ID A0A1S3MIX6_SALSA Unreviewed; 1570 AA.
AC A0A1S3MIX6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=LOC106572832 {ECO:0000313|RefSeq:XP_014002826.1};
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_014002826.1};
RN [1] {ECO:0000313|RefSeq:XP_014002826.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014002826.1};
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_014002826.1; XM_014147351.1.
DR STRING; 8030.ENSSSAP00000083278; -.
DR PaxDb; 8030-ENSSSAP00000083278; -.
DR GeneID; 106572832; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000087266; Chromosome ssa15.
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; 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; 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; 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 19..127
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 141..176
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 177..213
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 606..720
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 721..850
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 445..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1223..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1299..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1412..1431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1450..1524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..467
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1467..1510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1570 AA; 174284 MW; 76F46B6E10BE88C6 CRC64;
MELSGVAVLP QRYMEKCMSS MQTGTQMVKL RGGSRGLVRY FYLDQHKSCI RWRPSRKNEK
AKISIDSIRE VCEGKQSEIF QRYSDGSFDP NCCFSLYYGE RLESLDLVSS TGEEARTWIT
GLKYLVAGIS DEDSLAKRQR TRDQWLKQTF AEADKNGDGS LSIGEVLHLL HKLNVNLPRQ
KVKQMFKEAD TDDNQGTLGF EEFCSFYKMM STRRDLYLLM LTYSNHMDHL DTSNLARFLE
LDQKMTKVTK DHCLEIVNKF EPCPENQMQG VLGIDGFTSY MRSPAGDIFN PEHNVVTQDM
SQPLCNYFIA SSHNTYLMGD QLMSQSRLDM YAWVLQAGCR CVEVDCWDGQ DGDPIVHHGY
TLTSKILFKD VIETINKYAF VRNDYPVILS LENHCSVPQQ KKMAQYLVEV MGDKLDLSAI
KADERGRLPS PDTLKGKILI KGKKLPSNID EDNEEGDVTD EDSADEMEDD CKLINGATSM
TRKQVENVAK KKLDNLMKES KIRDQEDPDS FTIAAQPPSG KTTNKSPSKG KGDDGAEIGD
EANPSTNKRL GRTFMGSFSK RKKKAVKLKK TNSLEDTDTD QESTSSTSRV PLHHSRKKTM
KLTRALSDLV KYTKSVGVSD IEKQAASFSW QVSSLSETKA HQIMQQKAAT FIHFNQRQLS
RVYPSSYRVD SSNFNPQPFW NAGCHLVALN YQSEGRVLQL NRAKFNSNGN CGYILKPACM
CEGAFNPMIE DPFPGQMKKQ LVLKIISGQQ LPKPKDSMLG DRGEIIDPFV EVEIIGLPVD
CCKEQTRVVD DNGFNPMWEE TLVFTLHMPE LALVRFLVWD HDPIGQDFIG QRTIAFNSMI
PGYRHVYLEG MEAASIFVHV SVHDITGKGK VTSGIKGLFH RNPKQASLDS HAAAQLSHKH
TFGAHLLRRT ASAPTKVLPK VKKGFPEIAI DTKDYRSEGT SEDRELEDSH LIASSQPPLL
HQGTWDTTAA VAPAASRQGT NRHHGTNEAF LPDEGKDHST VQRPAPPIRL LAPISDELGD
RHLTHSSSTP ADHSSTRHSP RLPLPISTAI TIFTSSPASK CEADSPVNGR GEEGPVNGRV
DNKRPPAHHS TTSAPVTHDP KDLKPSQYSR DPRVDDGTSS LMEHSPSRAE APYTQSGHTK
DDAELKTEPT AESPVALAYP SVYASPLKVQ SLRALFGSSP LNTPVRMTKI EDHVQAVAGE
QQQSSAMPEV CIDATLNDRL WSKLEPKPGS HRDSVSSSSS ISSNDTVIDL SLPNLARKSL
TCLSNGTSPG DNIFPDPPSW VNRPRSAIAS FETLQVSKSN PNLLQGHLGE PEDELQPRPL
GAPREPPVDS PSRITQRRHT WSRLYMEGLK HSSPPAKKPS AAAALAAAAT SPLDTVASMS
KSLGDLTSDD IACNFDSKYR SITRSFIIRP SRNDLRQGYP NHNPQRPRPP SYLTEQLRRL
TDVEPLTAHD FAPQVPLEEP QEEPLLRRTS SRSQSRVRYI ANRAKQAQER QRLQGLNQSH
PATGAANASI SGGGSPMEER GNPEGACCVA QSPCTSLDLL SQLSPPGPPN RLSQTSLNSD
NNEVFFMLKL
//
