ID A0A3B3S0B7_9TELE Unreviewed; 1498 AA.
AC A0A3B3S0B7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Adhesion G protein-coupled receptor B1 {ECO:0000313|Ensembl:ENSPKIP00000024179.1};
GN Name=ADGRB1 {ECO:0000313|Ensembl:ENSPKIP00000024179.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000024179.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000024179.1}
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}.
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DR Ensembl; ENSPKIT00000004882.1; ENSPKIP00000024179.1; ENSPKIG00000007428.1.
DR GeneTree; ENSGT00940000157432; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
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; 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; 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; PF19188; AGRB_N; 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; SM00209; TSP1; 5.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 5.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50092; TSP1; 5.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1498
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017457133"
FT TRANSMEM 873..899
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 911..930
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 942..960
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 981..1000
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1020..1043
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1064..1086
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 876..1117
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 1419..1460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1419..1441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1498 AA; 164112 MW; 907E3BB7CC25B69A CRC64;
MTPTFVLSAC MALLLLGPAS STPSGPASET CVTLVQGRFF GFFSSTTAFP SAPCSWTLQN
PDPRRYTVFV KVTKPTESCQ PRRLKTFQFD SFLDTSRTFL GMESFDEVVK LCDASAPVAF
LQSNKQFLQM RKILPQEGPA LIEGDGEFKA EYLVVGNRNP SMPACQMLCQ WLEACLATST
NANPCGIMHT PCACASAHWY SGDGAGLQTG RAGGSTQCLT VGWFSQSLIG SCDPGGWSAW
GRWSECSSEC GGGTQTRSRT CQSNLEEGFL CEGVVEEGRP CNPQPCTGKS ALRSRSQSLR
ALDSRKRENT DAARFGNLAP HTDALTDEWS TWSECSATCG QAWQTRTRFC TTSSSSAPCS
GPLRENRPCN TTACPLHGVW DEWSPWSLCS STCGRGYRDR SRICKQPQFG GNPCTGPEKQ
TKFCNIAVCP GELDGAWTEW SRWTSCSTTC SNGTMQRTRE CNGPSYGGAE CRGDWLDTQN
CFLADCPVNG KWQPWGSWGS CSRSCGGGSQ VRRRFCSGPF FGGVPCPGNR EEQRKCNEKR
CPEPHEICGE ETFADVIWKK TPAGDTAAVH CPPNASGLIL RRVFLFQTQR GMQGDGISEV
LAKLKATSDD GTSYSGDLLA IIEILKNMTD LFKGPSYSPS AVDVQNFARS ISNLLMEENR
EKWEEAQMLV PNIKELFRLV EDFVEVIGLQ MEDFQDTYEA TDNLVLSIHK RPATVTSDIN
FPVRGWRGMM EWVRKSEDKV TITQNAVSTA IPEAINSSYV TGIVLYRNLG SVLSLQRNTT
VLNSKVVSVT VRPTPDFLPS PIEIEFAHAY NSTTNQTCIS WDESESSSLL GSWSARSCRA
VPLDAHRTKC VCERLSTFAI LAQLSPDMNM DKAALPSVTM IVGCGVSTLT LLLLIIIYVS
VWRYIRSERS VILINFCLSI ICSNALILVG QTQARSKLGC TMVAALLHFF FLSSFCWVLT
EAWQSYMAVT GRLRNRIIRK RFLCLGWGLP ALVVAVSVGF TKAKGYGTVN YCWLSLEGGL
LYSFVGPAAA VVLVNMIIGI LVFNKLVSKD GITDVKLKER AGASLWSSCV VLPLLALTWM
SAVLAITDRR SALFQILFAV FDSLEGFIIV MVHCILRREV QEAVKCRVVD RKDDGNGDGS
GSHKNGHTQL MVRTKTWLLF IQEAVNPTAC SLTSLTIFRT LKRPMPPSEE KSAPPPMSAP
KGSFHTLPGS IAKAPLPSVP DYASHTLTLK REKSRGGPGG EASGGRSVYV CDSELFKQLD
AELGRGPVPG GAPDGSGYVI LPNSTSTLRS KPKDDQGKYN ISIEQLPQTR FVHLSNPFSE
PASGFGLPSD RVSVSYSERD SPVQNLHNLS SESQMTGSLC DAGDSVNSMT KSETISSLSM
SSLEVRGQGL RLTSSLWCGK VMHTRKRHQD MFQDLNRKMQ HAEKERESPP SDSKDKPQTP
SDRAWEGVPK PHSPPAWVCP ELEPLQASPL ELQTVEWEKA SASIPLVGQE IIDLQTEV
//
