IP5PB_ARATH
ID IP5PB_ARATH Reviewed; 334 AA.
AC Q5EAF2; Q9SX81;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Type IV inositol polyphosphate 5-phosphatase 11 {ECO:0000303|PubMed:15181205};
DE Short=At5PTase11 {ECO:0000303|PubMed:15181205};
DE EC=3.1.3.36 {ECO:0000269|PubMed:15181205};
DE EC=3.1.3.86 {ECO:0000269|PubMed:15181205};
GN Name=IP5P11 {ECO:0000305};
GN OrderedLocusNames=At1g47510 {ECO:0000312|Araport:AT1G47510};
GN ORFNames=F16N3.22 {ECO:0000312|EMBL:AAD46036.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-334, FUNCTION, INDUCTION, TISSUE
RP SPECIFICITY, AND CATALYTIC ACTIVITY.
RX PubMed=15181205; DOI=10.1104/pp.104.040253;
RA Ercetin M.E., Gillaspy G.E.;
RT "Molecular characterization of an Arabidopsis gene encoding a phospholipid-
RT specific inositol polyphosphate 5-phosphatase.";
RL Plant Physiol. 135:938-946(2004).
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 DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=18392779; DOI=10.1007/s11103-008-9327-3;
RA Ercetin M.E., Ananieva E.A., Safaee N.M., Torabinejad J., Robinson J.Y.,
RA Gillaspy G.E.;
RT "A phosphatidylinositol phosphate-specific myo-inositol polyphosphate 5-
RT phosphatase required for seedling growth.";
RL Plant Mol. Biol. 67:375-388(2008).
RN [7]
RP INDUCTION BY SALT.
RX PubMed=21677096; DOI=10.1104/pp.111.176883;
RA Kaye Y., Golani Y., Singer Y., Leshem Y., Cohen G., Ercetin M.,
RA Gillaspy G., Levine A.;
RT "Inositol polyphosphate 5-phosphatase7 regulates the production of reactive
RT oxygen species and salt tolerance in Arabidopsis.";
RL Plant Physiol. 157:229-241(2011).
CC -!- FUNCTION: Has phosphatase activity toward PtdIns(4,5)P2, and in vitro
CC toward PtdIns(3,5)P2 and PtdIns(3,4,5)P3. Cannot dephosphorylate
CC PtdIns(5)P, Ins(1,4,5)P3 and Ins(1,3,4,5)P4.
CC {ECO:0000269|PubMed:15181205}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456; EC=3.1.3.36;
CC Evidence={ECO:0000269|PubMed:15181205, ECO:0000269|PubMed:18392779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-
CC trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + phosphate; Xref=Rhea:RHEA:25528,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57658,
CC ChEBI:CHEBI:57836; EC=3.1.3.86;
CC Evidence={ECO:0000269|PubMed:15181205};
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC {ECO:0000269|PubMed:18392779}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q5EAF2-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC {ECO:0000269|PubMed:15181205}.
CC -!- INDUCTION: Induced by abscisic acid (ABA), jasmonic acid (JA) and auxin
CC (PubMed:15181205). Up-regulated in seedlings and down-regulated in
CC mature plant by salt stress (PubMed:21677096).
CC {ECO:0000269|PubMed:15181205, ECO:0000269|PubMed:21677096}.
CC -!- DISRUPTION PHENOTYPE: Alterations in germination and in dark-growth
CC seedlings. Elevated level of Ins(1,4,5)P3 and InsP2 levels.
CC {ECO:0000269|PubMed:18392779}.
CC -!- SIMILARITY: Belongs to the inositol polyphosphate 5-phosphatase family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD46036.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC007519; AAD46036.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE32179.1; -; Genomic_DNA.
DR EMBL; BT020617; AAW81725.1; -; mRNA.
DR EMBL; BT021928; AAX49377.1; -; mRNA.
DR EMBL; AY627297; AAT45895.1; -; mRNA.
DR PIR; D96515; D96515.
DR RefSeq; NP_175182.2; NM_103644.3. [Q5EAF2-1]
DR AlphaFoldDB; Q5EAF2; -.
DR SMR; Q5EAF2; -.
DR BioGRID; 26385; 1.
DR IntAct; Q5EAF2; 1.
DR STRING; 3702.AT1G47510.1; -.
DR PaxDb; Q5EAF2; -.
DR EnsemblPlants; AT1G47510.1; AT1G47510.1; AT1G47510. [Q5EAF2-1]
DR GeneID; 841160; -.
DR Gramene; AT1G47510.1; AT1G47510.1; AT1G47510. [Q5EAF2-1]
DR KEGG; ath:AT1G47510; -.
DR Araport; AT1G47510; -.
DR TAIR; locus:2015388; AT1G47510.
DR eggNOG; KOG0565; Eukaryota.
DR HOGENOM; CLU_011711_5_2_1; -.
DR InParanoid; Q5EAF2; -.
DR OMA; NSECQHI; -.
DR OrthoDB; 885595at2759; -.
DR PhylomeDB; Q5EAF2; -.
DR BioCyc; ARA:AT1G47510-MON; -.
DR PRO; PR:Q5EAF2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q5EAF2; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IDA:TAIR.
DR GO; GO:0043813; F:phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity; IDA:TAIR.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
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 Pfam; PF03372; Exo_endo_phos; 1.
DR SMART; SM00128; IPPc; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Hydrolase; Membrane;
KW Reference proteome.
FT CHAIN 1..334
FT /note="Type IV inositol polyphosphate 5-phosphatase 11"
FT /id="PRO_0000209725"
FT REGION 206..222
FT /note="Catalytic 1"
FT /evidence="ECO:0000250|UniProtKB:Q84MA2"
FT REGION 282..297
FT /note="Catalytic 2"
FT /evidence="ECO:0000250|UniProtKB:Q84MA2"
SQ SEQUENCE 334 AA; 37580 MW; 73F28B12173C772A CRC64;
MPTMGNKNSM CGLKRFPNYK KSPIGSFAKN SSSHDGIKTI EAVNSCSFSR KADLCIRIIT
WNMNGNVSYE DLVELVGKER KFDLLVVGLQ EAPKANVDQL LQTASSPTHE LLGKAKLQSV
QLYLFGPKNS HTLVKELKAE RYSVGGCGGL IGRKKGAVAI RINYDDIKMV FISCHLSAHA
KKVDQRNTEL RHIANSLLPR DKRKRDLTVW LGDLNYRIQD VSNHPVRSLI QNHLQSVLVS
KDQLLQEAER GEIFKGYSEG TLGFKPTYKY NVGSSDYDTS HKIRVPAWTD RILFKIQDTD
NIQATLHSYD SIDQVYGSDH KPVKADLCLK WVNS
