ID A0A1D2NCI0_ORCCI Unreviewed; 1211 AA.
AC A0A1D2NCI0;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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 ORFNames=Ocin01_03717 {ECO:0000313|EMBL:ODN02952.1};
OS Orchesella cincta (Springtail) (Podura cincta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX NCBI_TaxID=48709 {ECO:0000313|EMBL:ODN02952.1, ECO:0000313|Proteomes:UP000094527};
RN [1] {ECO:0000313|EMBL:ODN02952.1, ECO:0000313|Proteomes:UP000094527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Mixed pool {ECO:0000313|EMBL:ODN02952.1};
RX PubMed=27289101; DOI=10.1093/gbe/evw134;
RA Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA Smit S., van Straalen N.M., Roelofs D.;
RT "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT in the Genome of the Collembolan Orchesella cincta.";
RL Genome Biol. Evol. 8:2106-2117(2016).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODN02952.1}.
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DR EMBL; LJIJ01000091; ODN02952.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D2NCI0; -.
DR STRING; 48709.A0A1D2NCI0; -.
DR OMA; YMRNPLY; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000094527; Unassembled WGS sequence.
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:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0060429; P:epithelium development; IEA:UniProt.
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; cd16201; EFh_PI-PLCgamma; 1.
DR CDD; cd13362; PH_PLC_gamma; 1.
DR CDD; cd08592; PI-PLCc_gamma; 1.
DR CDD; cd10341; SH2_N-SH2_PLC_gamma_like; 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 Gene3D; 3.30.505.10; SH2 domain; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR035024; PLC-gamma_N-SH2.
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 InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10336:SF159; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR Pfam; PF00017; SH2; 2.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00239; C2; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SMART; SM00252; SH2; 2.
DR SMART; SM00326; SH3; 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 SUPFAM; SSF55550; SH2 domain; 2.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
DR PROSITE; PS50001; SH2; 2.
DR PROSITE; PS50002; SH3; 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 Reference proteome {ECO:0000313|Proteomes:UP000094527};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 175..210
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 541..643
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 654..743
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 775..845
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 950..1067
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 1071..1187
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 509..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1211 AA; 139746 MW; AF45BCFBB7E27D17 CRC64;
MNFIPELEQV INQLERGTVV TKFFLRKRPE KRTLSIRRET RQIIWHRWKW WYVPRSLCEG
AVDVREIKLV RPGKSSKDFD RWPEDSKRHD AGKCLVIFYG SEFRLRTLSL AALSEKESDL
WIRGLNFLCT DTAKIPYPLQ LNMWLRKEFY AMANHRGNIT LKEMKSFLPR VNCKMSTNKL
RDMFQSVDTR KSGEVGFDDF SALFHDQLVH DRSIFDEYFA EKYSNDRNLI STREFESFLK
TEQKEVVVDV CTVIREYLQD PLRDVQLPEL TVPEFLDYLY SKQNEIWDSR NSHVSQDMTR
PISHYWIASS HNTYLTGDQF SSESSVEAYT RCLLQGCRCV ELDLWDGNDG IPFIFHGHTL
TTKIKFVDVL KAIKEYAFAA SDFPVILSLE DHCTLPQQRK MAQKFQEIFG DMLVTQSLDK
NETQLPSPEQ LKRRIILKHK KLPENGTIEE VPAKLPDEVS KEMDLSNTIR NGVMYLKDDT
GLEWIPHFFV LTGTRLLYTE MTSDDDIGDD ASVIADDDDP HDASNSKKKT NEEELHFSEK
WFHGRLKGGR NAANELIQQY APHLGEGCFL VRESENFVGD FTISFWRSGR THHAHIHSKY
EWGQVKYYLV DSLTFDSLYS LITHYRSNPI KGLEFHVKLG EPVPQPMSHE GKPWFHTNLD
RNGAEELLRK VPIDGAYLVR AISHNDARFA ISFRFQKAIK HCVIKEEGRL FMIGANKFES
LTDLISHYEK YPFYKKVRLT QAVNEDYVQS VGVNFDEDVY THTDYLDTNM LCSEGNNLRV
RAIYEYRARR TDELSFMKDD IISNVIKEDK DWWRGTLLTQ TDAFGTPGAL VQGWFPANYV
HELEPEECPD DDEEQTPLGS LQKGSVEMTL GAYVEINKNS SGDGMPFVIK IYTDGTGSGT
GSTPCIILGL KSEPDAKEWC EAIRETAQSA SDRENKNKRI ERMNRIAKEL SSLIVYCCSV
NKFNMDRVRS KGRVFYEMYS FPETAAEKQM LGLDRPFFMC HHQVQLSRVY PKGQRLDSSN
YNPVPLWNAG CQMVALNYQT PDKPMQLNQG KFRQNGGCGY ILRPDFMFKT SEEELALSAS
SEPIIVSLTI LGARHLSKSG RGIVSPFVEV EIIGNTSESR KTKTISDNGL NPFWNESFEF
EVHFPELAMI RFVVQDEDVF GDPNFIGQAS YPVPCVREGY RSVPLQNGYS EELELSSLLV
HYSVKRPPNF V
//
