ID A0A087Y2W8_POEFO Unreviewed; 1383 AA.
AC A0A087Y2W8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Adhesion G protein-coupled receptor A2 {ECO:0000313|Ensembl:ENSPFOP00000012371.1};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000012371.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000012371.1}
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 EMBL; AYCK01000950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01000951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01000952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007563790.1; XM_007563728.2.
DR STRING; 48698.ENSPFOP00000012371; -.
DR Ensembl; ENSPFOT00000012388.1; ENSPFOP00000012371.1; ENSPFOG00000012392.1.
DR GeneID; 103146020; -.
DR KEGG; pfor:103146020; -.
DR CTD; 25960; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000158941; -.
DR OMA; CAEDRPK; -.
DR OrthoDB; 2900279at2759; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; IPR000483; Cys-rich_flank_reg_C.
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; IPR017983; GPCR_2_secretin-like_CS.
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; PF13895; Ig_2; 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 SMART; SM00082; LRRCT; 1.
DR SUPFAM; SSF111418; Hormone receptor domain; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 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; 3.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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 Reference proteome {ECO:0000313|Proteomes:UP000028760};
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 21..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 767..788
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 800..823
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 835..856
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 881..901
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 921..941
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1002..1025
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1031..1050
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 254..356
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 339..433
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 761..1056
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 1106..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1265..1314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1360..1383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1265..1283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1299..1313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1383 AA; 150135 MW; 87FB2122CC42F21D CRC64;
MTGGGGAAEV RSRRRTMVAP AAGIPLLPGR LVLMLLLLSA SGAGLVQVCP GPLASTSGCS
CAEDRPKAHG AQSVGRRVSC SKEELVELPD FSLFPNRTVT LILSHNKIRV LRNGSFIGLN
SLEKLDLKHN LISTIMPGAF QGLSELRKLD LSNNRIGCLT TDMFLGLTNL TKLNLSGNII
STLDPGVFEE LPSLKQVNFV SDYLSCDCGL RWMPSFLRSS SVRVGEDTLC AFPRTLRGKP
LRGLRESQLS CDGPLELHTL SLLPSQRQVV FRGDRLPFHC TAALMDKLTS IHWRHNGQVV
TSDPDRGVQL EDSVVHDCTF ITSELILSNV HVEASGEWEC VVTTGRGNAS RTVEIVVLEN
SASFCPEDKV LNNRGEFRWP RTLAGITSHQ YCLQLRYPSL SVEGVTEQKK ASRYCDRSGK
WHEGDYSNCQ YTNGITRVLH TFILTPINAS NAVTVAHQVR TYTLEVAGFT DSVDVLYIAQ
IMEKFMEYVR QLRELSEVIV DMGSNLMQVD DQILALAQRE KRACSSIVYS LETLAWPQLH
GGAQDFSVVS KNIVMEAHLI RPAHFTGITC TAYYHRELPT GRPGVETSES APQQLLHFRC
STGSHNVSLT NFPLKNSVAL ASVTVPATLF PPDAAADCKL QFVAFRTGSF FPLLPNSSNA
VEQSRRRSVN TPVIFVGLDG CTMWNYSDHI WVSLRHLTPG TDAVAAQWSH TEPGKLGGWS
QQGCQLVHTD SSTSLMHCSV LGNYAVLQEV PTFPNSSLVS VRVLHPVVYA CTAVLLLCLF
TIIITHILHH SSIQISRKSW HTLLNTCFHI AMTSAIYAGG ISLTSYPLVC QAVGIALHYS
SLSTLLWIGV SARVIYKEAV WRTPRQTEGE SSPPPTQRPM LRFYLIADGV PLIICGITAA
VNVNNYGDNS PYCWLIWRSS LGSFFVPAGL VVLVTWIYFL CTVLRLRHRV SKECTGTTLS
SPGTEGHPAL AGSTSLLSTD SAGRPITPAA PPEDQYSLKT QFSILVATHF LFAALWCCGA
MAVWLTGRAS LLFSCLYGIV ATVLGVFLVV HHCFRRRDVQ TSWLGCCPGY RRSHPMSTYT
NTCTTVSGVQ TSEQGSQLFI NCHPPADSHN SSSARSSSTP SGISSVGPGP CKLTNLLQVA
QDNPSNASRV PTSNNTSTST DNITKPTNNV LPSINSSAPV HPQRKKVSSR TKQGSSQHYH
RGEGRGHYRL KALRTAGGGS LGALGPTGSE HLNSSHAFYK QATSENGSIH HSLSENQATL
LTNGKRVGES AATSPSEGSD GGSSGSRKPF PLPPSAASRV AMHSNQRRCS SRDNLKVAAS
AERETKRCSY PLNCVANTVP GAAAPNGTLK ISVLELEQDM SGTDQSQSSV GMKTGLWKSE
TTV
//
