ID A0A2U3TZV8_HUMAN Unreviewed; 1685 AA.
AC A0A2U3TZV8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
GN Name=PLCH1 {ECO:0000313|Ensembl:ENSP00000417502.2};
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:ENSP00000417502.2, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000417502.2, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [2] {ECO:0007829|PubMed:19413330}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [3] {ECO:0007829|PubMed:21406692}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [4] {ECO:0000313|Ensembl:ENSP00000417502.2}
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|ARBA:ARBA00023674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000256|ARBA:ARBA00023674};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR EMBL; AC012022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC068296; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_011510866.1; XM_011512564.2.
DR SMR; A0A2U3TZV8; -.
DR MassIVE; A0A2U3TZV8; -.
DR PeptideAtlas; A0A2U3TZV8; -.
DR Antibodypedia; 46750; 96 antibodies from 24 providers.
DR Ensembl; ENST00000460012.7; ENSP00000417502.2; ENSG00000114805.18.
DR MANE-Select; ENST00000460012.7; ENSP00000417502.2; NM_014996.4; NP_055811.2.
DR HGNC; HGNC:29185; PLCH1.
DR VEuPathDB; HostDB:ENSG00000114805; -.
DR GeneTree; ENSGT00940000157185; -.
DR OMA; CRTAKCR; -.
DR ChiTaRS; PLCH1; human.
DR Proteomes; UP000005640; Chromosome 3.
DR Bgee; ENSG00000114805; Expressed in bronchial epithelial cell and 134 other cell types or tissues.
DR ExpressionAtlas; A0A2U3TZV8; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050429; F:calcium-dependent phospholipase C activity; IEA:InterPro.
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; cd16220; EFh_PI-PLCeta1; 1.
DR CDD; cd08632; PI-PLCc_eta1; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
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 InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
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; IPR028392; PLC-eta1_cat.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR046972; PLCeta1_EF.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF51; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE ETA-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; SM00054; EFh; 2.
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; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
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 Calcium {ECO:0000256|ARBA:ARBA00022837};
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Proteomics identification {ECO:0007829|EPD:A0A2U3TZV8,
KW ECO:0007829|MaxQB:A0A2U3TZV8};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 32..140
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 154..189
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 190..226
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 613..725
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 727..855
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 538..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1044..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1292..1321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1570..1605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1685 AA; 188675 MW; DFEF4D083D573929 CRC64;
MSYWNLEKRN CVQYRRHFLV DNSVFHVERC MSVMQSGTQM IKLKRGTKGL VRLFYLDEHR
TRLRWRPSRK SEKAKILIDS IYKVTEGRQS EIFHRQAEGN FDPSCCFTIY HGNHMESLDL
ITSNPEEART WITGLKYLMA GISDEDSLAK RQRTHDQWVK QTFEEADKNG DGLLNIEEIH
QLMHKLNVNL PRRKVRQMFQ EADTDENQGT LTFEEFCVFY KMMSLRRDLY LLLLSYSDKK
DHLTVEELAQ FLKVEQKMNN VTTDYCLDII KKFEVSEENK VKNVLGIEGF TNFMRSPACD
IFNPLHHEVY QDMDQPLCNY YIASSHNTYL TGDQLLSQSK VDMYARVLQE GCRCVEVDCW
DGPDGEPVVH HGYTLTSKIL FRDVVETINK HAFVKNEFPV ILSIENHCSI QQQRKIAQYL
KGIFGDKLDL SSVDTGECKQ LPSPQSLKGK ILVKGKKLPY HLGDDAEEGE VSDEDSADEI
EDECKFKLHY SNGTTEHQVE SFIRKKLESL LKESQIRDKE DPDSFTVRAL LKATHEGLNA
HLKQSPDVKE SGKKSHGRSL MTNFGKHKKT TKSRSKSYST DDEEDTQQST GKEGGQLYRL
GRRRKTMKLC RELSDLVVYT NSVAAQDIVD DGTTGNVLSF SETRAHQVVQ QKSEQFMIYN
QKQLTRIYPS AYRIDSSNFN PLPYWNAGCQ LVALNYQSEG RMMQLNRAKF KANGNCGYVL
KPQQMCKGTF NPFSGDPLPA NPKKQLILKV ISGQQLPKPP DSMFGDRGEI IDPFVEVEII
GLPVDCCKDQ TRVVDDNGFN PVWEETLTFT VHMPEIALVR FLVWDHDPIG RDFVGQRTVT
FSSLVPGYRH VYLEGLTEAS IFVHITINEI YGKNRQLQGL KGLFNKNPRH SSSENNSHYV
RKRSIGDRIL RRTASAPAKG RKKSKMGFQE MVEIKDSVSE ATRDQDGVLR RTTRSLQARP
VSMPVDRNLL GALSLPVSET AKDIEGKENS LAEDKDGRRK GKASIKDPHF LNFNKKLSSS
SSALLHKDTS QGDTIVSTAH MSVTGEQLGM SSPRGGRTTS NATSNCQENP CPSKSLSPKQ
HLAPDPVVNP TQDLHGVKIK EKGNPEDFVE GKSILSGSVL SHSNLEIKNL EGNRGKGRAA
TSFSLSDVSM LCSDIPDLHS TAILQESVIS HLIDNVTLTN ENEPGSSISA LIGQFDETNN
QALTVVSHLH NTSVMSGHCP LPSLGLKMPI KHGFCKGKSK SSFLCSSPEL IALSSSETTK
HATNTVYETT CTPISKTKPD DDLSSKAKTA ALESNLPGSP NTSRGWLPKS PTKGEDWETL
KSCSPASSPD LTLEDVIADP TLCFNSGESS LVEIDGESEN LSLTTCEYRR EGTSQLASPL
KLKYNQGVVE HFQRGLRNGY CKETLRPSVP EIFNNIQDVK TQSISYLAYQ GAGFVHNHFS
DSDAKMFQTC VPQQSSAQDM HVPVPKQLAH LPLPALKLPS PCKSKSLGDL TSEDIACNFE
SKYQCISKSF VTTGIRDKKG VTVKTKSLEP IDALTEQLRK LVSFDQEDNC QVLYSKQDAN
QLPRALVRKL SSRSQSRVRN IASRAKEKQE ANKQKVPNPS NGAGVVLRNK PSAPTPAVNR
HSTGSYIAGY LKNTKGGGLE GRGIPEGACT ALHYGHVDQF CSDNSVLQTE PSSDDKPEIY
FLLRL
//
