ID A0A2K6KPI4_RHIBE Unreviewed; 969 AA.
AC A0A2K6KPI4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN Name=PLCL1 {ECO:0000313|Ensembl:ENSRBIP00000013192.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000013192.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000013192.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000013192.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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|RuleBase:RU361133};
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DR AlphaFoldDB; A0A2K6KPI4; -.
DR Ensembl; ENSRBIT00000036950.1; ENSRBIP00000013192.1; ENSRBIG00000030591.1.
DR GeneTree; ENSGT00940000158407; -.
DR OMA; CNRNSMT; -.
DR Proteomes; UP000233180; 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; cd16222; EFh_PRIP1; 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:UP000233180};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 30..140
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 502..618
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 618..747
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
SQ SEQUENCE 969 AA; 110383 MW; 5EC151D933929509 CRC64;
NQKCGGRKKT VSFSSMPSEK KISSANDCIS FMQAGCELKK VRPNSRIYNR FFTLDTDLQA
LRWEPSKKDL EKAKLDISAI KEIRLGKNTE TFRNNGLADQ ICEDCAFSIL HGENYESLDL
VANSADVANI WVSGLRYLVS RSKQPLDFME GNQNTPRFMW LKTVFEAADV DGNGIMLEDT
SVELIKQLNP TLKEAKIRLK FKEIQKSKEK LTTRVTEEEF CEAFCELCTR PEVYFLLVQI
SKNKEYLDAN DLMLFLEAEQ GVTHITEDMC LDIIRRYELS EEGRQKGFLA IDGFTQYLLS
SECDIFDPEQ KKVAQDMTQP LSHYYINASH NTYLIEDQFR GPADINGYVR ALKMGCRSIE
LDVSDGSDNE PILCNRNNMT THVSFRSVIE VINKFAFVAS EYPLILCLGN HCSLLQQKVM
VQQMKKVFGN KLYTEAPLPS ESYLPSPEKL KRMIIVKGKK LPSDPDMLEG EVTDEDEEAE
MSRRMSVDYN GVQKQIRLCR ELSDLVSICK SVQYRDFELS MKSQNYWEIC SFSETEASRI
ANEYPEDFVN YNKKFLSRIY PSAMRIDSSN LNPQDFWNCG CQIVAMNFQT PGPMMDLHTG
WFLQNGGCGY VLRPSIMRDE VSYFSANTKG IVPGVSPLAL HIKIISGQNF PKPKGACAKG
DVIDPYVCIE IHGIPADCSE QRTKTVQQNS DNPIFDETFE FQVNLPELAM IRFVALDDDY
IGDEFIGQYT IPFECLQPGY RHVPLRSFVG DIMEHVTLFV HIAITNRSGG GKAQKRSLSV
RMGKKVREYT MLRNIGLKTI DDIFKIAVHP LREAIDMREN MQNAIVSIKE LCGLPPIASL
KQCLLTLSSR LITSDNTPSV SLVMKDNFPY LEPLSAIPDV QKKMLAAYDL MIQESRFLIE
MADTVQEKIV QCQKAGMEFH EELHNLGAKE GLKGRKLNKA TESFAWNITV LKVDETFRKG
IIFLWVYTH
//
