ID A0A2K6S4U1_SAIBB Unreviewed; 1426 AA.
AC A0A2K6S4U1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Adhesion G protein-coupled receptor B1 {ECO:0000313|Ensembl:ENSSBOP00000002404.1};
GN Name=ADGRB1 {ECO:0000313|Ensembl:ENSSBOP00000002404.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000002404.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000002404.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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 STRING; 39432.ENSSBOP00000002404; -.
DR Ensembl; ENSSBOT00000013795.1; ENSSBOP00000002404.1; ENSSBOG00000012102.1.
DR GeneTree; ENSGT00940000157432; -.
DR OMA; SAMPRWG; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0001891; C:phagocytic cup; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
DR GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR GO; GO:0001786; F:phosphatidylserine binding; IEA:Ensembl.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:Ensembl.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; IEA:Ensembl.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0006910; P:phagocytosis, recognition; IEA:Ensembl.
DR GO; GO:1901741; P:positive regulation of myoblast fusion; IEA:Ensembl.
DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IEA:Ensembl.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IEA:Ensembl.
DR CDD; cd15990; 7tmB2_BAI1; 1.
DR Gene3D; 1.25.40.610; -; 1.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 5.
DR InterPro; IPR043838; AGRB_N.
DR InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like_7TM.
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; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR12011:SF39; ADHESION G PROTEIN-COUPLED RECEPTOR B1; 1.
DR PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF19188; AGRB_N; 1.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF02793; HRM; 1.
DR Pfam; PF00090; TSP_1; 5.
DR PRINTS; PR01694; BAIPRECURSOR.
DR PRINTS; PR00249; GPCRSECRETIN.
DR PRINTS; PR01705; TSP1REPEAT.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00209; TSP1; 5.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 5.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50092; TSP1; 5.
PE 4: Predicted;
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW Transducer {ECO:0000256|ARBA:ARBA00023224};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 869..890
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 902..921
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 933..951
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 972..991
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1011..1034
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1055..1077
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1083..1107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 509..579
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 867..1108
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 89..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1293..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1426 AA; 157568 MW; A75DB5A566DA98E2 CRC64;
AAVFPANASR CSWTLRNPDP RRYTLYMKVA KAPVPCAGPG RVRTYQFDSF LESTRTYLGV
ESFDDVLRLC DSSAPLAFLQ ASKQFLQMRR QQPPQDHDLG PRAAPAGPGD DFSVEYLVVG
NRNPSRAACQ MLCRWLDACL AGSHSSHPCG IMQTPCACLG GEAGGPAAGP LAPNGDVCLR
DAVAGGPENC LTSLTQDRGG HGTTGGWKLW SLWGECTRDC GGGLQTRTRT CLPAQGVEGG
SSEKGVTGHG RQDPQEGTPA AGRTSSRSQS LRSTDARRRE ELGDELQHFG FPAPQTGDPA
AEEWSPWSVC SSTCGEGWQT RTRFCVSSSY STQCSGPLRE QRLCNNSAVC PVHGAWDEWS
PWSLCSSTCG RGFRDRTRTC RPPQFGGNPC EGPEKQTKFC NIALCPVDGS WNEWSSWGTC
SASCSQGRQQ RTRECNGPSY GGAECQGHWV ETRDCFLQQC PVDGRWQAWA SWGSCSVTCG
AGSQRRERVC SGPFFGGAAC QGPHDEYRQC GTQRCPEPHE ICDEDNFGAV IWKETPAGEV
AAVRCPRNAT GLILRRCELD EEGIAYWEPP TYIRCVSIDY RNIQMMTREH LAKAQRGLPG
EGVSEVIQTL VEISQDGTSY SGDLLSTIDV LRNMTEIFRR AYYSPTPGDV QNFVQILSNL
LAEENREKWE EAQLAGPNAK ELFRLVEDFV DVIGFRMKDL RDAYQVTDNL VLSIHKLPAS
GATDISFPMK GWRATGDWAK VPEDRVTVSK SVFSTGLAEA DEASVFVVGT VLYRNLGSFL
ALQRNTTVLN SKVISVTVKP PPRSLRTPLE IEFAHMYNVS AVRVHTLVPA ETRVHRPCPS
PQPLSLRGLL RTVFPRFSQN MEKATLPSVT LIVGCGVSSL TLLMLVIIYV SVWRYIRSER
SVILINFCLS IISSNALILI GQTQTRNKVV CTLVAAFLHF FFLSSFCWVL TEAWQSYMAV
TGHLRNRLIR KRFLCLGWGL PALVVAISVG FTKAKGYSTM NYCWLSLEGG LLYAFVGPAA
AVVLVNMVIG ILVFNKLVSK DGITDKKLKE RAGASLWSSC VVLPLLALTW MSAVLAVTDR
RSALFQILFA VFDSLEGFVI VMVHCILRRE VQDAVKCRVV DRQEEGNGDS GGSFQNGHAQ
LMTDFEKDVD LACRSVLNKD IAACRTATIT GTLKRPSLPE EEKLKLAHAK GPPTNFNSLP
ANVSKLHLHG SPRYPGGPLP DFPNHSLTLK RDKAPKSSFV GDGDIFKKLD SELSRAQEKA
LDTSYVILPT ATATLRPKPK EETKYSIHID QMPQTRPSTK NENVTTLSVS SLERRKSRYA
ELDFEKIMHT RKRHQDMFQD LNRKLQHAVE KDKEVLGPES KPEKQQTPNK RPWESLRKAH
GTPTWVKKEL EPLQPSPLEL RSVEWERSGA TIPLVGQDII DLQTEV
//
