ID A0A3Q1AV32_AMPOC Unreviewed; 1285 AA.
AC A0A3Q1AV32;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Adhesion G protein-coupled receptor B1 {ECO:0000313|Ensembl:ENSAOCP00000001891.1};
GN Name=ADGRB1 {ECO:0000313|Ensembl:ENSAOCP00000001891.1};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000001891.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000001891.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR Ensembl; ENSAOCT00000012436.1; ENSAOCP00000001891.1; ENSAOCG00000005082.1.
DR GeneTree; ENSGT00940000157432; -.
DR Proteomes; UP000257160; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
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; 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; IPR000203; GPS.
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; PF16489; GAIN; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF00090; TSP_1; 5.
DR PRINTS; PR01694; BAIPRECURSOR.
DR PRINTS; PR00249; GPCRSECRETIN.
DR PRINTS; PR01705; TSP1REPEAT.
DR SMART; SM00303; GPS; 1.
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; PS50221; GPS; 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:UP000257160};
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 680..701
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 713..732
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 744..762
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 783..802
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 822..845
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 866..888
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 294..374
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 678..919
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 53..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1206..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1206..1244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1285 AA; 142072 MW; 8A8CE7CF9C7CC02B CRC64;
MCVCVSPGGW SVWGQWAQCS SECGGGIQTR TRTCQSPPEE LYLCEGVVEE GRPCNSQSCT
GKGRHLSRSQ SLRSVDSRKR DDVDKPRSGQ QSPQTGEEWS AWSVCSATCG EGWQSRTRFC
VSSSYSTQCS GPLREQRPCN NSAVCPVHGA WDEWSPWSLC SSTCGRGYRS RTRTCTPPQF
GGDPCDGPEK QTKFCNIAVC PVDGVWNEWS SWSSCSASCS NGTMQRTREC NGPSYGGSEC
RGEWLETVDC FLGECPVDGK WQPWSLWSGC SKTCGGGNQQ RNRICYGPFF GGQSCPGEQE
EIRRCNEKRC PELYEICGED NFSNVVWKMT AAGDTAAVRC PPNAIGLILR RCTLDEEGIA
YWENPTYMKC ISNDYRSIQT LTREHLSKAQ RGLVGDGVSE VMNKLRVTSS EGTSYSGDLL
AIVDVLKNMT EIFRRAYYSP SSADMRNFVQ SVSNLLMEEN RERWEEAQLL GPNIKELFRL
VEDFVDVIGL RMKDFQDMYE VTDNLVLSIH KRPVVGQADI SFPMKGWRGM VDWARNSEDR
VTIPKNILST GQPGENDSST FVTGIVLYRN LGSILTLQRN STVLNSKVLS VTIKPTPASL
SAPVVVEFSH LYNGTTNQTC ISWDESDSAS LLGSWSARGC KAVLVDSFRT KCVCDRLSTF
AILARLNPEM NMDKTQLPSV TLIVGCGVSS LTLLLLIIIY VSVWRYIRSE RSVILINFCL
SIISSNALIL IGQTQTRNKV LCTLIAAFLH FFFLSSFCWV LTEAWQSYMA VTGRLRNRII
RKRFLCLGWG LPALVVAISV GFTKAKGYGT PSYCWLSLEG GLLYAFVGPA AAVVLVNMVI
GILVFNKLVS KDGITDMKLK ERAGASLWSS CVVLPLLALT WMSAVLAITD RRSALFQILF
AVFDSLEGFV IVMVHCILRR EVQEAVKCRV VDRQEDANGD SGGSFQNGHA QLMTDFEKDV
DMACRSGKLQ VLSVFDFVFV LCTMKRSSLQ GEEKASSGTL TLQKGSNFNT MPASMAKVHL
QNVADYTSHT LTLRREKGAA KGISTELSSE GAGKGPGYVI LPTNNTGTLK PAKGKEEQTA
KYNMGIEQLP QTRLIHLANP ASGEPVPGFG LQSLPADQVS VSCSDRDSPA HNLQNMSRDS
QVANNMCDGG ESGNSGVMSK SETVSTLSMS SLERRKSRYA ELDFEKIMHT RKRHQDMFQD
LNRKIHSADK DRESPPVDAK ADKQQTPSKR AWEGIRKPHS PPSWVRKDLE TVAASPLELQ
TVEWEKTSAT IPLVGQEIMD LQTEV
//
