHEKIKD LLRKNHSIMQ LCNSKNAFVF LQYDKNFIQI RRVFPTNFPG LQKKGEEDQK SFFEFLVLNK VSPSQFGCHV LCTWLESCLK SENGRTESCG IMYTKCTCPQ HLGEWGIDDQ SLILLNNVVL PLNEQTEGCL TQELQTTQVC NLTREAKRPP KEEFGMMGDH TIKSQRPRSV HEKRVPQEQA DAAKFMAQTG ESGVEEWSQW STCSVTCGQG SQVRTRTCVS PYGTHCSGPL RESRVCNNTA LCPVHGVWEE WSPWSLCSFT CGRGQRTRTR SCTPPQYGGR PCEGPETHHK PCNIALCPVD GQWQEWSSWS QCSVTCSNGT QQRSRQCTAA AHGGSECRGP WAESRECYNP ECTANGQWNQ WGHWSGCSKS CDGGWERRIR TCQGAVITGQ QCEGTGEEVR RCNEQRCPAP YEICPEDYLM SMVWKRTPAG DLAFNQCPLN ATGTTSRRCS LSLHGVAFWE QPSFARCISN EYRHLQHSIK EHLAKGQRML AGDGMSQVTK TLLDLTQRKN FYAGDLLMSV EILRNVTDTF KRASYIPASD GVQNFFQIVS NLLDEENKEK WEDAQQIYPG SIELMQVIED FIHIVGMGMM DFQNSYLMTG NVVASIQKLP AASVLTDINF PMKGRKGMVD WARNSEDRVV IPKSIFTPVS SKELDESSVF VLGAVLYKNL DLILPTLRNY TVINSKIIVV TIRPEPKTTD SFLEIELAHL ANGTLNPYCV LWDDSKTNES LGTWSTQGCK TVLTDASHTK CLCDRLSTFA ILAQQPREII MESSGTPSVT LIVGSGLSCL ALITLAVVYA ALWRYIRSER SIILINFCLS IISSNILILV GQTQTHNKSI CTTTTAFLHF FFLASFCWVL TEAWQSYMAV TGKIRTRLIR KRFLCLGWGL PALVVATSVG FTRTKGYGTD HYCWLSLEGG LLYAFVGPAA AVVLVNMVIG ILVFNKLVSR DGILDKKLKH RAGQMSEPHS GLTLKCAKCG VVSTTALSAT TASNAMASLW SSCVVLPLLA LTWMSAVLAM TDKRSILFQI LFAVFDSLQG FVIVMVHCIL RREVQDAFRC RLRNCQDPIN ADSSSSFPNG HAQIMTDFEK DVDIACRSVL HKDIGPCRAA TITGTLSRIS LNDDEEEKGT NPEGLSYSTL PGNVISKVII QQPTGLHMPM SMNELSNPCL KKENSELRRT VYLCTDDNLR GADMDIVHPQ ERMMESDYIV MPRSSVNNQP SMKEESKMNI GMETLPHERL LHYKVNPEFN MNPPVMDQFN MNLEQHLAPQ EHMQNLPFEP RTAVKNFMAS ELDDNAGLSR SETGSTISMS SLERRKSRYS DLDFEKVMHT RKRHMELFQE LNQKFQTLDR FRDIPNTSSM ENPAPNKNPW DTFKNPSEYP HYTTINVLDT EAKDALELRP AEWEKCLNLP LDVQEGDFQT EV //