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Database: UniProt
Entry: A0A3P8UW42_CYNSE
LinkDB: A0A3P8UW42_CYNSE
Original site: A0A3P8UW42_CYNSE 
ID   A0A3P8UW42_CYNSE        Unreviewed;      1522 AA.
AC   A0A3P8UW42;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|ARBA:ARBA00012368, ECO:0000256|RuleBase:RU361133};
DE            EC=3.1.4.11 {ECO:0000256|ARBA:ARBA00012368, ECO:0000256|RuleBase:RU361133};
OS   Cynoglossus semilaevis (Tongue sole).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC   Cynoglossinae; Cynoglossus.
OX   NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000006582.1, ECO:0000313|Proteomes:UP000265120};
RN   [1] {ECO:0000313|Ensembl:ENSCSEP00000006582.1, ECO:0000313|Proteomes:UP000265120}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24487278;
RA   Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA   Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA   Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA   Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA   Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA   Zhao Y., Schartl M., Tang Q., Wang J.;
RT   "Whole-genome sequence of a flatfish provides insights into ZW sex
RT   chromosome evolution and adaptation to a benthic lifestyle.";
RL   Nat. Genet. 46:253-260(2014).
RN   [2] {ECO:0000313|Ensembl:ENSCSEP00000006582.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC         bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-
CC         diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456,
CC         ChEBI:CHEBI:203600; EC=3.1.4.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00023674};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC         Evidence={ECO:0000256|ARBA:ARBA00023674};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR   Ensembl; ENSCSET00000006655.1; ENSCSEP00000006582.1; ENSCSEG00000004211.1.
DR   GeneTree; ENSGT00940000158374; -.
DR   Proteomes; UP000265120; Chromosome 10.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00275; C2_PLC_like; 1.
DR   CDD; cd16221; EFh_PI-PLCeta2; 1.
DR   CDD; cd13364; PH_PLC_eta; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 2.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR001192; PI-PLC_fam.
DR   InterPro; IPR046971; PLC-eta2_EFh.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR015359; PLC_EF-hand-like.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR   PANTHER; PTHR10336:SF166; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE ETA-2; 1.
DR   PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF09279; EF-hand_like; 1.
DR   Pfam; PF16457; PH_12; 1.
DR   Pfam; PF00388; PI-PLC-X; 1.
DR   Pfam; PF00387; PI-PLC-Y; 1.
DR   PRINTS; PR00390; PHPHLIPASEC.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00148; PLCXc; 1.
DR   SMART; SM00149; PLCYc; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361133};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|RuleBase:RU361133};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|RuleBase:RU361133};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265120};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT   DOMAIN          142..177
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          178..214
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          608..721
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   DOMAIN          722..851
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          446..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          497..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          910..1105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1257..1294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1307..1336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1360..1425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1443..1522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..469
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..511
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        524..543
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        937..955
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        971..990
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1034..1057
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1074..1105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1360..1384
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1401..1418
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1443..1469
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1485..1501
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1522 AA;  170234 MW;  DCAB839F5E721ECF CRC64;
     MEISSNIRSL SPEQVEKCMS SMQMGTQMVK LRGGSKGLVR FFYLDEHKSC IRWRPSRKNE
     KAKISIDSIR EVCEGKQSEI FQRYAEGSFD PNCCFSLYYG EHVESLDLVS GTGEEARTWI
     TGLKYLMAGI SDEDSLAKRQ RTRDQWLKQT FAEADKNGDG SLSISEVLQL LHKLNVNLPR
     QKVKQMFKEA DTDDNQGTLG FEEFCYFYKM MSTRRDLYLL MLTYSNHKDH LNSDDLARFL
     ETEQKMTKVT KEHCLEIINK FEPCSENQKE GVLGIDGFTN YMRSPAGDIF NPDHYDINQD
     MNQPLCNYFI ASSHNTYLMG DQLMSQSRVD MYAWVLQAGC RCVEVDCWDG QDNEPIVHHG
     YTLTSKILFK DVIETINKYA FVKNDYPVIL SIENHCSVPQ QKKMAQYLVE ILGDKLDLSS
     VKADESGWLP SPEALKGKIL VKGKKLPPNI DEDAEEGDVS DEDSADEMEE DCKLMNGDTS
     ANRKQVENMA KKKLDSLMKE SKIRDREDPD NFTITALPPS GKSTDKTRKQ KGKTEDGADT
     ADEANPSNKH TSRSFINSFS KRKKKTTKLK KTSSFEDTDT DPESTSSASR APSHHSKKKK
     TMKLSRALSD LVKYTRSVGF YDIEAQANCS WQVSSLSETK AHQLMQQKAM SFIKFNQRQL
     SRIYPSSYRV DSSNFNPQPF WNAGCQLVAL NYQSDGRVLQ LNRAKFYSNG NCGYIIKPAC
     MCEGIFNPNL EDPLPNQMRK QLVLKIISGQ QLPKPKDSML GDRGEIIDPF VEVEIIGLPV
     DCCKEQTRVV DDNGFNPMWE ETLVFTVHMP ELALIRFLVW DHDPIGQDFI GQRTIAFNSM
     MPGYRHVYLE GMEEASIFVH VAVHDITGKA RAASGIKGLF HRNPKQASLD SHAAAQQGRK
     HPFGAHLLRR TASAPTKGQP KVKKGFPEIT IDTKEYSSEG ASEERESDDR DKASAAASHQ
     PTPPQHHAGD SLASHPDKGP RDHPDTNGAF HPEEAKVCSS VQRPLPPPPP SFVLKSEDPK
     NTDFIRSVSP PKGSPFSHHA STTPLPLPST AITTDSPVPA PPTGAVDSPV KMNMESSKPG
     TFCRTPPVQI EQNSRDTPNK RNTLPFTENT QTQIENQETL PEKKIEASST LTACSSVQAR
     RALFTNPTSR TPVRRTKSEG HVRVAVTPPD HRQSAIPEVC TDATMNDRLW RKLEPSSHRD
     SMSSSSSISS SDTVIDLSLP NLARKSLTSL PAANSSPWVN CRHSGLLSYD TLLVGKSKSN
     PNLQQSQNQD DELKPRPLQP SQEASFDSPN RLTQRRHTWS RLYMEGLKQS SGSKPLSAAT
     TPTATSSMSK SLGDLTSDDI SCNFDSKYRS ISRSFIVRPN REQLRRASPH KSRPTSDLTE
     QLRKLTDVEP LTPNDFSPVN RPKDSQEEEV DETMVRRTSS RSQSRVRYIA NRAKKAQERL
     RLQGLTQGRS ASFSLSSSVG SSSSASPIEE RGNPEGACCV ARSPCSSLDQ LSQLAPLGSP
     SPRLSQSPPD PENSEVFFML KL
//
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