PTN2A_ARATH
ID PTN2A_ARATH Reviewed; 611 AA.
AC Q9LT75; Q8GZT8;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and protein-tyrosine-phosphatase PTEN2A {ECO:0000305};
DE EC=3.1.3.48 {ECO:0000255|PROSITE-ProRule:PRU10044, ECO:0000269|PubMed:21864294};
DE EC=3.1.3.67 {ECO:0000269|PubMed:21864294};
DE AltName: Full=Protein PHOSPHATASE AND TENSIN HOMOLOG 2-a {ECO:0000303|PubMed:21864294};
DE Short=AtPTEN2 {ECO:0000303|PubMed:12368500};
DE Short=AtPTEN2a {ECO:0000303|PubMed:21864294};
GN Name=PTEN2A {ECO:0000303|PubMed:21864294};
GN Synonyms=PTEN2 {ECO:0000303|PubMed:12368500};
GN OrderedLocusNames=At3g19420 {ECO:0000312|Araport:AT3G19420};
GN ORFNames=MLD14.15 {ECO:0000303|PubMed:10819329};
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].
RC STRAIN=cv. C24;
RA Elge S., Mueller-Roeber B.;
RT "Cloning and functional analysis of a plant PTEN-like protein.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 NOMENCLATURE.
RX PubMed=12368500; DOI=10.1105/tpc.005702;
RA Gupta R., Ting J.T.L., Sokolov L.N., Johnson S.A., Luan S.;
RT "A tumor suppressor homolog, AtPTEN1, is essential for pollen development
RT in Arabidopsis.";
RL Plant Cell 14:2495-2507(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91 AND SER-509, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP FUNCTION, MUTAGENESIS OF CYS-263 AND 267-MET-ALA-268, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION BY SALT AND
RP OSMOTIC STRESSES, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=21864294; DOI=10.1042/bj20110776;
RA Pribat A., Sormani R., Rousseau-Gueutin M., Julkowska M.M., Testerink C.,
RA Joubes J., Castroviejo M., Laguerre M., Meyer C., Germain V., Rothan C.;
RT "A novel class of PTEN protein in Arabidopsis displays unusual
RT phosphoinositide phosphatase activity and efficiently binds phosphatidic
RT acid.";
RL Biochem. J. 441:161-171(2012).
CC -!- FUNCTION: Binds phosphatidic acid. Protein tyrosine phosphatase that
CC exhibits also lipid phosphatase activity. Hydrolyzed poorly p-
CC nitrophenyl phosphate (p-NPP). Can use PtdIns isomers as substrates.
CC Removes efficiently phosphate from the D3 position of the inositol
CC ring, less from the D4 position and not at all from the D5 position on
CC monophosphorylated PtdIns isomers (PIPs). The presence of a phosphate
CC group in the D5 position on PIP(2) isomers reduces lipid phosphatase
CC activity. Mostly active on PtdIns(3)P and PtdIns(3,4)P(2), to a lower
CC extent, on PtdIns(4)P and PtdIns(3,5)P(2), but barely against
CC PtdIns(3,4,5)P(3) as substrate. {ECO:0000269|PubMed:21864294}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044, ECO:0000269|PubMed:21864294};
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-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:25017,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57836,
CC ChEBI:CHEBI:58456; EC=3.1.3.67;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.5 mM for p-NPP {ECO:0000269|PubMed:21864294};
CC Vmax=206 nmol/min/mg enzyme with p-NPP as substrate
CC {ECO:0000269|PubMed:21864294};
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, stems, leaves,
CC flowers and siliques. However, at protein level, not observed in older
CC leaves and mature siliques. {ECO:0000269|PubMed:21864294}.
CC -!- INDUCTION: Accumulates in response to salt (e.g. NaCl) and osmotic
CC stresses (e.g. mannitol). {ECO:0000269|PubMed:21864294}.
CC -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC {ECO:0000305|PubMed:21864294}.
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DR EMBL; AF268257; AAO13749.1; -; mRNA.
DR EMBL; AB025624; BAB02466.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76238.1; -; Genomic_DNA.
DR EMBL; AY070042; AAL49799.1; -; mRNA.
DR RefSeq; NP_188573.1; NM_112829.5.
DR AlphaFoldDB; Q9LT75; -.
DR SMR; Q9LT75; -.
DR STRING; 3702.AT3G19420.1; -.
DR iPTMnet; Q9LT75; -.
DR PaxDb; Q9LT75; -.
DR PRIDE; Q9LT75; -.
DR ProteomicsDB; 226419; -.
DR EnsemblPlants; AT3G19420.1; AT3G19420.1; AT3G19420.
DR GeneID; 821476; -.
DR Gramene; AT3G19420.1; AT3G19420.1; AT3G19420.
DR KEGG; ath:AT3G19420; -.
DR Araport; AT3G19420; -.
DR TAIR; locus:2090659; AT3G19420.
DR eggNOG; KOG2283; Eukaryota.
DR HOGENOM; CLU_021394_1_0_1; -.
DR InParanoid; Q9LT75; -.
DR OMA; PLNANPE; -.
DR OrthoDB; 639380at2759; -.
DR PhylomeDB; Q9LT75; -.
DR BioCyc; ARA:AT3G19420-MON; -.
DR PRO; PR:Q9LT75; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LT75; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:TAIR.
DR GO; GO:0052866; F:phosphatidylinositol phosphate phosphatase activity; IDA:TAIR.
DR GO; GO:0016314; F:phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:TAIR.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR CDD; cd14509; PTP_PTEN; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR045101; PTP_PTEN.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR SMART; SM01326; PTEN_C2; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Lipid metabolism; Phospholipid metabolism; Phosphoprotein;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..611
FT /note="Phosphatidylinositol 3,4,5-trisphosphate 3-
FT phosphatase and protein-tyrosine-phosphatase PTEN2A"
FT /id="PRO_0000435168"
FT DOMAIN 145..324
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT DOMAIN 331..458
FT /note="C2 tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 263
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590,
FT ECO:0000269|PubMed:21864294"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MUTAGEN 263
FT /note="C->S: Loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:21864294"
FT MUTAGEN 267..268
FT /note="MA->KG: Reduced phosphatase activity toward
FT PtdIns(3)P and PtdIns(4)P, but strongly increased activity
FT for PtdIns(3,4)P(2), PtdIns(3,5)P(2) and PtdIns(3,4,5)P(3)
FT as substrates."
FT /evidence="ECO:0000269|PubMed:21864294"
FT CONFLICT 19..23
FT /note="HPPPP -> PPPPL (in Ref. 1; AAO13749)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 611 AA; 66430 MW; CB4FB3CFE0C6C577 CRC64;
MSSESPNLPA AAGTVPDNHP PPPPVVTAAE AGSDDSPKGV ASKLSAAGIS NWAKNLKVPQ
PFASTQNDSG VENTEKSAFA KFTSGLGIRL SPKSPQTNDT TTEGTSSATE SSFIGTITKG
LVDTSKNAVK AVQVKARHAV SQNKRRYQEG GFDLDLTYIT ENIIAMGFPA GDMSSGFFGY
VEGFYRNQME EVINFLETQH KGKYKVYNLC SERLYDVSLF EGKVASFPFD DHNCPPIHLV
TSFCQSAYSW LKEDIENVVV VHCKAGMART GLMICSLLLY LKFFPTAEEC MDFYNQKRCV
DGKGLVLPSQ IRYVKYFERI LTYFNGENQP GRRCMLRGFR LHRCPYWIRP SITISDHNGV
LFTTKKHPRT KDLSPEDFWF SAPKKGVMVF ALPGEPGLTE LAGDFKIQFH DRQGDFYCWL
NTTMMENRVI LKTSELDGFD KRKLPSPGFM VEVVLADINA TIPTNPSSET ASKTPEETSA
ANSSPVDGSA SVPGPDKETE NPDKDDVFSD NEGDSTGPTK TTSSASSQTP EAKKSADETA
VLTKATEKVS ISGNKGSSQP VQGVTVSKGE ATEKPSGAGV NASSSSESEF KVMAADASVF
SFGDEDDFES D
