ID A0A3B3H636_ORYLA Unreviewed; 1518 AA.
AC A0A3B3H636;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=plch2a {ECO:0000313|Ensembl:ENSORLP00000027389.1};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000027389.1, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000027389.1, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000027389.1,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000027389.1}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000027389.1};
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 RefSeq; XP_011475993.1; XM_011477691.1.
DR STRING; 8090.ENSORLP00000027389; -.
DR Ensembl; ENSORLT00000047081.1; ENSORLP00000027389.1; ENSORLG00000016877.3.
DR GeneTree; ENSGT00940000158374; -.
DR InParanoid; A0A3B3H636; -.
DR Proteomes; UP000001038; Chromosome 7.
DR Bgee; ENSORLG00000016877; Expressed in ovary and 10 other cell types or tissues.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
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:UP000001038};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 191..226
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 227..263
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 656..769
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 770..899
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 489..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1167..1232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1278..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1489..1518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..518
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..997
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1489..1508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1518 AA; 169400 MW; 63E149652B4BA23A CRC64;
MTGSENFYDL ARAWSLKEWQ SRIQIYATWS KVWEPPRASL RYPNSVYGWA SGRRSAGTQP
RGTVEKCMSS MQMGTQMVKL RGGSKGLVRF FFLDEHKSCI RWRPSRKNEK AKISIDSIRE
VCEGKRSEIF QRYAEGSFNQ NCCFSLYYGE HMESLDLVSG TGEDARTWIT GLKYLMAGIS
DEDSLAKRQR TRDQWLKQTF TEADKNGDGS LSINEVLQLL HKLNVNLPRQ KVKQMFKEAD
TDDNQGTLDF EEFCSFYKMM STRRDLYLLM LTYSNHKDHM DTDDLTRFLE HEQKMTKVTK
DHCLEIINKF EPCSENQKQG VLGIDGFTNY MRSPAGDIFN PEHYSVSQDM TQPLCNYFIA
SSHNTYLMGD QLMSQSRVDM YAWVLQAGCR CVEVDCWDGQ DGEPIVHHGY TLTSKILFRD
VVETINKYAF IKNDYPVILS IENHCSVPQQ KKMAQYLTEI LGDKLDVSSI KVDESGQLPS
PESLRGKILV KGKKLPPNID ENAEEGDVSD EDSADEMEDD CKLMNGDTTA NRKQVENMAK
KKLDSLMKES KIRDCEDPDS FTIGALPPAG KPGENRGCKG KSDDSTDTTD EAHPSSSKRS
GRSFIGSFSK RKKKASKLKK TSSFEDTDTD QESSSASRAP PSHSKKKKTM KLSRALSDLV
KYTCSVGLYD IEAQAGCSWQ VSSLSETKAH QVMQQKATSF ILFNQRQLSR IYPSSYRVDS
SNFNPQPFWN AGCQLVALNY QSEGRVLQLN RAKFYSNGNC GYILKPTCMC EGAFNPNLED
PVPGRMKKQL VLKIISGQQL PKPKDSMLGD RGEIIDPFVE VEIIGLPVDC CKEQTRVVDD
NGFNPMWEET LVFMVHMPEL ALVRFLVWDH DPIGQDFIGQ RTISFNSMMP GYRHVYLEGM
EEASIFVHVA VNDISGKARA ASGIKGLFHR NPKQSSLDSH AAVQQGRKHP FGAHLLRRTA
SAPTRGQPKV RKGFPEMDTK DYSSEGASEE RDSEDKASAT ASFQFTPPRH HNGESLSPPR
RKGSWEHPDS NGAFCPEGGK DCSLPQNPAP PPHPPAPTAG DGQIFTPGPD QRASPHHLTS
TATVSLKEAT RSILCPPLTG KPEHHSQTNI VSSSSGKDLP RLHDEGTLLE SQHAEANLAP
SHPMLPQGTP TAHAAPLAHT RRALFSDLPG HTPMRRAKSE GHVRAPPAPS GPVQSVVPEV
STDATANDRL WSKLEPGSHR DSMSSSSSIS SNDTVIDLSL SNLAWRSHAH PPSSTAEPPW
INYRHSALVC YEVPRVDKSK SNPNLQQSDC STPERGQDAL KDPPVELGGR RHSWSRLYME
GLKNSSGRGS SSAAAPSMSK SLGDLTSDDI SCNFDSKYRS INRSFVVRSN REQHRRGGLT
RPAPQNNLTE QLRRLTDVEP LTARDFAYQT QDQQEDAVDE SLVRRTSSRS QSRVRYIANR
AKKAQERQRL QGLLQGRSAS FSHPVSPIEE RGNPEGACCV TRSPCSGLDM LSRPNSTESP
SPAQTEPGNS EVFLRLKL
//
