ID B7P4X9_IXOSC Unreviewed; 1201 AA.
AC B7P4X9;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 08-NOV-2023, entry version 118.
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};
DE Flags: Fragment;
GN ORFNames=IscW_ISCW015942 {ECO:0000313|EMBL:EEC01651.1};
OS Ixodes scapularis (Black-legged tick) (Deer tick).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=6945;
RN [1] {ECO:0000313|EMBL:EEC01651.1, ECO:0000313|Proteomes:UP000001555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wikel {ECO:0000313|Proteomes:UP000001555}, and Wikel colony
RC {ECO:0000313|EMBL:EEC01651.1};
RG Ixodes scapularis Genome Project Consortium;
RA Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT "Annotation of Ixodes scapularis.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ISCW015942-PA}
RP IDENTIFICATION.
RC STRAIN=wikel {ECO:0000313|EnsemblMetazoa:ISCW015942-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-
CC sphingosyl-1,3-cyclic phosphate + ethanolamine; Xref=Rhea:RHEA:60648,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:143891, ChEBI:CHEBI:143892;
CC Evidence={ECO:0000256|ARBA:ARBA00000110};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; ABJB010334257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010359695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB011028291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS637651; EEC01651.1; -; Genomic_DNA.
DR RefSeq; XP_002406591.1; XM_002406547.1.
DR AlphaFoldDB; B7P4X9; -.
DR STRING; 6945.B7P4X9; -.
DR PaxDb; 6945-B7P4X9; -.
DR EnsemblMetazoa; ISCW015942-RA; ISCW015942-PA; ISCW015942.
DR KEGG; isc:IscW_ISCW015942; -.
DR VEuPathDB; VectorBase:ISCI015942; -.
DR VEuPathDB; VectorBase:ISCP_004550; -.
DR VEuPathDB; VectorBase:ISCW015942; -.
DR HOGENOM; CLU_002738_5_0_1; -.
DR InParanoid; B7P4X9; -.
DR OMA; YMRNPLY; -.
DR Proteomes; UP000001555; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; 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; cd16201; EFh_PI-PLCgamma; 1.
DR CDD; cd13362; PH_PLC_gamma; 1.
DR CDD; cd08592; PI-PLCc_gamma; 1.
DR CDD; cd09932; SH2_C-SH2_PLC_gamma_like; 1.
DR CDD; cd10341; SH2_N-SH2_PLC_gamma_like; 1.
DR CDD; cd11825; SH3_PLCgamma; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
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; IPR001849; PH_domain.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR016279; PLC-gamma.
DR InterPro; IPR035023; PLC-gamma_C-SH2.
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 PIRSF; PIRSF000952; PLC-gamma; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 2.
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 1: Evidence at protein level;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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}; Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteomics identification {ECO:0007829|PeptideAtlas:B7P4X9};
KW Reference proteome {ECO:0000313|Proteomes:UP000001555};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 187..222
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 544..645
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 656..745
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 780..840
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 943..1057
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 1059..1180
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EEC01651.1"
FT NON_TER 1201
FT /evidence="ECO:0000313|EMBL:EEC01651.1"
SQ SEQUENCE 1201 AA; 139180 MW; B3EDB3C45D43CF90 CRC64;
VMAASVQQNG SVPVASSCLP EIEQIIRKLE HGTSLIKFYQ KGRPEKRTFA IKLETRQVIW
WRPVTGRTVE EGAVDLREVK EVRLGRNSKI FDRWPEDARK WDPAQCFVIF YGNTFRLKTL
SCVATSAKDC EQWIRGIRYL TSDTVTAPYP LQVERWLRKE FYSMQNPRNV ITLKDLKAFF
PRVNCKLSTN KLKEYFQEVD SKRAGEIGFE GFASLYHNLM YDNKVLTYNA IPLSACWSPF
RCLFMHKQTS YFYLHKQGEP ALEDEQSMSK FMRDYLQDPL RDAQEPYFTV PEFLDFLFSK
QNEIWDSKHN QVNQDMTQPL THYWVASSHN TYLTGDQVKS ESSTEAYARC LSMSCRCIEL
DCWDGPDGMP YVYHGHTLTT KIRFIDVIKA IKEHAFVVSE YPVILSIENH CTLPQQRKMA
NLFQEVFGEM LLTQPIERDG TRMPSPEQLK RKIIIKHKKL PEGTDEKVIV TRRGQETDVS
NAVKNGILFL EDPVDKEWRA HFFMLTQNRM YYAEEQQAQD EEDEGEGDGT GLQQQRELHF
GEKWFHGKLA GGRLKAQELL QQHSHLGDGT FLVRESDTFV GDYSLSFWRQ GKVNHCRIKS
KQERGQTKYY LIDTVAFDTL YNLISHYQTH PLRSQEFYMY LNEPVPQPNK HEGKEWYHAN
MTRTQSEELL KRVKYDGTFL VRPSEKEDSC FAISFRAENK IKHCRIKQEG RLFLIGTAQF
ESLVELVSYY EKHPLYRKVK LKYPVNEDVI RRIGTEPEES PPHAGGPAGT YMDPDSFSGA
SQMTVKALYD YRAQREDELS FCKHAIITHV VRQDGGWWRG NYGGKRHHWF PANFVEKPGC
VEFDATYSHA VHLQSGEAMP LGTLQKGSID IAGCTVGNWP GRGREWVFRI VSPTQLVPIE
IAALSREEMH DWVLKIRETA QSANDMIQQR REMERSLRLA KELSNLIIYC RSVQFCPERI
GNFTEMSSFP ETKVEKWISP QHCSFFLKYP FYDCLFSRVY PKGSRIDSSN YDPVHLWNCG
CQMVALNYQT PDRPMQLNQG RFLQNGRSGY VLRPEFMHED GYDPYDRTSL KSVHPVTLAI
KVIAARHLMK SGRGIVSPFV EIEIVGADFD CSKYKTGTIP DNGLNPIWNE AFMFDVCNPS
VALLRFVVQD EDMFGDPNFL GQVTYPVSCL RTGNLSPLKN EYSEELELAS LLIHLEVYAT
R
//
