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Database: UniProt
Entry: A0A1S3R932_SALSA
LinkDB: A0A1S3R932_SALSA
Original site: A0A1S3R932_SALSA 
ID   A0A1S3R932_SALSA        Unreviewed;      1080 AA.
AC   A0A1S3R932;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE            EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN   Name=LOC106601024 {ECO:0000313|RefSeq:XP_014048352.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014048352.1};
RN   [1] {ECO:0000313|RefSeq:XP_014048352.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014048352.1};
RG   RefSeq;
RL   Submitted (NOV-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|RuleBase:RU361133};
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DR   RefSeq; XP_014048352.1; XM_014192877.1.
DR   AlphaFoldDB; A0A1S3R932; -.
DR   GeneID; 106601024; -.
DR   OrthoDB; 2900494at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa03.
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; cd16206; EFh_PRIP; 1.
DR   CDD; cd13364; PH_PLC_eta; 1.
DR   CDD; cd08597; PI-PLCc_PRIP_metazoa; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
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; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR001192; PI-PLC_fam.
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:SF85; PHOSPHOINOSITIDE PHOSPHOLIPASE C; 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; 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; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|RuleBase:RU361133};
KW   Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT   DOMAIN          15..125
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          492..608
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   DOMAIN          608..737
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          973..1035
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1047..1080
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1080 AA;  122150 MW;  31F74C632BE331D5 CRC64;
     MPNDRKINST AACMAFMMEG CEMKKVRSNS RMYNRYFLLD PDMHWLRWEP SKKDSEKAKL
     EIKSIKEVRL GKKTPVLRSN GLSDQFPDEC AFSIIYGDNY ESLDLVASTA DVVSTWVMGL
     RYLVSYGRHT VDVVEPSQPS LRTSWIGSVF ELADMERNGH IDLFRATQII KGLNPGMKES
     RIELKFKELQ KAKDQYGEDI DMETFVEAYC ELCTRPEIFF LLVQFSSNKE YLDSKDLLLF
     VEVEQGMEGV TEDMCRDIVQ KYEPSAEGRQ KASLSIDGFT HYLLSSECHI FDPQHKRVCQ
     DMSQPLSHYY INSSHNASLL EDHFWGSSDI SSYIRTLKMG CRSLEVIVWD GPDNEPVVYV
     GNSVASQLAL CKVLDIINQY AFESSEYPLI VCLVTHCCIP QQRVMAQHMK KILGDKLYLD
     APSSEDHYLP SPEELKGKIL LKGKRLPPNY PESEGEVTDE EEGLEMSRRV GADDKDHLNG
     LSCKRLRLCK ELSDLVSLCK SVQFRDFDIS KRDQKYWEMC SFNEVDANRF ANEFPEDFVC
     YNKRFLSRVY PTPMRIDASN MNPQDFWKCG CQIVAMNYQT PGLMMDLNLG WFRQNGNCGY
     VLRPAIMREE VSYFSANARE SLPGVSAQLL HIKVISGQNL PKPRGSAAKG DVVEPYIYAE
     IHGIPADCAE QRTKTVSQNG DNPVFDESFE FQINLPELAA LRFVVLDDDY IGDEFIGQYT
     IPFECLQPGY RHVPLQSLTG EFLPNCTLFV HVAITNRRGG GKAHKRGLSV RKGKKAREYT
     SSKTTGIKVV DELFRASTQP LREATDLREN VQNAMVSFKE LCGLTPAANM KQCILTVSTW
     LMNSERALRV TVDLSQAYPT MEAQGPVPEL LRKVLNAYNM MIQTSRTLIE SADVVYSKLT
     QAQRAGLDFH VDLHRIGAKE GLKGRKLQKA MESYAWNITV LKGQADLLKH AKSEALDTLR
     QIHCATQSCG LSKNGATSPQ LQHPPLQAQA QYQAQPHHSP QSHHLQPQAQ TQPQAQPLSQ
     HLAEPQPEAQ SQLQAQLHTQ HHPLTQRLLL PPLPPQPPQY RAAGSHDAIS ENETASDGSC
//
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