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Database: UniProt
Entry: A0A3R7P558_PENVA
LinkDB: A0A3R7P558_PENVA
Original site: A0A3R7P558_PENVA 
ID   A0A3R7P558_PENVA        Unreviewed;      1661 AA.
AC   A0A3R7P558;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=G-protein coupled receptor 64 {ECO:0000313|EMBL:ROT61522.1};
GN   ORFNames=C7M84_020685 {ECO:0000313|EMBL:ROT61522.1};
OS   Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC   Penaeoidea; Penaeidae; Penaeus.
OX   NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT61522.1, ECO:0000313|Proteomes:UP000283509};
RN   [1] {ECO:0000313|EMBL:ROT61522.1, ECO:0000313|Proteomes:UP000283509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Muscle {ECO:0000313|EMBL:ROT61522.1};
RA   Zhang X., Yuan J., Li F., Xiang J.;
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ROT61522.1, ECO:0000313|Proteomes:UP000283509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Muscle {ECO:0000313|EMBL:ROT61522.1};
RA   Sun Y., Gao Y., Yu Y.;
RT   "The decoding of complex shrimp genome reveals the adaptation for benthos
RT   swimmer, frequently molting mechanism and breeding impact on genome.";
RL   Submitted (JAN-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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:ROT61522.1}.
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DR   EMBL; QCYY01004126; ROT61522.1; -; Genomic_DNA.
DR   Proteomes; UP000283509; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   CDD; cd15040; 7tmB2_Adhesion; 1.
DR   CDD; cd00054; EGF_CA; 5.
DR   Gene3D; 2.60.220.50; -; 1.
DR   Gene3D; 2.10.25.10; Laminin; 6.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR046338; GAIN_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   PANTHER; PTHR47767; ADHESION G PROTEIN-COUPLED RECEPTOR G7; 1.
DR   PANTHER; PTHR47767:SF1; G_PROTEIN_RECEP_F2_4 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF00008; EGF; 4.
DR   PRINTS; PR01983; NOTCH.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00179; EGF_CA; 5.
DR   SUPFAM; SSF57196; EGF/Laminin; 5.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS00022; EGF_1; 6.
DR   PROSITE; PS01186; EGF_2; 6.
DR   PROSITE; PS50026; EGF_3; 6.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000313|EMBL:ROT61522.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1052..1071
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1078..1099
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1129..1147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1167..1193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1220..1243
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1249..1269
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          20..57
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          58..96
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          97..147
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          148..185
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          202..237
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          239..275
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1052..1271
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   REGION          318..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          401..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          937..962
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1288..1373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1387..1409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1529..1549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..584
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..704
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        24..34
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        47..56
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        86..95
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        137..146
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        175..184
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        206..216
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        227..236
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        265..274
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1661 AA;  176941 MW;  207135B285DBC266 CRC64;
     MPRLYQCPAP SPIPLTCPAH APDCALGVCG EGTCTLQEAA PGYACECHPG YYGPQCQHHN
     PCEPVNPCNH IGKCLNHSDG SYTCDCLHGF YGQNCSRIDP CAAVSSNPCH NGGSCVRSST
     NPQSHVRQES GEYTCLCPFG FFGGTCERRD PCSSSPCLHG SACANVTDTE FTCNCTEGYT
     GGTCEVNIDE CGSSPCTLCQ TEIDECAPSP CLRGSCVDKI GDFECDCPRG WGGKTCEVDL
     DECASSPCLN GATCIDGLDA FACACASGYG GKVCEVPESC PAHTTVLDTG EFHWPATRHG
     QTAALSCTYG LRTTIGAVPP SASPTATAEP PPADASSGAS HEASALLSSG EMSLEYEEDL
     DSSPTLLPDS DEFTTQAEWQ GGRFRISRRT RDVAAHAGNV DFSRGPAFRK DNPGARRRLV
     TSRLRGAVSR RAGRRMQRRK QQTQEEGAPD DAGQGARPPR GEHGLEGPQR PRGRPRIRGF
     RAQKQAPVAQ PRIGEGAGGS PSRRGRQFVS PPGDMPRIGE APDPPRIGDA FAEQPRIGAR
     MAQQSRGGTE VIEDYPRIGE SASDRPRIGK SLSEHPRIGE NIAEHPRIGE SLSEPPRIGE
     SLSEPPRIGE SLSEPPRIGE SQPAPPIGES QPAPPRVGES ASGPPRLSER ASQRQRPAGG
     ARELPRIGET LSGRSEERIP LQSLGDALHG DSEGGEEVDV EPQAVRAKDG AAPGARSPEE
     TAAPEHSRAS SAGAGSPRAI PVLGSEIMKL QKADKPDTTP PPTIGPARSH VQAGAVRACV
     LLPNGTVAWQ EPDTEMCRGK EAQAAENAAM SIATLTASPA SVSSALFTRA AKELAKLVEH
     ALHDRAVSGG ARAGRSFCGL VAKNMVSAIS NMMEVNDSVV AEGDRDSNIT QQLVGTINSF
     TESVPLEVGE KVEFRSNNLV VEARMLRSDS SDAILFQPQL QETSTSRRKR EVNSSETSQP
     KDSYLKLPPA VLSMATGESV RLEFVSFGND KFFRGSRPLG MPVITARITN TTVKNLSEPV
     TYTIAEANTN ANESLFRPSC VYWDDAGGSG KIVMNLSLAL LLLNCVFFIT TQVKPSSIAC
     TALGAALHYL VLAAFAWMLV EAANMYQLLI TVFASAETHF MAKRVVGAWG VPLMVVVTAL
     AVDYRVYQDE ARDICVINPR HNVIVYYAAY MGPICCVLAV NCVVFVMVTR VLCQRRPRSH
     KPHSSSVTPK REGPVTLAQV RGAVTVVALL GVTWVAGAVS IGWARLTLQY IFCITTPLQG
     LIIFVVRVAQ HPEARAAWIA LLTTGTLRRR PPTTHTHSTH SSAHTHSTTS TPPRNHHSSA
     RTVSTRASPL NSVKKSSSTV RNGSTKRSRG ASKNGSVYRS ASGPMDSASR NSGMGTLLSR
     IVSRLNSGGL EPHASPRAER GAGETSAAAK TALHTMPTGC PPPALSPQLY ESEAFFSQAL
     LDETYYQHSA MNGHAQRPHS LVLLRTESHG GAAKSQPPVV PQPFVGSQIP ALLSPNQQLQ
     TLLNAGVPPA MIPRRSLGSL MLLGEGKEGD DSSWHFVRPP PDGRSDPMDN DLPYDERNDV
     AARTPTAFRR TAILETSKRR TTTTTTATES GCVVLAGQRV ATRASPIIMA DEGKEASPFS
     ALTRANSEMQ MGSPAVGAAT LRRTASVYTL GEWEDPRSSQ A
//
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