ID A0A2Y9IWU2_ENHLU Unreviewed; 1096 AA.
AC A0A2Y9IWU2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN Name=LOC111141861 {ECO:0000313|RefSeq:XP_022350415.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022350415.1};
RN [1] {ECO:0000313|RefSeq:XP_022350415.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022350415.1};
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};
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DR RefSeq; XP_022350415.1; XM_022494707.1.
DR AlphaFoldDB; A0A2Y9IWU2; -.
DR STRING; 391180.A0A2Y9IWU2; -.
DR KEGG; elk:111141861; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000248482; Unplaced.
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 CDD; cd08597; PI-PLCc_PRIP_metazoa; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
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; 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:SF102; INACTIVE PHOSPHOLIPASE C-LIKE PROTEIN 1; 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; 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; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 114..224
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 586..702
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 702..831
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1096
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1096 AA; 122856 MW; 3F3EC8E827885600 CRC64;
MAEGAAGREG PAPPDAAGCE DDPRVGPDAA SGEGVAGAPG GRWRDRRSGV ALPGAAGAPA
DSEAGLLEAV RATPRRSSII KDPSNQKCGG RKKTVSFSSM PSEKKISSAS DCISFMQAGC
ELKKVRPNSR IYNRFFTLDT DLQALRWEPS KKDLEKAKLD ISAIKEIRLG KNTETFRNNG
LADQICEDCA FSILHGENYE SLDLVANSAD VANIWVSGLR YLVSRSKQPL DFMEDNQNTP
RFMWLKTVFE AADVDGNGIM LEDTCVELIK QLNPTLKESK IRLKFKEIQK SKEKLTTRVT
EEEFCEAFCE LCTRPEVYFL LVQISKNKEY LDANDLMLFL EAEQGVTHIT EDMCLDIIRR
YELSEEGRQK GFLAIDGFTQ YLLSPECDIF DPEQKKVAQD MTQPLSHYYI NASHNTYLIE
DQFRGPADIN GYVRALKMGC RSIELDVSDG SDNEPILCNR NNVTTHLSFR SVIEVINKFA
FVASEYPLIL CLGNHCSLPQ QKIMVQQMKK VFGDKLYTEA PLPSETYLPS PEKLKRMIIV
KGKKLPSDPD ILEGEVTDED EEAEMSRRLS VDYNGEQKQI LLCRELSDLV SICKSVQYRD
FELSMKSQNY WEMCSFSETE ASRIANEYPE DFVNYNKRFL SRIYPSAMRI DSSNLNPQDF
WNCGCQIVAM NFQTPGPMMD LHTGWFLQNG GCGYVLRPSI MRDEVSYFSA NTKGIVPGVS
PLALHIKIIS GQNFPKPKGA CAKGDVIDPY VCIEIHGIPA DCSEQRTKTV QQNSDNPIFD
ETFEFQVNLP ELAMIRFVVL DDDYIGDEFI GQYTIPFECL QPGYRHVPLR SFVGDIMEHV
TLFVHIAITN RSGGGKAQKR SLSVRMGKKV REYTMLRNIG LKTIDDIFKI AVHPLREAID
MRENMQNAIV SIKELCGLPP IASLKQCLLT LSSRLITSDN TPSVSLVMKD NFPYLEPLGA
IPDVQKKMLA AYDLMIQESR FLIEMADTVQ EKIVQCQKAG MEFHEELHNL GSKEGLKGRK
LNKATESFAW NITVLKGQGD LLKNAKNEAV ENMKQIQLAC LSCGLSKAPS SGAEAKSKRS
LEAIEEKESS EENGKL
//
