ID A0A452F795_CAPHI Unreviewed; 1560 AA.
AC A0A452F795;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Adhesion G protein-coupled receptor B1 {ECO:0000313|Ensembl:ENSCHIP00000020126.1};
GN Name=ADGRB1 {ECO:0000313|Ensembl:ENSCHIP00000020126.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000020126.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000020126.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000020126.1}
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 EMBL; LWLT01000011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9925.ENSCHIP00000020126; -.
DR Ensembl; ENSCHIT00000027955.1; ENSCHIP00000020126.1; ENSCHIG00000018848.1.
DR GeneTree; ENSGT00940000157432; -.
DR Proteomes; UP000291000; Chromosome 14.
DR Bgee; ENSCHIG00000018848; Expressed in frontal cortex and 13 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
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:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IEA:Ensembl.
DR CDD; cd15251; 7tmB2_BAI_Adhesion_VII; 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; 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; PF02793; HRM; 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:UP000291000};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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 SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1560
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019565073"
FT TRANSMEM 943..964
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 976..995
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1007..1025
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1046..1065
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1085..1108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1129..1151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 562..632
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 941..1182
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 312..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1371..1530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1418
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1560 AA; 170399 MW; DDA93D000536EB77 CRC64;
MRGQAAAPGA LWILGPLLLL LLGRQAGTAA GTAAGPGAEP CATLVQGKFF GYFSAAAVFP
ANASRCSWTL RNPDPRRYTL YMKVAKAPAC SGPARVRTYQ FDSFLESTRT YLGVESFDEV
LRLCDPSAPL AFLQASKQFL QMQRLRPPQD NTLGARDGPP GPSDDFSVEY LVVGNRNPSR
AACQMLCRWL DACLAGSRSS HPCGIMQTPC ACLGGDTSDP ASGSLAPRGD VCLRDGVAGG
PENCLTSLTQ DRGEDGAPGG WKLWSLWGEC TRDCGGGLQT RTRTCLPAPG IEGGGCEGVL
EEGRLCNRKA CGPAGRTNSR SQSLRSTDAR RREELGDDLQ QFGFPAPQTG DPAAEEWSPW
SVCSSTCGEG WQTRTRFCVS SSYSTQCSGP LREQRLCNNS AVCPVHGAWD EWSPWSLCSS
TCGRGFRDRT RTCRPPQFGG NPCEGPEKQT KFCNIALCPV DGNWNEWSSW STCSASCSQG
RQQRTRECNG PSYGGAECQG HWVETRDCFL QQCPVDGKWQ AWASWGSCSV TCGGGTQRRE
RACLGPFFGG AACQGPQDEY RQCGAQRCPE PHEICDEDNF GAVVWKETPA GEVAAVRCPR
NATGLILRRC ELDEEGIAYW EPPTYIRCVS IDYRNIQMMT REHLAKAQRG LPGEGVSEVI
QTLVEISQDG TSYSGDLLST IDVLRNMTEI FRRAYYSPTP GDVQNFVQII SNLLAEENRD
KWEEAQLMGP NAKELFRLVE DFVDVIGFRM KDLRDAYQVT DNLVLSIHKL PASGATDISF
PMKGWRATGD WAKVPEDRVT VSKSVFSTGL AEADDSSVFV VGTVLYRNLG SFLALQRNTT
VLNSKVISVT VKPPPRSLLT PLEIEFAHMY NGTTNQTCIL WDETDPPSSP APPQLGPWSW
RGCRTVPLDA LRTRCLCDRL STFAILAQLS ADASMEKAAA PSVTLIVGCG VSSLTLLMLI
IIYVSVWRYI RSERSVILIN FCLSIISSNA LILIGQTQTR NKAVCTLVAA FLHFFFLSSF
CWVLTEAWQS YMAVTGRLRN RLVRKRFLCL GWGLPALVVA ISVGFTKARG YSTMNYCWLS
LEGGLLYAFV GPAAAVVLVN MVIGILVFNK LVSKDGITDK KLKERAGASL WSSCVVLPLL
ALTWMSAVLA VTDRRSALFQ ILFAVFDSLE GFVIVMVHCI LRREVQDAVK CRVVDRQEEG
NGDSGGSFQN GHAQLMVGFG AGTQTAPDIA ACRTATITGT LKRPSLPEEE KLKLAHAKAP
SNFNSLPANV SKLHLHGSPR CPGGPLPDFP NHSLTLKKDR VPKSSFVGDG DIFKKLDSEL
SRAQEKALDT SYVILPTATA TLRPKPPEEP KYSIHIDQMP QTRLIHLSMA PDAGLPARSP
PSRQPPSTPT TPAPAAPPPQ QPLPPPPPLE PAPPSVGEPG EPAAHQGPST GPGTKTENVS
TLSVSSLERR KSRYAELDFE KIMHTRKRHQ DMFQDLNRKL QHAEKDKDVL GPDSKPEKQQ
TPNKRPWESL RKAHGPPAWV KKELEPLPPS PLELRSVEWE KSGATIPLVG QDIIDLQTEV
//
