PLCD5_ARATH
ID PLCD5_ARATH Reviewed; 578 AA.
AC Q944C2; Q8W4B4; Q9LUZ0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Phosphoinositide phospholipase C 5;
DE EC=3.1.4.11;
DE AltName: Full=Phosphoinositide phospholipase PLC5;
DE Short=AtPLC5;
DE Short=AtPLCx;
DE Short=PI-PLC5;
GN Name=PLC5; Synonyms=ATHATPLC6; OrderedLocusNames=At5g58690;
GN ORFNames=MZN1.13, MZN1.15;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=17142056; DOI=10.1016/j.pep.2006.10.007;
RA Cao Z., Zhang J., Li Y., Xu X., Liu G., Bhattacharrya M.K., Yang H.,
RA Ren D.;
RT "Preparation of polyclonal antibody specific for AtPLC4, an Arabidopsis
RT phosphatidylinositol-specific phospholipase C in rabbits.";
RL Protein Expr. Purif. 52:306-312(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12226484; DOI=10.1104/pp.004770;
RA Mueller-Roeber B., Pical C.;
RT "Inositol phospholipid metabolism in Arabidopsis. Characterized and
RT putative isoforms of inositol phospholipid kinase and phosphoinositide-
RT specific phospholipase C.";
RL Plant Physiol. 130:22-46(2002).
RN [6]
RP FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX AGRICOLA=IND43668249; DOI=10.1111/j.1469-8137.2004.01069.x;
RA Hunt L., Otterhag L., Lee J.C., Lasheen T., Hunt J., Seki M., Shinozaki K.,
RA Sommarin M., Gilmour D.J., Pical C., Gray J.E.;
RT "Gene-specific expression and calcium activation of Arabidopsis thaliana
RT phospholipase C isoforms.";
RL New Phytol. 162:643-654(2004).
CC -!- FUNCTION: The production of the second messenger molecules
CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated
CC by activated phosphatidylinositol-specific phospholipase C enzymes.
CC {ECO:0000269|Ref.6}.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane; Peripheral
CC membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, roots, flowers and siliques.
CC High levels of expression in the guard cells and vasculature of leaves
CC and roots. {ECO:0000269|Ref.6}.
CC -!- INDUCTION: By environmental stresses such as dehydration, salinity and
CC low temperature. {ECO:0000269|Ref.6}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97337.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; AF434167; AAL30748.2; -; mRNA.
DR EMBL; AB020755; BAA97337.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97085.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70993.1; -; Genomic_DNA.
DR EMBL; AY062681; AAL32759.1; -; mRNA.
DR EMBL; BT010399; AAQ56842.1; -; mRNA.
DR RefSeq; NP_001332556.1; NM_001345318.1.
DR RefSeq; NP_200677.2; NM_125256.3.
DR AlphaFoldDB; Q944C2; -.
DR SMR; Q944C2; -.
DR STRING; 3702.AT5G58690.1; -.
DR PaxDb; Q944C2; -.
DR PRIDE; Q944C2; -.
DR EnsemblPlants; AT5G58690.1; AT5G58690.1; AT5G58690.
DR EnsemblPlants; AT5G58690.3; AT5G58690.3; AT5G58690.
DR GeneID; 835983; -.
DR Gramene; AT5G58690.1; AT5G58690.1; AT5G58690.
DR Gramene; AT5G58690.3; AT5G58690.3; AT5G58690.
DR KEGG; ath:AT5G58690; -.
DR Araport; AT5G58690; -.
DR TAIR; locus:2178833; AT5G58690.
DR eggNOG; KOG0169; Eukaryota.
DR HOGENOM; CLU_002738_3_2_1; -.
DR InParanoid; Q944C2; -.
DR OMA; HEHNMSE; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; Q944C2; -.
DR BioCyc; ARA:AT5G58690-MON; -.
DR BRENDA; 3.1.4.11; 399.
DR PRO; PR:Q944C2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q944C2; baseline and differential.
DR Genevisible; Q944C2; AT.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
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; PTHR10336; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF09279; EF-hand_like; 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; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism;
KW Membrane; Reference proteome; Transducer.
FT CHAIN 1..578
FT /note="Phosphoinositide phospholipase C 5"
FT /id="PRO_0000324130"
FT DOMAIN 28..111
FT /note="EF-hand-like"
FT DOMAIN 112..256
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 314..430
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 430..560
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 258..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..297
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
SQ SEQUENCE 578 AA; 66253 MW; A744F73545FC7364 CRC64;
MKRDMGSYKM GLCCSDKLRM NRGAPPQDVV TAFVEYTEGR SHMTAEQLCR FLVEVQDETE
VLVSDAEKII ERITCERHHI TKFLRHTLNL DDFFSFLFSD DLNHPIDSKV HQDMASPLSH
YFIYTSHNSY LTGNQINSEC SDVPLIKALK RGVRALELDM WPNSTKDDIL VLHGWAWTPP
VELVKCLRSI KEHAFYASAY PVILTLEDHL TPDLQAKAAE MMKEIFMDMV YFPEAGGLKE
FPSPEDLKYK IVISTKPPKG SLRKDKDSES DASGKASSDV SADDEKTEEE TSEAKNEEDG
FDQESSNLDF LTYSRLITIP SGNAKNGLKE ALTIDNGGVR RLSLREQKFK KATEMYGTEV
IKFTQKNLLR IYPKATRVNS SNYRPYNGWM YGAQMVAFNM QGYGRALWMM HGMFRGNGGC
GYVKKPDFMM NNNLSGEVFN PKAKLPIKKT LKVKVYMGKG WDSGFQRTCF NTWSSPNFYT
RVGITGVRGD KVMKKTKKEQ KTWEPFWNEE FEFQLTVPEL ALLRIEVHDY NMPEKDDFSG
QTCLPVSELR QGIRSVPLYD RKGERLVSVT LLMRFHFL
