ID H3BUD4_HUMAN Unreviewed; 1012 AA.
AC H3BUD4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
DE Flags: Fragment;
GN Name=PLCL1 {ECO:0000313|Ensembl:ENSP00000457588.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000457588.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000457588.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2] {ECO:0007829|PubMed:23186163}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23186163;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [3] {ECO:0000313|Ensembl:ENSP00000457588.1}
RP IDENTIFICATION.
RG Ensembl;
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|RuleBase:RU361133};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC005235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC013478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC019330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC109589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC116629; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3BUD4; -.
DR SMR; H3BUD4; -.
DR MassIVE; H3BUD4; -.
DR PeptideAtlas; H3BUD4; -.
DR ProteomicsDB; 42900; -.
DR Antibodypedia; 34073; 179 antibodies from 25 providers.
DR Ensembl; ENST00000487695.6; ENSP00000457588.1; ENSG00000115896.17.
DR UCSC; uc061rai.1; human.
DR HGNC; HGNC:9063; PLCL1.
DR VEuPathDB; HostDB:ENSG00000115896; -.
DR GeneTree; ENSGT00940000158407; -.
DR HOGENOM; CLU_002738_0_1_1; -.
DR ChiTaRS; PLCL1; human.
DR Proteomes; UP000005640; Chromosome 2.
DR Bgee; ENSG00000115896; Expressed in heart right ventricle and 181 other cell types or tissues.
DR ExpressionAtlas; H3BUD4; baseline and differential.
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 1: Evidence at protein level;
KW Hydrolase {ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Proteomics identification {ECO:0007829|EPD:H3BUD4,
KW ECO:0007829|MaxQB:H3BUD4};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 39..149
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 511..627
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 627..756
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1012
FT /evidence="ECO:0000313|Ensembl:ENSP00000457588.1"
SQ SEQUENCE 1012 AA; 114689 MW; A4AFBEEBEFD8C541 CRC64;
MKNKLQDPSN QKCGGRKKTV SFSSMPSEKK ISSANDCISF MQAGCELKKV RPNSRIYNRF
FTLDTDLQAL RWEPSKKDLE KAKLDISAIK EIRLGKNTET FRNNGLADQI CEDCAFSILH
GENYESLDLV ANSADVANIW VSGLRYLVSR SKQPLDFMEG NQNTPRFMWL KTVFEAADVD
GNGIMLEDTS VELIKQLNPT LKEAKIRLKF KEIQKSKEKL TTRVTEEEFC EAFCELCTRP
EVYFLLVQIS KNKEYLDAND LMLFLEAEQG VTHITEDICL DIIRRYELSE EGRQKGFLAI
DGFTQYLLSS ECDIFDPEQK KVAQDMTQPL SHYYINASHN TYLIEDQFRG PADINGYIRA
LKMGCRSVEL DVSDGSDNEP ILCNRNNMTT HVSFRSVIEV INKFAFVASE YPLILCLGNH
CSLPQQKVMA QQMKKVFGNK LYTEAPLPSE SYLPSPEKLK RMIIVKGKKL PSDPDVLEGE
VTDEDEEAEM SRRMSVDYNG EQKQIRLCRE LSDLVSICKS VQYRDFELSM KSQNYWEMCS
FSETEASRIA NEYPEDFVNY NKKFLSRIYP SAMRIDSSNL NPQDFWNCGC QIVAMNFQTP
GPMMDLHTGW FLQNGGCGYV LRPSIMRDEV SYFSANTKGI LPGVSPLALH IKIISGQNFP
KPKGACAKGD VIDPYVCIEI HGIPADCSEQ RTKTVQQNSD NPIFDETFEF QVNLPELAMI
RFVVLDDDYI GDEFIGQYTI PFECLQPGYR HVPLRSFVGD IMEHVTLFVH IAITNRSGGG
KAQKRSLSVR MGKKVREYTM LRNIGLKTID DIFKIAVHPL REAIDMRENM QNAIVSIKEL
CGLPPIASLK QCLLTLSSRL ITSDNTPSVS LVMKDSFPYL EPLGAIPDVQ KKMLTAYDLM
IQESRFLIEM ADTVQEKIVQ CQKAGMEFHE ELHNLGAKEG LKGRKLNKAT ESFAWNITVL
KGQGDLLKNA KNEAIENMKQ IQLACLSCGL SKAPSSSAEA KSKRSLEAIE EK
//
