PTEN1_ARATH
ID PTEN1_ARATH Reviewed; 412 AA.
AC Q9FLZ5;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and protein-tyrosine-phosphatase PTEN1 {ECO:0000305};
DE EC=3.1.3.48 {ECO:0000255|PROSITE-ProRule:PRU10044, ECO:0000269|PubMed:12368500};
DE EC=3.1.3.67 {ECO:0000269|PubMed:12368500};
DE AltName: Full=Protein PHOSPHATASE AND TENSIN HOMOLOG 1 {ECO:0000303|PubMed:21864294};
DE Short=AtPTEN1 {ECO:0000303|PubMed:12368500};
GN Name=PTEN1 {ECO:0000303|PubMed:12368500};
GN OrderedLocusNames=At5g39400 {ECO:0000312|Araport:AT5G39400};
GN ORFNames=MUL8.80 {ECO:0000312|EMBL:BAB11013.1};
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 [MRNA], FUNCTION, MUTAGENESIS OF CYS-152, DISRUPTION
RP PHENOTYPE, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND ACTIVITY REGULATION.
RC STRAIN=cv. Columbia;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
RP FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, ACTIVE SITE, 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: Protein tyrosine phosphatase that exhibits also lipid
CC phosphatase activity. Can use phosphatidylinositol substrates such as
CC PtdIns(3,4,5)P(3) as substrate. Pollen-specific phosphatase required
CC for pollen development. {ECO:0000269|PubMed:12368500}.
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:12368500};
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 Evidence={ECO:0000269|PubMed:12368500};
CC -!- ACTIVITY REGULATION: Inhibited by vanadate.
CC {ECO:0000269|PubMed:12368500}.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in pollen grains during the
CC late stage of development (at protein level).
CC {ECO:0000269|PubMed:12368500, ECO:0000269|PubMed:21864294}.
CC -!- DISRUPTION PHENOTYPE: Pollen cell death after mitosis, during the late
CC stage of development, characterized by collapsed pollen grains,
CC shrunken, with highly deformed exines and reduced size.
CC {ECO:0000269|PubMed:12368500}.
CC -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC {ECO:0000305|PubMed:21864294}.
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DR EMBL; AJ490172; CAD35363.1; -; mRNA.
DR EMBL; AB009054; BAB11013.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94429.1; -; Genomic_DNA.
DR EMBL; AK118115; BAC42741.1; -; mRNA.
DR EMBL; BT005560; AAO63980.1; -; mRNA.
DR RefSeq; NP_198756.2; NM_123302.4.
DR AlphaFoldDB; Q9FLZ5; -.
DR SMR; Q9FLZ5; -.
DR IntAct; Q9FLZ5; 2.
DR STRING; 3702.AT5G39400.1; -.
DR PaxDb; Q9FLZ5; -.
DR PRIDE; Q9FLZ5; -.
DR EnsemblPlants; AT5G39400.1; AT5G39400.1; AT5G39400.
DR GeneID; 833936; -.
DR Gramene; AT5G39400.1; AT5G39400.1; AT5G39400.
DR KEGG; ath:AT5G39400; -.
DR Araport; AT5G39400; -.
DR TAIR; locus:2175713; AT5G39400.
DR eggNOG; KOG2283; Eukaryota.
DR HOGENOM; CLU_020105_5_0_1; -.
DR InParanoid; Q9FLZ5; -.
DR OMA; ELARGCC; -.
DR OrthoDB; 639380at2759; -.
DR PhylomeDB; Q9FLZ5; -.
DR BioCyc; ARA:AT5G39400-MON; -.
DR PRO; PR:Q9FLZ5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLZ5; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016791; F:phosphatase activity; IDA:TAIR.
DR GO; GO:0052866; F:phosphatidylinositol phosphate phosphatase activity; IDA:UniProtKB.
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:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
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 Pfam; PF10409; PTEN_C2; 1.
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; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..412
FT /note="Phosphatidylinositol 3,4,5-trisphosphate 3-
FT phosphatase and protein-tyrosine-phosphatase PTEN1"
FT /id="PRO_0000435167"
FT DOMAIN 42..211
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT DOMAIN 239..396
FT /note="C2 tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT ACT_SITE 152
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT MUTAGEN 152
FT /note="C->S: Loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:12368500"
SQ SEQUENCE 412 AA; 47355 MW; 4F9F0FD80F115ABB CRC64;
MGLKLSRGPV KEKSPLEFTR VHILTYFTTN SYLRNLVSKK RRRLIIGGYD LDMSYISDKL
LAMSFPAERM RAVYRNPLWQ VKSVLDMRHP DHYKVYNLCI EESYDPDNFY GRVERFPFDD
NHVPSLKMIQ LFCESVHSWL SLDPKNIAVV HCMAGKGRTG LMVSAYLVYG GMSAEEALEM
YASRRTTNNN GVSIPSQRRY VKYWSDLLSF SKKGPPEVKL PQEHSRELLR IRLYDTANVD
SVFFVVSELQ EVPNEMYRPS VELARGCCRQ FKKGYCRSSS PRYYISHVNC DSEEDEEVTD
GEEPHLVVQM DTESSIIDEK TCLDFYFDKP VRVSGDIRIT FYQKMIGSRL FYTCFNTAFI
TNGLLQFSIG ELDKVGGNGR SISGPDFSLE LLFGPACSKF GKFLSRDDLS LS
