AGRB2_PONAB
ID AGRB2_PONAB Reviewed; 1485 AA.
AC Q5R7Y0;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Adhesion G protein-coupled receptor B2;
DE AltName: Full=Brain-specific angiogenesis inhibitor 2;
DE Flags: Precursor;
GN Name=ADGRB2; Synonyms=BAI2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Orphan G-protein coupled receptor involved in cell adhesion
CC and probably in cell-cell interactions. Activates NFAT-signaling
CC pathway, a transcription factor, via the G-protein GNAZ. Involved in
CC angiogenesis inhibition (By similarity). {ECO:0000250|UniProtKB:O60241,
CC ECO:0000250|UniProtKB:Q8CGM1}.
CC -!- ACTIVITY REGULATION: Receptor activity is regulated by proteolytic
CC processing. The long N-terminal has a an inhibitory effect on the
CC constitutive signaling activity. Removal of the N-terminal region
CC induces an increase of the receptor activity.
CC {ECO:0000250|UniProtKB:O60241}.
CC -!- SUBUNIT: Heterodimer of 2 chains generated by proteolytic processing;
CC the large extracellular N-terminal fragment and the membrane-bound C-
CC terminal fragment predominantly remain associated and non-covalently
CC linked. Interacts with GABPB2 (By similarity). Interacts (via carboxy-
CC terminus) with TAX1BP3. Interacts with GNAZ. Interacts with SH3GL2 (By
CC similarity). {ECO:0000250|UniProtKB:O60241,
CC ECO:0000250|UniProtKB:Q8CGM1}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O60241};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:O60241}.
CC -!- PTM: Proteolytic processes at the GPS domain; this cleavage modulates
CC receptor activity. Additionally, furin is involved in the cleavage at
CC another site, in the middle of the extracellular domain, generating a
CC soluble fragment. {ECO:0000250|UniProtKB:O60241}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH92130.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR859978; CAH92130.1; ALT_INIT; mRNA.
DR RefSeq; NP_001126245.1; NM_001132773.1.
DR AlphaFoldDB; Q5R7Y0; -.
DR SMR; Q5R7Y0; -.
DR STRING; 9601.ENSPPYP00000001855; -.
DR MEROPS; P02.029; -.
DR GeneID; 100173216; -.
DR KEGG; pon:100173216; -.
DR CTD; 576; -.
DR eggNOG; ENOG502QRKJ; Eukaryota.
DR InParanoid; Q5R7Y0; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0033173; P:calcineurin-NFAT signaling cascade; ISS:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:InterPro.
DR Gene3D; 2.20.100.10; -; 3.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR043838; AGRB_N.
DR InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
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 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; 3.
DR PRINTS; PR01694; BAIPRECURSOR.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00209; TSP1; 3.
DR SUPFAM; SSF82895; SSF82895; 3.
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; 3.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1485
FT /note="Adhesion G protein-coupled receptor B2"
FT /id="PRO_0000245614"
FT TOPO_DOM 21..869
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 870..890
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 891..898
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 899..919
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 920..927
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 928..948
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 949..969
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 970..990
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 991..1011
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1012..1032
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1033..1053
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1054..1074
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1075..1080
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1081..1101
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1102..1485
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 297..350
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 352..405
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 408..461
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 463..516
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 804..856
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 217..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1259..1285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1323..1354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1398..1485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 284..285
FT /note="Cleavage; by furin"
FT /evidence="ECO:0000250|UniProtKB:O60241"
FT MOD_RES 1251
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGM1"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 800
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 309..344
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 313..349
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 324..334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 364..399
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 368..404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 379..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 420..455
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 424..460
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 435..445
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 467..502
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 490..520
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 807..839
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 827..841
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
SQ SEQUENCE 1485 AA; 162022 MW; 3FCE3D9B8197C278 CRC64;
MTPACPLLLS VILSLRLAAA FDPAPSACSA LASGVLYGAF SLQDLFPTIA SGCSWTLENP
DPTKYSLYLR FNRQEQVCAH FAPRLLPLDH YLVNFTCLRP SPEEAVTQAE SEVGRPEEEE
AEAAAGLELC SGAGPFTFLH FDKNFVQLCL SAEPSEAPRL LAPAALAFRF VEVLLINNNN
SSQFTCGVLC RWSEECGRAA GRACGFAQPG CSCPGEAGAG SATTTSPGPP AAHTLSNALV
PGGPAPPAEA DLHSGSSNDL FTTEMRYGEE PEEEPKVKTQ WPRSADEPGL YMAQTVHGVW
EEWGSWSLCS RSCGRGSRSR MRTCVPPQHG GKACEGPELQ TKLCSMAACP VEGQWLEWGP
WGPCSTSCAN GTQQRSRKCS VAGPAWATCT GALTDTRECS NLECPATDSK WGPWNAWSLC
SKTCDTGWQR RFRMCQATGT QGYPCEGTGE EVKPCSEKRC PAFHEMCRDE YVMLMTWKKA
AAGEIIYNKC PPNASGSASR RCLLSAQGVA YWGLPSFARC ISHEYRYLYL SLREHLAKGQ
RMLAGEGMSQ VVRSLQELLA RRTYYSGDLL FSVDILRNVT DTFKRATYVP SADDVQRFFQ
VVSFMVDAEN KEKWDDAQQV SPGSVHLLRV VEDFIHLVGD ALKAFQSSLI VTDNLVISIQ
REPVSAVSSD ITFPMRGRRG MKDWVRHSED RLFLPKEVLS LSSPGKPATS GAAGSPGRGR
GPGTVPPGPG HSHQRLLPAD PDESSYFVIG AVLYRTLGLI LPPPRPPLAV ASRVMTVTVR
PPTQPPAEPL ITVELSYIIN GTTDPHCASW DYSRADASSG DWDTENCQTL ETQAAHTRCQ
CQHLSTFAVL AQPPKDLTLE LAGSPSVPLV IGCAVSCMAL LTLLAIYAAF WRFVKSERSI
ILLNFCLSIL ASNILILVGQ SRVLSKGVCT MTAAFLHFFF LSSFCWVLTE AWQSYLAVIG
RMRTRLVRKR FLCLGWGLPA LVVAVSVGFT RTKGYGTSSY CWLSLEGGLL YAFVGPAAVI
VLVNMLIGII VFNKLMARDG ISDKSKKQRA GASLWSSCVV LPLLALTWMS AVLAMTDRRS
VLFQALFAVF NSAQGFVITA VHCFLRREVQ DVVKCQMGVC RADESEDSPD SCKNGQLQIL
SDFEKDVDLA CQTVLFKEVN TCNPSTITGT LSRLSLDEDE EPKSCLVGPE GSLSFSPLPG
NILVPMAASP GLGEPPPPQE ANPVYMCGEG GLRQLDLTWL RPTEPGSEGD YMVLPRRTLS
LQPGGGGGGG EDAPRARPEG TPRRAAKTVA HTEGYPSFLS VDHSGLGLGP AYGSLQNPYG
MTFQPPPPTP SARQVPEPGE RSRTMPRTVP GSTMKMGSLE RKKLRYSDLD FEKVMHTRKR
HSELYHELNQ KFHTFDRYRS QSTAKREKRW SVSSGGAAER SVCADKPSPG ERPSLSQHRR
HQSWSTFKSM TLGSLPPKPR ERLTLHRAAA WEPTEPPDGD FQTEV
