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
//