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Database: UniProt
Entry: A0A3B4GG65_9CICH
LinkDB: A0A3B4GG65_9CICH
Original site: A0A3B4GG65_9CICH 
ID   A0A3B4GG65_9CICH        Unreviewed;      1378 AA.
AC   A0A3B4GG65;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Adhesion G protein-coupled receptor A2 {ECO:0000313|Ensembl:ENSPNYP00000021129.1};
OS   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000021129.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000021129.1}
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}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       Adhesion G-protein coupled receptor (ADGR) subfamily.
CC       {ECO:0000256|ARBA:ARBA00007343}.
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DR   STRING; 303518.ENSPNYP00000021129; -.
DR   Ensembl; ENSPNYT00000021638.1; ENSPNYP00000021129.1; ENSPNYG00000015829.1.
DR   GeneTree; ENSGT00940000158941; -.
DR   Proteomes; UP000261460; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:1990909; C:Wnt signalosome; IEA:Ensembl.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0022009; P:central nervous system vasculogenesis; IEA:Ensembl.
DR   GO; GO:1990791; P:dorsal root ganglion development; IEA:Ensembl.
DR   GO; GO:0002040; P:sprouting angiogenesis; IEA:Ensembl.
DR   Gene3D; 2.60.220.50; -; 1.
DR   Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   InterPro; IPR046338; GAIN_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
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; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR45930:SF1; ADHESION G PROTEIN-COUPLED RECEPTOR A2; 1.
DR   PANTHER; PTHR45930; G-PROTEIN COUPLED RECEPTOR 124-LIKE PROTEIN; 1.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF00560; LRR_1; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00369; LRR_TYP; 4.
DR   SUPFAM; SSF111418; Hormone receptor domain; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
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; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51450; LRR; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
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        763..784
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        796..819
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        831..852
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        879..897
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        917..937
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        998..1021
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1027..1046
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          249..353
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          336..430
FT                   /note="G-protein coupled receptors family 2 profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50227"
FT   DOMAIN          757..1052
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   REGION          1096..1123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1137..1201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1262..1289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1354..1378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1096..1121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1137..1194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1262..1280
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1378 AA;  149803 MW;  25F66DC6CEE00870 CRC64;
     LLQLSSPEVR SSRRTMFAPG VGIPLLPGRL VLMLLLLPRL YQACPGLLAS TSGCSCAEER
     PKLHSVQAVG IRVSCSKGEL TELPDPGLLP NRTVTLILSH NKIRVLRNGS FLGLYALDKL
     DLKHNLISTI MPGAFQSLSE LRKLDLSNNR IGCLTADMFQ GLTNLTKLNL SGNIISTMNP
     GVFEELPSLK LVNFNSDYLT CDCELQWVPN FFRGSPARLG EETLCAYPMS LRGKPLRGLR
     EGHLSCDGPL ELHTMSLLPS QRQVVFKGDR LPFHCAAALV DKMTTLHWRH NGQPVTTDPE
     MGVQLESSVV HDCTFITSAK TLILYDVHVE ASGEWECVVS TGRGNKSLTV EIVVLENSAS
     FCPEDKVVNN RGEFRWPRTL AGITSHQYCL QLRYPSLSVE GGMEQKKASR YCDRTGKWED
     GDYSNCHYTN GITRVLHTFI LRPINASNVV TVAHQVRTYT LEAAGFTDSV DVLYMAQIME
     KFMEYVTQIK ELLAVMVEMG SNLMQVDEQI LALAQREKRA CSSIVNSLET LAWSQLHSNA
     KEFSMMSKNI VMEAHLIQPA HFTGITCTAH QQREVSVGNL GMETSESVHE QQLRVHCSTG
     AHNTSLNNFF LKNSVALASV TLPANLFASD AAADCKLQFV AFRTGSFFPL TGNSSTTTEH
     SRRRTVNSPV VFVGLDGCSM QNNSDPIWVS LRHLSPGTDA MAAHWSLKGP EKQGGWSQEG
     CQLVRSDSNT STMRCSLLSN YAVLQEVPDF PSSPLTVRVL HPVVYACTAV LLLCLFTIII
     THILHHSSIC ISRKSWHTLL NTCFHIAMTT AIYAGGISLT SYPVVCQAVG IALHYSSLST
     LLWIGVSARV IYKEAVWRMP RQPDGESPVP PTQRPMLRFY LIADGVPLII CGITAAVNVN
     DYGDNSPYCW LVRRSSLGSF FVPAGLVVLV TWIYFLCTVF RLRRRGAKEC TGTTLSSPVT
     ESHPALAGST SLLSTDSVTG PVHPVMSPED QYSLKTQFSV LVATHFLFVA LWSCAAMAVW
     FTGHTSLLFS CLYGIVATVL GGFLVVHHCF RRQDVQTSWL ACCPGYQRPH PMSTYTHTCT
     TGSGVQTSEQ GSQLFINCHP PGDSHNSSSA RSSSTPSGIS SVGPGPCKLT NLLQATQDNS
     NGTSRAPTGN NTSTSTDNIT KPTNNVLPTI NSAAPGQPQR RKASSRTKQG SSQYYHRGEG
     RGHYRLKALR AAGGGGSLGA LGPIGLDHLS SSHAVYKQAT SENGSIHHSL SENQASVLTN
     GKRVGESVAT SPSEGSDGGS SGSRKPFPLL PSMASRVAMQ NAQRRCASRD NLKVAASAET
     KRCSYPLNGD TATVPGAAGQ NGNLKNSVLE LEQDMSGTDQ SQSSVGMKSG LWKSETTV
//
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