ID A0A9L0RQG0_HORSE Unreviewed; 1059 AA.
AC A0A9L0RQG0;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 18-JUN-2025, entry version 11.
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:ENSECAP00000064068.1,
GN ECO:0000313|VGNC:VGNC:56160};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000064068.1, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000064068.1, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000064068.1,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000064068.1}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000064068.1};
RG Ensembl;
RL Submitted (MAR-2025) 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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR Ensembl; ENSECAT00000084503.1; ENSECAP00000064068.1; ENSECAG00000007274.4.
DR VGNC; VGNC:56160; PLCL1.
DR GeneTree; ENSGT00940000158407; -.
DR Proteomes; UP000002281; Chromosome 18.
DR GO; GO:0004435; F:phosphatidylinositol-4,5-bisphosphate phospholipase C activity; IEA:InterPro.
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 FunFam; 1.10.238.10:FF:000005; Phosphoinositide phospholipase C; 1.
DR FunFam; 2.30.29.30:FF:000025; Phosphoinositide phospholipase C; 1.
DR FunFam; 2.60.40.150:FF:000017; Phosphoinositide phospholipase C; 1.
DR FunFam; 3.20.20.190:FF:000001; Phosphoinositide phospholipase C; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 77..187
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 549..665
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 665..794
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1029..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1059
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1059 AA; 119771 MW; 8B4B82167B49BA0F CRC64;
MGEYSSCVCL WLQLLQDRPT VVPASFLTMA LGYWEHHLLL LSLQDPSNQK CGGRKKTVSF
SSMPSEKKIS SASDCISFMQ AGCELKKVRP NSRIYNRFFT LDTDLQALRW EPSKKDLEKA
KLDISAIKEI RLGKNTETFR NNGLADQICE DCAFSIVHGE NYESLDLVAN SADVANIWVS
GLRYLVSRSK QPLDFMEGNQ STPRFMWLKT VFEAADVDGN GIMLEDTAVE LIKQLNPTLK
ESKIRLKFKE IQKSKEKLTT RVTEEEFCEA FCELCTRSEV YFLLVQISKN KEYLDANDLM
LFLEAEQGVT HITEDMCLDI IRRYELSEEG RQKGFLAIDG FTQYLLSPEC EIFDPEQKKV
AQDMTQPLSH YYINASHNTY LIEDQFRGPA DINGYVRALK MGCRSIELDV SDGSDNEPIL
CNRNNMTTHL SFLSVIEVIN KFAFVASEYP LILCLGNRCS LPQQKVMVQQ MRKVFGNTLY
TEAPLPSESY LPSPEKLKRM IIVKGKKLPS DPDVLEGEVT DEDEEAEMSR RMSVDYNGEQ
KQVWLCRELS DLVSICQSVQ YRDFELSMKS QNYWEICSFS ETEASRIANE YPEDFVNYNK
KFLSRIYPSA MRIDSSNLNP QDFWNCGCQI VAMNFQTPGP MMDLHTGWFL QNGGCGYVLR
PSIMRDEVSY FSANTKGIVP GVSPLALHIK IISGQNFPKP KGACAKGDVI DPYVCIEIHG
IPADCSEQRT KTVQQNSDNP IFDETFEFQV NLPELAMIRF VVLDDDYIGD EFIGQYTIPF
ECLQPGYRHV PLRSFVGDIM EHVTLFVHIA ITNRSGGGKA QKRSLSVRMG KKIRECTMLR
NVGLKTIDDV FKTALHPLRE AIDMRENMQN AIVSVKELCG LPPIASLKQC LLTLSSRLIA
SDNSPSVSLV MKDNFPYLEP LGAIPDVQKK MLAAYDLMIQ ESRFLIEMAD TVQEKIVQCQ
KSGMEFHEEL HNLGAKEGLK GRKLNKATES FAWNITVLKG QGDLLKNAKN EAIENMKQIQ
LACLSCGLSK APSSGSEAKS KRSLEAIEEK ESGEENGKL
//
