ID A0A3Q1C609_AMPOC Unreviewed; 1315 AA.
AC A0A3Q1C609;
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:ENSAOCP00000020699.1};
GN Name=ADGRB1 {ECO:0000313|Ensembl:ENSAOCP00000020699.1};
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:ENSAOCP00000020699.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000020699.1}
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; ENSAOCT00000012384.1; ENSAOCP00000020699.1; 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 684..705
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 717..736
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 748..766
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 787..806
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 826..849
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 870..892
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 898..922
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1287..1309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 298..378
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 682..923
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 53..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1077
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"
SQ SEQUENCE 1315 AA; 144635 MW; 599166A8715F2EBD CRC64;
MCVCVSPGGW SVWGQWAQCS SECGGGIQTR TRTCQSPPEE LYLCEGVVEE GRPCNSQSCT
GKGRHLSRSQ SLRSVDSRKR DDVDKPRSGQ QSPQTDSTSG EEWSAWSVCS ATCGEGWQSR
TRFCVSSSYS TQCSGPLREQ RPCNNSAVCP VHGAWDEWSP WSLCSSTCGR GYRSRTRTCT
PPQFGGDPCD GPEKQTKFCN IAVCPVDGVW NEWSSWSSCS ASCSNGTMQR TRECNGPSYG
GSECRGEWLE TVDCFLGECP VDGKWQPWSL WSGCSKTCGG GNQQRNRICY GPFFGGQSCP
GEQEEIRRCN EKRCPELYEI CGEDNFSNVV WKMTAAGDTA AVRCPPNAIG LILRRCTLDE
EGIAYWENPT YMKCISNDYR SIQTLTREHL SKAQRGLVGD GVSEVMNKLR VTSSEGTSYS
GDLLAIVDVL KNMTEIFRRA YYSPSSADMR NFVQSVSNLL MEENRERWEE AQLLGPNIKE
LFRLVEDFVD VIGLRMKDFQ DMYEVTDNLV LSIHKRPVVG QADISFPMKG WRGMVDWARN
SEDRVTIPKN ILSTGQPDSD DSSTFVTGIV LYRNLGSILT LQRNSTVLNS KVLSVTIKPT
PASLSAPVVV EFSHLYNGTT NQTCISWDES DSASLLGSWS ARGCKAVLVD SFRTKCVCDR
LSTFAILARL NPEMNMDKTQ LPSVTLIVGC GVSSLTLLLL IIIYVSVWRY IRSERSVILI
NFCLSIISSN ALILIGQTQT RNKVLCTLIA AFLHFFFLSS FCWVLTEAWQ SYMAVTGRLR
NRIIRKRFLC LGWGLPALVV AISVGFTKAK GYGTPSYCWL SLEGGLLYAF VGPAAAVVLV
NMVIGILVFN KLVSKDGITD MKLKERAGAS LWSSCVVLPL LALTWMSAVL AITDRRSALF
QILFAVFDSL EGFVIVMVHC ILRREVQEAV KCRVVDRQED ANGDSGGSFQ NGHAQLMTDF
EKDVDMACRS GTMKRSSLQG EEKASSGTLT LQKGSNFNTM PASMAKVHLQ NVADYTSHTL
TLRREKGAAK GISTELPGAK SIYICDGELF KQLDGDLPRG NGEGSSSEGA GKGPGYVILP
TNNTGTLKPA KGKEEQTAKY NMGIEQLPQT RLIHLANPAS GEPVPGFGLQ SLPADQVSVS
CSDRDSPAHN LQNMSRDSQV ANNMCDGGES GNSGVMSKSE TVSTLSMSSL ERRKSRYAEL
DFEKIMHTRK RHQDMFQDLN RKIHSADKDR ESPPVDAKAA KRWSVSSASS DKTNMSVKSL
TLFCSAPPSP ISSVSLFSYD QHKLPRLSGV ACLIVSAAIL KIAFFNMPIV SVPEQ
//
