ID A0A3Q3B9T5_KRYMA Unreviewed; 1879 AA.
AC A0A3Q3B9T5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-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};
GN Name=PLCH1 {ECO:0000313|Ensembl:ENSKMAP00000026528.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000026528.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000026528.1}
RP IDENTIFICATION.
RG Ensembl;
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 Ensembl; ENSKMAT00000026867.1; ENSKMAP00000026528.1; ENSKMAG00000019663.1.
DR GeneTree; ENSGT00940000157185; -.
DR OMA; QVVESHI; -.
DR Proteomes; UP000264800; Unplaced.
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; cd16220; EFh_PI-PLCeta1; 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; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR046972; PLCeta1_EF.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF51; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE ETA-1; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF13499; EF-hand_7; 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:UP000264800};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 20..128
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
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 597..709
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 711..839
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 548..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1445..1475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1634..1654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1723..1789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1739..1753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1879 AA; 210433 MW; FDC420129B795421 CRC64;
MAELEVCRNL SLERVERCMS VMQSGTQMVK VKAGSKGLVR LFYLDEHRSC IRWKPSRKSE
KAKITIDSLY KVTEGGQSDI FHRHPDGSFD HACCFTVYHG NHMESLDLVT SNAEEARTWI
TGLRYLMAGI SDEDSLARRQ RTHDQWMKQT FEEADKNGDG LLNIDEIYQL LHKLNVNLPR
RKVKQMFQEA DTDDQQGTLT YEEFSVFYKM MSLRRDLFLL MMAYSDRKDH LTADELANFL
HNEQKMTNIT SEYVAEIVDK FEVSDENKQK GVLGIEGFTS FMRSPTCDIF NPLHHELNQD
MEQPLCNYFI ASSHNTYLTG DQLLSHSKTD MYAWVLQSGC RCVEVDCWDG SDGEPMVQHG
YTLTSKIPFK SVIETINKYA FVNNQFPVIL SIENHCNIQQ QKKIAQYLRE IFGDKLDVGD
VLSRGSKTLP SPQSLQGKIL IKGKRLPAYL SADAEEGEVS DDDSADEIEE DFKLKSSNGN
GHHQVESHIR KKLDSLLKES RIGDKEDSDS FSIRALLRAT HQGLQKNLRQ SSNRVLKKSH
SRSLITTLKQ KRHSKSRLSC QTVDKEEEVQ ERSGREAGGQ FNRGGRKRKT MKLSRDLSNL
VVFTNSVASQ ECLNEGTPGD VLSFSETRAQ SLVNHRAEQF LAFNQRQLSR IYPSAYRIDS
SNFNPQFYWN VGCQLVALNY QTEGRMMQLN RAKFMVNGGI GYVLKPPPMC KGSFNPFSDD
PLPACPKKQL ILKIISGQQL PKPPDSMLGD RGEIIDPYVE VEIIGLPVDC CKEQTRVVDD
NGFNPVWEES LSFTLHMAEL ALVRFLVWDH DPIGRDFIGQ RTVAFSSLMP GYRHVYLEGL
TEASIFVHVS VHDVYGKGNQ LRGIRGFFNR SSKSSVDTNT SGLRKRSISD HLLRRTASAP
AKGRKKTKMM LSESVASISD HKNGTGPGGE GASGKEEWVE KPLQPRAPLI HRPISMPLDR
LLQGQLSICS PDKEQHDMGG DTVIRGCHFS RPRSSSVDRL LESSLTADSN ISPPLKSNRN
KKPEEASYLV VGAGEVKKED IYVNYQSELN KSTISSTETE KKHSMFLSTN SQTTSDKPET
SSNSTTFTVG PSVSSSSSSS SSYTPSSVAL NSPVRMNSGL KGPSSLHDST ISRLIDAVSL
GNEQDTCCSI SALIDQFEST VDQSNLSRAS NLRPTTPKAL ENLRSPLKTN STSPKKNPLI
SPQKVTQKTN HVNREICSPP KVSSADTCTP ALISSPETAE FEEIYTILDE EILLPVSVYN
LRKQTVHIQA DTTDRSPSSS LGSSPAKAVH SLGKGPSVAW NDVDRNWGKT EDAEDTEERV
YEEVNDLPIA LPKSDLGSST SYMKSSNNYL QIFHHSARET FTEVELNVDE DPLEMMLPYH
GNQCEGLTNP AKHDAIYQNH ESIPSYSQQK HPSSYPQPHY PKRASYASFS QFQSPVDQPS
HQLFNHHQQQ GSLQPPVHHK YTDHGPSNLG PLRQNSYPMC QSYSEVFNNN RDFSISNKQQ
RNFSGSQIHN KSQQDRPGNK QLKTERVGCF YNGFSSGEGL SGQCAVSGNI STERGLYSPS
FECETLYSQL DYDCILPSTE PCASQNIQPQ NQSQTKLYGH KQFGIRKNHL VNNKLLPHSE
TRVPLHSDLE SSSAYLQSAT TDSKTPSPCK SKSLGDLTSE DISCNFQSKY HIISRSFVTS
HMRKQKHKGT MGEATFHSQS LDPLTEQLRK LVSLEADDGV RESLRPPQLQ QEAKHQARSL
SPNDSRDLDD SPPTLTRRLS SRSQSRVRHI NSRARERQQE ALKPRPGVVI NSTSSIGGVV
RRNKPALQNL TPNRHSTGSY IAGYLGELDD RGLPEGACTS VRYGNGDSLG DLFYTDSSLP
PVNTSHSSSE PEVYFLLRL
//
