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Database: UniProt
Entry: A0A2T7PEV8_POMCA
LinkDB: A0A2T7PEV8_POMCA
Original site: A0A2T7PEV8_POMCA 
ID   A0A2T7PEV8_POMCA        Unreviewed;      1149 AA.
AC   A0A2T7PEV8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=G-protein coupled receptors family 1 profile domain-containing protein {ECO:0000259|PROSITE:PS50262};
GN   ORFNames=C0Q70_07378 {ECO:0000313|EMBL:PVD31952.1};
OS   Pomacea canaliculata (Golden apple snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX   NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD31952.1, ECO:0000313|Proteomes:UP000245119};
RN   [1] {ECO:0000313|EMBL:PVD31952.1, ECO:0000313|Proteomes:UP000245119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD31952.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PVD31952.1};
RA   Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA   Zhang G., Qian W., Fan W.;
RT   "The genome of golden apple snail Pomacea canaliculata provides insight
RT   into stress tolerance and invasive adaptation.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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:PVD31952.1}.
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DR   EMBL; PZQS01000004; PVD31952.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7PEV8; -.
DR   STRING; 400727.A0A2T7PEV8; -.
DR   Proteomes; UP000245119; Miscellaneous, Linkage group lg4.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   CDD; cd15137; 7tmA_Relaxin_R; 1.
DR   CDD; cd00112; LDLa; 9.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 11.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR24372; GLYCOPROTEIN HORMONE RECEPTOR; 1.
DR   PANTHER; PTHR24372:SF77; GPR INSULIN LIKE RECEPTOR 1; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   Pfam; PF00057; Ldl_recept_a; 6.
DR   Pfam; PF00560; LRR_1; 1.
DR   Pfam; PF13855; LRR_8; 2.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00192; LDLa; 12.
DR   SMART; SM00369; LRR_TYP; 6.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 9.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS01209; LDLRA_1; 5.
DR   PROSITE; PS50068; LDLRA_2; 10.
DR   PROSITE; PS51450; LRR; 2.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124};
KW   G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000245119};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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        802..825
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        837..860
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        926..946
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        976..1001
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1022..1043
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1055..1083
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          818..1074
FT                   /note="G-protein coupled receptors family 1 profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50262"
FT   DISULFID        111..123
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        118..136
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        130..145
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        150..162
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        157..175
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        169..184
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        189..201
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        196..214
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        266..278
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        273..291
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        367..385
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        379..394
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        401..413
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        408..426
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        420..435
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        440..452
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        447..465
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        459..474
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        482..494
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        526..538
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        533..551
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   1149 AA;  129543 MW;  7E9425505A4A405B CRC64;
     MSLTFNCLDV CGGVLASPPQ TSTNLNKLHL VEAVDRTCLP DSRQQLRKWA DGTFTNGEVV
     EDEDATKSLC AEDWSFKCDE SMQECIDPKF LCNGVSECLN GRDESVEQCG CLPNEFQCNR
     SHCIDVIKRC DLTDDCQDGS DERNCETYLC PLTHVKCTNH FCVPRDLMCD YVDDCGDNSD
     EAQCEPRECA QTEFRCNNSE CVSMNYICDG QPDCKDHSDE LPESCERNFK CPTGLYILQS
     LVCDGWEDCV FTHADEFHCE LLQNLCRSDE FRCNSSRCIS RNAVCDGVCD CINTCEDENG
     CRNYGCKLGE GYLCRTTHRC LAPDLVCDGH NDCKNTQNGM DEHFCQTGKT NCNGLPVAEF
     GENPLLCDSG QCVPDSTLCD HYMDCLDGKD EENCDSTFKP CEENQFQCSN KQCIHKSARC
     DGKPDCIDRT DEVDCGDEPC PQHTRRCGGG QCVSETKWCD FERDCPDGSD EMSCRPEMHP
     QCTASQFRCS SGQCVDQDVV CYDGKAAKNR GCKDNSHLIN CTTHSCKEGQ FKCRRSYCVD
     SGQRCDGVVD CLMAAWDEHG CAFKCPYYSP VCICEGEDIH CENKQLTTLP HIERKAEPFS
     NHFSGNRLEL TADTFVGLDR MTYLDLSNNS LESIPDGCFQ KLWRLVYLNL KNNKLHILTN
     GTFQGLSNLR TLFLEGNEIG TIVPHAFVGL ASLTSLDLSK HRLSKIPQNA FVGLRNLHVL
     SLSQNLIDTI ANGAFNGLDN LLSLDLSQNV IVLVEKNVFH GMGKLDTLYT DGFWFCCLAG
     RVPHCYPEPD EFSSCEDLMS NYVLRVSIWV LGMVASFGNL LVIGWRARDM RCGKVHSFLI
     TNLALGDFFM GVYLLIIAVV DSYYRGVYII YDRSWRTSDL CRFSGFISTF SSELSVFTLT
     VITLDRLVCI IFPLKLKRLG LKQATIVMLM VWLAVFIVSI LPLLGFDYFR EFYGRSGVCL
     ALHVTPDRPP GWEYSVAIFL VLNFASFLLI FFSYLWMFFI AKRTRSAVRS SESKNDSAMA
     RRMTLIVMTD FCCWVPIILL GFASLGGARS SNEVYAWIAV FVLPLNSAIN PILYTISTAP
     FLGNVRKRAS RFRKSFISSF TMDNTKHSYV DDRTTNSYYD RKSPYRQMDL IRMRSLNRSP
     LNSHSESDI
//
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