AGRB3_HUMAN
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 03-AUG-2022, entry version 189.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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; DOI=10.1159/000134693;
RA Shiratsuchi T., Nishimori H., Ichise H., Nakamura Y., Tokino T.;
RT "Cloning and characterization of BAI2 and BAI3, novel genes homologous to
RT 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 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. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., 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., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, 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 [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH C1QL1; C1QL2; C1QL3 AND 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 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 PROCESSING,
RP GLYCOSYLATION AT ASN-540 AND ASN-625, DISULFIDE BONDS, AND SUBCELLULAR
RP LOCATION.
RX PubMed=22333914; DOI=10.1038/emboj.2012.26;
RA Arac D., Boucard A.A., Bolliger M.F., Nguyen J., Soltis S.M., Sudhof T.C.,
RA Brunger A.T.;
RT "A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates
RT 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., Liebscher I.,
RA Lin H.H., Martinelli D.C., Monk K.R., Peeters M.C., Piao X., Promel S.,
RA Schoneberg T., Schwartz T.W., Singer K., Stacey M., Ushkaryov Y.A.,
RA Vallon M., Wolfrum U., Wright M.W., Xu L., Langenhan T., Schioth H.B.;
RT "International union of basic and clinical pharmacology. XCIV. Adhesion G
RT 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. Interacts
CC (via TSP N-terminal domains) with C1QL1, C1QL2, C1QL3 and C1QL4
CC (PubMed:21262840). Interacts with ELMO1, ELMO2 AND ELMO3
CC (PubMed:24567399). {ECO:0000269|PubMed:21262840,
CC ECO:0000269|PubMed:24567399}.
CC -!- INTERACTION:
CC O60242; Q8N954: GPATCH11; NbExp=3; IntAct=EBI-2682765, EBI-2555378;
CC O60242; O60883: GPR37L1; NbExp=3; IntAct=EBI-2682765, EBI-2927498;
CC O60242; P15941-11: MUC1; NbExp=3; IntAct=EBI-2682765, EBI-17263240;
CC O60242; P30825: SLC7A1; NbExp=3; IntAct=EBI-2682765, EBI-4289564;
CC O60242; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-2682765, EBI-12947623;
CC O60242; Q9ESN4: C1ql3; Xeno; NbExp=4; IntAct=EBI-2682765, EBI-15907894;
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 -!- 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 subunits,
CC an extracellular subunit and a seven-transmembrane subunit.
CC {ECO:0000269|PubMed:22333914}.
CC -!- MISCELLANEOUS: Autoproteolysis appears to be cell specific, does not
CC 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. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25476.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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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. [O60242-1]
DR RefSeq; XP_005248809.1; XM_005248752.2.
DR PDB; 4DLO; X-ray; 2.30 A; A/B=498-868.
DR PDBsum; 4DLO; -.
DR AlphaFoldDB; O60242; -.
DR SMR; O60242; -.
DR BioGRID; 107053; 11.
DR DIP; DIP-56121N; -.
DR IntAct; O60242; 10.
DR STRING; 9606.ENSP00000359630; -.
DR MEROPS; P02.027; -.
DR TCDB; 9.A.14.6.7; the g-protein-coupled receptor (gpcr) family.
DR GlyConnect; 2016; 1 N-Linked glycan (1 site).
DR GlyGen; O60242; 14 sites, 2 N-linked glycans (1 site).
DR iPTMnet; O60242; -.
DR PhosphoSitePlus; O60242; -.
DR BioMuta; ADGRB3; -.
DR MassIVE; O60242; -.
DR PaxDb; O60242; -.
DR PeptideAtlas; O60242; -.
DR PRIDE; O60242; -.
DR ProteomicsDB; 49275; -. [O60242-1]
DR ProteomicsDB; 6341; -.
DR Antibodypedia; 2938; 239 antibodies from 32 providers.
DR DNASU; 577; -.
DR Ensembl; ENST00000370598.6; ENSP00000359630.1; ENSG00000135298.15. [O60242-1]
DR Ensembl; ENST00000546190.5; ENSP00000441821.2; ENSG00000135298.15. [O60242-1]
DR GeneID; 577; -.
DR KEGG; hsa:577; -.
DR MANE-Select; ENST00000370598.6; ENSP00000359630.1; NM_001704.3; NP_001695.2.
DR UCSC; uc003pev.5; human. [O60242-1]
DR CTD; 577; -.
DR DisGeNET; 577; -.
DR GeneCards; ADGRB3; -.
DR HGNC; HGNC:945; ADGRB3.
DR HPA; ENSG00000135298; Group enriched (brain, pituitary gland).
DR MIM; 602684; gene.
DR neXtProt; NX_O60242; -.
DR OpenTargets; ENSG00000135298; -.
DR PharmGKB; PA25249; -.
DR VEuPathDB; HostDB:ENSG00000135298; -.
DR eggNOG; ENOG502QRKJ; Eukaryota.
DR GeneTree; ENSGT00940000155081; -.
DR HOGENOM; CLU_003751_1_0_1; -.
DR InParanoid; O60242; -.
DR OMA; CESKNAF; -.
DR OrthoDB; 27621at2759; -.
DR PhylomeDB; O60242; -.
DR TreeFam; TF331634; -.
DR PathwayCommons; O60242; -.
DR SignaLink; O60242; -.
DR BioGRID-ORCS; 577; 8 hits in 1070 CRISPR screens.
DR ChiTaRS; ADGRB3; human.
DR GeneWiki; Brain-specific_angiogenesis_inhibitor_3; -.
DR GenomeRNAi; 577; -.
DR Pharos; O60242; Tbio.
DR PRO; PR:O60242; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O60242; protein.
DR Bgee; ENSG00000135298; Expressed in middle temporal gyrus and 124 other tissues.
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; 2.60.220.50; -; 1.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR043838; AGRB_N.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
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; PF19188; AGRB_N; 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; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1522
FT /note="Adhesion G protein-coupled receptor B3"
FT /id="PRO_0000012865"
FT TOPO_DOM 25..880
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 881..901
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 902..910
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 911..931
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 932..939
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 940..960
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 961..981
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 982..1002
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1003..1023
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1024..1044
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1045..1098
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1099..1119
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1120..1125
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1126..1146
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1147..1522
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 30..159
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 291..343
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 345..398
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 400..453
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 455..508
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 816..868
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80ZF8"
FT MOD_RES 1411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80ZF8"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22333914"
FT CARBOHYD 625
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22333914"
FT CARBOHYD 779
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 812
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 828
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 937
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 303..336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 307..342
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 318..326
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 357..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 361..397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 372..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 412..447
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 416..452
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 427..437
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 467..502
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 471..507
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 482..492
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 514..549
FT /evidence="ECO:0000269|PubMed:22333914"
FT DISULFID 537..567
FT /evidence="ECO:0000269|PubMed:22333914"
FT DISULFID 819..851
FT /evidence="ECO:0000269|PubMed:22333914"
FT DISULFID 839..853
FT /evidence="ECO:0000269|PubMed:22333914"
FT VAR_SEQ 1..1036
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056939"
FT VARIANT 503
FT /note="N -> S (in dbSNP:rs1932618)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9533023, ECO:0000269|PubMed:9628581"
FT /id="VAR_046525"
FT TURN 502..504
FT /evidence="ECO:0007829|PDB:4DLO"
FT TURN 519..521
FT /evidence="ECO:0007829|PDB:4DLO"
FT STRAND 532..535
FT /evidence="ECO:0007829|PDB:4DLO"
FT STRAND 541..551
FT /evidence="ECO:0007829|PDB:4DLO"
FT STRAND 557..559
FT /evidence="ECO:0007829|PDB:4DLO"
FT STRAND 563..569
FT /evidence="ECO:0007829|PDB:4DLO"
FT HELIX 570..583
FT /evidence="ECO:0007829|PDB:4DLO"
FT HELIX 589..608
FT /evidence="ECO:0007829|PDB:4DLO"
FT HELIX 613..632
FT /evidence="ECO:0007829|PDB:4DLO"
FT HELIX 639..652
FT /evidence="ECO:0007829|PDB:4DLO"
FT HELIX 655..657
FT /evidence="ECO:0007829|PDB:4DLO"
FT HELIX 658..664
FT /evidence="ECO:0007829|PDB:4DLO"
FT TURN 665..667
FT /evidence="ECO:0007829|PDB:4DLO"
FT HELIX 670..687
FT /evidence="ECO:0007829|PDB:4DLO"
FT STRAND 694..698
FT /evidence="ECO:0007829|PDB:4DLO"
FT STRAND 700..710
FT /evidence="ECO:0007829|PDB:4DLO"
FT STRAND 718..721
FT /evidence="ECO:0007829|PDB:4DLO"
FT HELIX 730..734
FT /evidence="ECO:0007829|PDB:4DLO"
FT STRAND 738..741
FT /evidence="ECO:0007829|PDB:4DLO"
FT HELIX 743..746
FT /evidence="ECO:0007829|PDB:4DLO"
FT STRAND 759..769
FT /evidence="ECO:0007829|PDB:4DLO"
FT HELIX 770..772
FT /evidence="ECO:0007829|PDB:4DLO"
FT STRAND 781..783
FT /evidence="ECO:0007829|PDB:4DLO"
FT STRAND 787..794
FT /evidence="ECO:0007829|PDB:4DLO"
FT STRAND 803..808
FT /evidence="ECO:0007829|PDB:4DLO"
FT STRAND 815..823
FT /evidence="ECO:0007829|PDB:4DLO"
FT STRAND 833..835
FT /evidence="ECO:0007829|PDB:4DLO"
FT STRAND 839..845
FT /evidence="ECO:0007829|PDB:4DLO"
FT STRAND 848..855
FT /evidence="ECO:0007829|PDB:4DLO"
FT STRAND 857..864
FT /evidence="ECO:0007829|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
