ID A0A3B3TN15_9TELE Unreviewed; 1320 AA.
AC A0A3B3TN15;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Adhesion G protein-coupled receptor A3 {ECO:0000313|Ensembl:ENSPLAP00000001669.1};
GN Name=ADGRA3 {ECO:0000313|Ensembl:ENSPLAP00000001669.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000001669.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000001669.1}
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 Ensembl; ENSPLAT00000014356.1; ENSPLAP00000001669.1; ENSPLAG00000002802.1.
DR GeneTree; ENSGT00940000157235; -.
DR Proteomes; UP000261500; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
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; 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:SF2; ADHESION G PROTEIN-COUPLED RECEPTOR A3; 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; PF13855; LRR_8; 1.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00369; LRR_TYP; 3.
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; 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.
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, 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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1320
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017331515"
FT TRANSMEM 721..741
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 753..775
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 787..810
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 836..856
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 876..899
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 975..996
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1008..1027
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 218..316
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 299..394
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 719..903
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 910..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1229..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1320 AA; 146061 MW; 55EA0BAD9BDE61EF CRC64;
MRLDWLQLVV VLLLSGLRGS AVPFACKTSD EGPKSGGKSP ASDRKVVCSN MELHQVLPAD
SFPNRTVILI LNNNKIQELR NGAFSGLSTL EKLNLFYCSF FPPLLSMFYR DLSNNSISCL
NGDVFKGLDS LSRLNLSGNM FSSLAQGMFD RLVSLKALEF QTPYLLCDCN LRWLLRWIKD
RNVSVKNTKC SYPQSLQGQL ITSLRTELLT CDAPLELPSF QLTPSHRQVV FQGDSLPFQC
QASLVAEDMQ VLWYQNGRMV KPDATQGIFI EKRVVQNCSL IASALTISNI QPGFTGNWEC
RVRTSRGNTT RTVHIVVLQS SAKSCAPERI SNNKGEFRWP RTPAGIKAYL PCNSPTSSAR
AYSGVPSEER QAWRHCSPEG QWMEGDYSQC QFQKEVTRGL YVINQMPLNE TNVVIKAQSL
LVYTIDAANL SDKMDIIFMA EMIEKFGKFV EKFKDLGEVM VNMASNLMLA DERVLWMAQR
EAMACSRIIA CLQKISVYRL ATAQAFSLTS PNIALEAHTV RVNDWNGMTC MLFQRPSPER
LPGHDRQLTF KCNTTGSFAS VLYKSTVVEA SLQLPRSLFS QVATPGQTDD NVYKLYLLGF
RNGKFFPSTG NNSLLADGGR KRSVATPVIM AKMDGVALRS LKTPINITLR RFARGSDAVS
ARWNFSLAGD QGGWRSEGCR ILENHDNFTT MSCNSLGNYG LLMDLNTIEQ FSPSIQPLHP
VIYATSVILL LCLFTIILSY IYHYRSVRVS RKFWHMLVNL CFHMALTCGV FVGGINQTRY
ASVCQAVGIL LHYSTLATAL WVGVTARNIY KQLTRKAKRY EELDEPPPPP RPMLRFYLIG
GGIPIIVCGI TAAANIKNYG SQRYSPYCWM AWEPSIGAFY GPAGFIVFVD CMYFLSILLQ
VRRHPERRYE LKESSEEQQH LASGSSEATP EGPGSLSHPL TAQLQPNKAS SSVASAPHAV
PLSALENEHT FTAQLIGAVG ALGLYSGLWV FGAMAVSQDH PFDMAFTWLF GLTALALGAF
MVAHHCVNRQ DMRRFWLQVC CSGRPAYSVQ EEVLLPQTGI AVMSTATTEK ADGQSAKCGH
SSADSSYTNR SAPSVRNSGH GSKLTNLHAE AAQCKAASAP ATANGTAVLD NSLTEHSLDN
EIKMHVTPVE VQFRPLSNIS NPAANGSTSR HQKNRARAHR ASRLTVLREY AYDVPTSVEG
SVQSAPSRRH HYYDMAARNS RRAAYMAYRE RHQSQLQQDS SDSASLPRRS RFSEKGSGAL
KDAVPPPGSS EPENQSSKWY GLNLVTQNGG TLKKNGQAVP LVNGDGACIK TGLWKHETTV
//
