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Database: UniProt
Entry: A0A2K5CZW9_AOTNA
LinkDB: A0A2K5CZW9_AOTNA
Original site: A0A2K5CZW9_AOTNA 
ID   A0A2K5CZW9_AOTNA        Unreviewed;      1565 AA.
AC   A0A2K5CZW9;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Adhesion G protein-coupled receptor B1 {ECO:0000313|Ensembl:ENSANAP00000014233.1};
GN   Name=ADGRB1 {ECO:0000313|Ensembl:ENSANAP00000014233.1};
OS   Aotus nancymaae (Ma's night monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000014233.1, ECO:0000313|Proteomes:UP000233020};
RN   [1] {ECO:0000313|Ensembl:ENSANAP00000014233.1}
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   STRING; 37293.ENSANAP00000014233; -.
DR   Ensembl; ENSANAT00000032064.1; ENSANAP00000014233.1; ENSANAG00000025001.1.
DR   GeneTree; ENSGT00940000157432; -.
DR   Proteomes; UP000233020; Unplaced.
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; 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; 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:UP000233020};
KW   Signal {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..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..1565
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014408993"
FT   TRANSMEM        936..957
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        969..988
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1000..1018
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1039..1058
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1078..1101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1122..1144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          563..633
FT                   /note="G-protein coupled receptors family 2 profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50227"
FT   DOMAIN          934..1175
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   REGION          310..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1371..1451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1488..1529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1399..1425
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1435..1451
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1488..1524
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1565 AA;  171831 MW;  BAB31C81C120F089 CRC64;
     MRGQAAAPGP VWILAPLLLL LLGRRARAAA GADTGLVPEP CATLVQGKFF GYFSAAAVFP
     ANASRCSWTL RNPDPRRYTL YMKVAKAPVP CAGPGRVRTY QFDSFLESTR TYLGVESFDD
     VLRLCDSSAP LAFLQASKQF LQMRRQQPPR DGDLGPRAVP AGPGDDFSVE YLVVGNRSPS
     RAACQMLCRW LDACLAGSRS SHPCGIMQTP CACLGGEAGG PAAGPLAPNG DVCLRDALAG
     GPENCLTSLT QDRGGHGTTG GWKLWSLWGE CTRDCGGGLQ TRTRTCLPAQ GVEGGSCEGV
     LEEGRQCNSE ACGPAGRTSS RSQSLRSTDA RRREELGDEL QHFGFPAPQT GDPAAEEWSP
     WSVCSSTCGE GWQTRTRFCV SSSYSTQCSG PLREQRLCNN SAVCPVHGAW DEWSPWSLCS
     STCGRGFRDR TRTCRPPQFG GNPCEGPEKQ TKFCNIALCP VDGNWNEWSS WSACSASCSQ
     GRQQRTRECN GPSYGGAECQ GHWVETRDCF LQQCPVDGKW QAWASWGSCS VTCGAGSQRR
     ERVCSGPFFG GTACQGPHDE YRQCGTQRCP EPHEICDEDN FGAVIWKETP AGEVAAVRCP
     RNATGLILRR CELDEEGIAY WEPPTYIRCV SIDYRNIQMM TREHLAKAQR GLPGEGVSEV
     IQTLVEISQD GTSYSGDLLS TIDVLRNMTE IFRRAYYSPT PGDVQNFVQI LSNLLAEENR
     EKWEEAQLAG PNAKELFRLV EDFVDVIGFR MKDLRDAYQV TDNLVLSIHK LPASGATDIS
     FPMKGWRATG DWAKVPEDRV TVSKSVFSTG LAEADEASVF VVGTVLYRNL GSFLALQRNT
     TVLNSKVISV TVKPPPRSLR TPLEIEFAHM YNGTTNQTCI LWDETDQLGP WSWRGCRTVP
     LDALRTRCLC DRLSTFAILA QLSADANMEK ATLPSVTLIV GCGVSSLTLL MLVIIYVSVW
     RYIRSERSVI LINFCLSIIS SNALILIGQT QTRNKVVCTL VAAFLHFFFL SSFCWVLTEA
     WQSYMAVTGH LRNRLIRKRF LCLGWGLPAL VVAISVGFTK AKGYSTMNYC WLSLEGGLLY
     AFVGPAAAVV LVNMVIGILV FNKLVSKDGI TDKKLKERAG ASLWSSCVVL PLLALTWMSA
     VLAVTDRRSA LFQILFAVFD SLEGFVIVMV HCILRREVQD AVKCRVVDRQ EEGNGDSGGS
     FQNGHAQLMT DFEKDVDLAC RSVLNKDIAA CRTATITGTL KRPSLPEEEK LKLAHAKGPP
     TNFNSLPANV SKLHLHGSPR YPGGPLPDFP NHSLTLKRDK APKSSFVGDG DIFKKLDSEL
     SRAQEKALDT SYVILPTATA TLRPKPKEEA KYSIHIDQMP QTRLIHLSTA PDAGLPARSP
     PSRQPPRPAA TRGIHHYPAL PPPQQPLPPP PSLEPAPPSL GEPGEPAAHP GPSAGPSTKN
     ENVTTLSVSS LERRKSRYAE LDFEKIMHTR KRHQDMFQDL NRKLQHAVEK DKEVLGPESK
     PEKQQTPNKR PWESLRKAHG TPTWVKKELE PLQPSPLELR SVEWERSGAT IPLVGQDIID
     LQTEV
//
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