ID A0A4D9EM62_9SAUR Unreviewed; 1307 AA.
AC A0A4D9EM62;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Adhesion G protein-coupled receptor A2 {ECO:0000313|EMBL:TFK08202.1};
GN ORFNames=DR999_PMT08872 {ECO:0000313|EMBL:TFK08202.1};
OS Platysternon megacephalum (big-headed turtle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Platysternidae; Platysternon.
OX NCBI_TaxID=55544 {ECO:0000313|EMBL:TFK08202.1, ECO:0000313|Proteomes:UP000297703};
RN [1] {ECO:0000313|EMBL:TFK08202.1, ECO:0000313|Proteomes:UP000297703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DO16091913 {ECO:0000313|EMBL:TFK08202.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TFK08202.1};
RA Gong S.;
RT "Draft genome of the big-headed turtle Platysternon megacephalum.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TFK08202.1, ECO:0000313|Proteomes:UP000297703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DO16091913 {ECO:0000313|EMBL:TFK08202.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TFK08202.1};
RA Gong S.;
RT "The genome sequence of big-headed turtle.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TFK08202.1}.
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DR EMBL; QXTE01000071; TFK08202.1; -; Genomic_DNA.
DR STRING; 55544.A0A4D9EM62; -.
DR Proteomes; UP000297703; Unassembled WGS sequence.
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:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
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; 1.
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; 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; 1.
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, ECO:0000313|EMBL:TFK08202.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000297703};
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..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1307
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5020027655"
FT TRANSMEM 751..772
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 784..804
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 810..834
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 867..888
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 908..931
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 986..1005
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1011..1034
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 234..329
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 318..413
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 748..1040
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 1130..1274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1168
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1307 AA; 144017 MW; 321635CB845238E6 CRC64;
MGSGPPRRMR CAAGLLCLAA WLCAGGARGC PAQTPRCKCV GERPKGLGLP GAARRKVICS
DQELPEPPDP RLLPNTTVTL LLSNNKITAL KNGSFFGLHA LEKLDLKNNL ISTIQPGAFL
GLSELKRLDI SNNRIGCLGA SVFQGLANLL RLNVSGNIFS SLQPGVFDEL PSLKVVDFAT
EYLTCDCNLR WTLPWSRNRS AQISDKTLCI YPSPLHAKPL RSVRESQLQC VGAPELHTHH
LIPSLRQVVF QGDRLPFQCT ATYLDSSTRI RWYHNRVLVE GDEQTGIILE ESLIHDCTFI
TSELILSNIH VSANGEWECA VSTSQGNVSK KVEIVVLETS ASYCPAERVT NNRGDFRWPR
TLGGITAYQS CLQYPFTSLA ANGGPAAEMQ ASRRCDRLGR WEEGDYSHCL YTNDITRVLY
TFVLMPINAS NALTLAHQLR VYTAEAANFS DMMDVIYVAQ MIEKFIGYVD QIKQLPAVMV
EMASNMMLVD DHILWMAQIE DKACTGIVRS VEKIAGYVLS GNSQHVAVNS RNIAFEAYLI
KPESYTGLSC TAFQKRDGGR PSLQEQEAEP LADQQLKFRC TTGRPNISLA NFHIKNSIAL
ASIQLPPSLF SASAPLSPPQ ACKVQFLVFR NGKLFRSTGN SSRLADNGKR RSVATPVIYA
GTHGCGVSNL TEPVTVSLRH FREGADPMPA HWNFEVLGGN GGWSAEGCQL ARREPNITTL
LGRHLNNFAV LMELSNFPRE APGPAEVLHP VLYTCTALLL LCLFATIITY IVNHSTIQIS
RKCWHMLLNL CFYIAMTSAV FAGGITLTNY MIVCQAVGII LHYSSLSTLL WMAVKARVLY
KEVTWKAPQQ QQEGDVPQPA PRPMLRFYLI AGGIPLIICG ITAAVNIHNY QDNNPYCWLV
WRPSLGAFYV PVAFILLITW IYFLCTGVNI WCQSKNQKDP PVPLETPPRL DGSSNLLTDS
GSISVTLNSG TPGTDVDGVY SLKMQFWALL ITHFLYIALW TFGAVAVSQR WYLNVIFSCL
YGVTAVALGL FIFIHHCARR RDVQNSWFAC CPSYRNALPM QAYVRPGMAA EEGSQIFIRC
NPEVAHSIKS SSSPSSTNST VGHCKLTNLQ VAQNQAESCP LPRPACYKET EPGNNKNASA
ARYANNVHGR RNHKSRTKQY REGKHHRLKV LRGPSSDHPS SESGSLHNSH SESYHSGRNS
PLNNSRVGPR VAAVQEGDAA LTQSEGSDGG SSGHQVPDFG RAQRRSASRD NLKQAHTIEK
ETKRRSYPLN MANQNGGLKG SKYDINLTGA ESMAGMKTGL WKSETTV
//
