IP5PC_ARATH
ID IP5PC_ARATH Reviewed; 1316 AA.
AC O80560; F4IS64; Q712G3;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JUN-2015, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Type I inositol polyphosphate 5-phosphatase 12 {ECO:0000303|PubMed:15574849};
DE Short=At5PTase12 {ECO:0000303|PubMed:15574849};
DE EC=3.1.3.56 {ECO:0000269|PubMed:15574849};
GN Name=IP5P12 {ECO:0000305};
GN Synonyms=5PTASE12 {ECO:0000303|PubMed:22573619}, IPP3;
GN OrderedLocusNames=At2g43900 {ECO:0000312|Araport:AT2G43900};
GN ORFNames=F6E13.3 {ECO:0000312|EMBL:AAC23399.1};
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 [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, TISSUE
RP SPECIFICITY, INDUCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=15574849; DOI=10.1093/pcp/pch187;
RA Zhong R., Ye Z.-H.;
RT "Molecular and biochemical characterization of three WD-repeat-domain-
RT containing inositol polyphosphate 5-phosphatases in Arabidopsis thaliana.";
RL Plant Cell Physiol. 45:1720-1728(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Hypocotyl;
RA Lin W.-H., Xu Z.-H., Mueller-Roeber B., Xue H.-W.;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
RP GENE FAMILY.
RX PubMed=11402208; DOI=10.1104/pp.126.2.801;
RA Berdy S.E., Kudla J., Gruissem W., Gillaspy G.E.;
RT "Molecular characterization of At5PTase1, an inositol phosphatase capable
RT of terminating inositol trisphosphate signaling.";
RL Plant Physiol. 126:801-810(2001).
RN [6]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-946, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [7]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=22573619; DOI=10.1242/dev.081224;
RA Wang Y., Chu Y.J., Xue H.W.;
RT "Inositol polyphosphate 5-phosphatase-controlled Ins(1,4,5)P3/Ca2+ is
RT crucial for maintaining pollen dormancy and regulating early germination of
RT pollen.";
RL Development 139:2221-2233(2012).
CC -!- FUNCTION: Has phosphatase activity toward Ins(1,4,5)P3
CC (PubMed:15574849). Controls Ins(1,4,5)P3/Ca(2+) levels that is crucial
CC for maintaining pollen dormancy and regulating early germination of
CC pollen (PubMed:22573619). {ECO:0000269|PubMed:15574849,
CC ECO:0000269|PubMed:22573619}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,4,5-trisphosphate + H2O = 1D-myo-inositol
CC 1,4-bisphosphate + phosphate; Xref=Rhea:RHEA:19797,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58282,
CC ChEBI:CHEBI:203600; EC=3.1.3.56;
CC Evidence={ECO:0000269|PubMed:15574849};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15574849};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=223 uM for Ins(1,4,5)P3 {ECO:0000269|PubMed:15574849};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O80560-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O80560-2; Sequence=VSP_036160;
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves and flowers and only
CC weakly expressed in roots, stem and young seedlings. More precisely
CC detected in cotyledon tips, hydathodes of leaves and mature pollen
CC grains. {ECO:0000269|PubMed:22573619}.
CC -!- INDUCTION: Not induced by stresses. {ECO:0000269|PubMed:15574849}.
CC -!- DISRUPTION PHENOTYPE: Precocious pollen germination within anthers.
CC Hypersensitivity to abscisic acid (ABA) during seed germination.
CC Elevated levels of Ins(1,4,5)P3 and cytosolic Ca(2+).
CC {ECO:0000269|PubMed:22573619}.
CC -!- SIMILARITY: Belongs to the inositol polyphosphate 5-phosphatase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC23399.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAV87314.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAV87318.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAC81919.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY761187; AAV87314.1; ALT_FRAME; mRNA.
DR EMBL; AY761191; AAV87318.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AJ277884; CAC81919.1; ALT_FRAME; mRNA.
DR EMBL; AC004005; AAC23399.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CP002685; AEC10342.1; -; Genomic_DNA.
DR PIR; T00670; T00670.
DR RefSeq; NP_181918.4; NM_129952.7. [O80560-1]
DR AlphaFoldDB; O80560; -.
DR SMR; O80560; -.
DR STRING; 3702.AT2G43900.1; -.
DR iPTMnet; O80560; -.
DR PaxDb; O80560; -.
DR PRIDE; O80560; -.
DR ProteomicsDB; 228820; -. [O80560-1]
DR EnsemblPlants; AT2G43900.1; AT2G43900.1; AT2G43900. [O80560-1]
DR GeneID; 818994; -.
DR Gramene; AT2G43900.1; AT2G43900.1; AT2G43900. [O80560-1]
DR KEGG; ath:AT2G43900; -.
DR Araport; AT2G43900; -.
DR eggNOG; KOG0565; Eukaryota.
DR HOGENOM; CLU_004721_0_1_1; -.
DR InParanoid; O80560; -.
DR BioCyc; ARA:AT2G43900-MON; -.
DR BioCyc; MetaCyc:AT2G43900-MON; -.
DR BRENDA; 3.1.3.56; 399.
DR SABIO-RK; O80560; -.
DR PRO; PR:O80560; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80560; baseline and differential.
DR Genevisible; O80560; AT.
DR GO; GO:0052659; F:inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR GO; GO:0009846; P:pollen germination; IGI:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SMART; SM00128; IPPc; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Isopeptide bond; Magnesium; Metal-binding;
KW Reference proteome; Repeat; Ubl conjugation; WD repeat.
FT CHAIN 1..1316
FT /note="Type I inositol polyphosphate 5-phosphatase 12"
FT /id="PRO_0000359742"
FT REPEAT 153..193
FT /note="WD 1"
FT REPEAT 213..252
FT /note="WD 2"
FT REPEAT 264..302
FT /note="WD 3"
FT REPEAT 441..480
FT /note="WD 4"
FT REPEAT 520..557
FT /note="WD 5"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..804
FT /note="Catalytic 1"
FT /evidence="ECO:0000250|UniProtKB:Q84MA2"
FT REGION 867..882
FT /note="Catalytic 2"
FT /evidence="ECO:0000250|UniProtKB:Q84MA2"
FT REGION 1100..1316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 946
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
FT VAR_SEQ 1220..1255
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_036160"
FT CONFLICT 798
FT /note="Y -> N (in Ref. 2; CAC81919)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1316 AA; 144731 MW; DD508A05B962A1A4 CRC64;
MDIINNNHRD ENDDDEEEAL SAMSSVPPPR KIHSYSHQLR ATGQKGHHRQ RQHSLDDIPK
ITEIVSGCGI SGDSSDDEFY PYATTTNSSS FPFTGGDTGD SDDYLHQPEI GEDFQPLPEF
VGSGGGVGMF KVPTRSPLHS ARPPCLELRP HPLKETQVGR FLRNIACTET QLWAGQESGV
RFWNFDDAFE PGCGLSGRVQ RGDEDAAPFQ ESASTSPTTC LMVDNGNRLV WSGHKDGKIR
SWKMDYVLDD GDDSPFKEGL AWQAHKGPVN SVIMSSYGDL WSCSEGGVIK IWTWESMEKS
LSLRLEEKHM AALLVERSGI DLRAQVTVNG TCNISSSEVK CLLADNVRSK VWAAQLQTFS
LWDGRTKELL KVFNSEGQTE NRVDMPLGQD QPAAEDEMKA KIASTSKKEK PHGFLQRSRN
AIMGAADAVR RVATRGGGAY EDAKRTEAMV LAGDGMIWTG CTNGLLIQWD GNGNRLQDFR
HHQCAVLCFC TFGERIYIGY VSGHIQIIDL EGNLIAGWVA HNNAVIKMAA ADGYIFSLAT
HGGIRGWPVI SPGPLDGIIR SELAEKERTY AQTDSVRILT GSWNVGQGKA SHDALMSWLG
SVASDVGILV VGLQEVEMGA GFLAMSAAKE SVGGNEGSTI GQYWIDTIGK TLDEKAVFER
MGSRQLAGLL ISLWVRKNLR THVGDIDVAA VPCGFGRAIG NKGGVGLRIR VFDRIMCFIN
CHLAAHLEAV NRRNADFDHI YKTMSFTRSS NAHNAPAAGV STGSHTTKSA NNANVNTEET
KQDLAEADMV VFFGDFNYRL FGISYDEARD FVSQRSFDWL REKDQLRAEM KAGRVFQGMR
EAIITFPPTY KFERHRPGLG GYDSGEKKRI PAWCDRVIFR DTRTSPESEC SLDCPVVASI
MLYDACMDVT ESDHKPVRCK FHVKIEHVDR SVRRQEFGRI IKTNEKVRAL LNDLRYVPET
IVSSNSIVLQ NQDTFVLRIT NKCVKENAVF RILCEGQSTV REDEDTLELH PLGSFGFPRW
LEVMPAAGTI KPDSSVEVSV HHEEFHTLEE FVDGIPQNWW CEDTRDKEAI LVVNVQGGCS
TETVCHRVHV RHCFSAKNLR IDSNPSNSKS QSLKKNEGDS NSKSSKKSDG DSNSKSSKKS
DGDSNSKSSK KSDGDSNSKS SKKSDGDSNS KSSKKSDGDS NSKSSKKSDG DSNSKSSKKS
DGDSCSKSQK KSDGDTNSKS QKKGDGDSSS KSHKKNDGDS SSKSHKKNDG DSSSKSHKKS
DGDSSSKSHK KSEGDSSSKS HKKNDGDSSS SYKSQSGKKN SNSSTVEESR NNHNKR
