ID A0A1S3R837_SALSA Unreviewed; 827 AA.
AC A0A1S3R837;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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};
GN Name=LOC106600791 {ECO:0000313|RefSeq:XP_014047924.1};
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_014047924.1};
RN [1] {ECO:0000313|RefSeq:XP_014047924.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014047924.1};
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|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 RefSeq; XP_014047924.1; XM_014192449.1.
DR AlphaFoldDB; A0A1S3R837; -.
DR STRING; 8030.ENSSSAP00000038492; -.
DR PaxDb; 8030-ENSSSAP00000038492; -.
DR KEGG; sasa:106600791; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000087266; Chromosome ssa03.
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; cd16218; EFh_PI-PLCdelta3; 1.
DR CDD; cd13363; PH_PLC_delta; 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; 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; 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; IPR039504; PLC-delta3_EF-hand.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF33; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA-3; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF14788; EF-hand_10; 1.
DR Pfam; PF00169; PH; 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; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
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:UP000087266};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 41..152
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 198..233
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 234..269
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 543..657
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 658..787
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 93840 MW; 21F39E762926FAC8 CRC64;
MLGRSKKPPT AVHHEPKAVE SQPKTQDPLR RLGVLDDENV RAMMHGSNMV KVRSQRWQKS
RSLRLLEDGV TVWCESTKSS RKAKAQQTFS VTEVECVREG CQSEALRRLS GSVPENQCFT
VVFRGARKSL DLLCSCEEEA RRWVKGIRTL KERVANMTQK EKLDQYPLPP PWAFVALCQA
ASFRLKRFGM LPWLLSLTPH TWIRGYLRRA DENDDGKMSY DEVKCLLQMI NIDLNEQYAR
SLFKKADRSC DGRLDHVEIE EFCRELMRRP ELDAVFRHYS GNGCVLSTAE LRDFLGDQGE
DASLIHAQSL IRTYELNDWA QKNQFMTQNG FTVYMLSLEN DVFNPDHARV HQDMTRPLAH
YFISSSHNTY LTKDQVTSAS SAEPYIRALN QGCRCVELDC WDGDKGEPVI YHGHTLTSKV
PFKEVIETIA QYAFKASPYP LILSIENHCT VEQQTVMARH LRTILGKRLL TKPLKDQPLK
DLPSPEELRG RILVKGKKDV HHLNQLGKTS SFDTSSDDEA SSRNKKDKKD PAKAVSSKLS
PELSELVVYC RSVPFRGFQH STQKPPNEMS SFNENDALKH IKDTGKLFVR HNSRQLSRIY
PSGQRLQSSN YDPQDMWNGG CSMVALNFQT PGEQMDLNQG RFLPNGRCGY ILKPSFLCSP
SSHFNPEITG GGPGHIPTQL TIRIISAQQL PKINTDKPNS IVDPQVWVEI HGVAIDNSRD
KTHRIDNNGF NPRWDSTLSF QLQVPELALV RFVVEDHDHK ARNDFVGQYT LPFTSLRTGY
RHVHLLKADG SSLSPSTLFI HVKVSGKGVP IKTVSERMAL AKSNGKA
//