PTN2B_ARATH
ID PTN2B_ARATH Reviewed; 632 AA.
AC Q8H106; Q9SN07;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and protein-tyrosine-phosphatase PTEN2B {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-b {ECO:0000303|PubMed:21864294};
DE Short=AtPTEN2b {ECO:0000303|PubMed:21864294};
DE Short=AtPTEN3 {ECO:0000303|PubMed:12368500};
GN Name=PTEN2B {ECO:0000303|PubMed:21864294};
GN Synonyms=PTEN3 {ECO:0000303|PubMed:12368500};
GN OrderedLocusNames=At3g50110 {ECO:0000312|Araport:AT3G50110};
GN ORFNames=F3A4.190 {ECO:0000312|EMBL:CAB62119.1};
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 {ECO:0000312|EMBL:AAN41331.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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;
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 [4]
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY SALT AND OSMOTIC STRESSES, GENE
RP 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: Protein tyrosine phosphatase that exhibits also a weak lipid
CC phosphatase activity towards PtdIns(3)P. {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};
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 -!- TISSUE SPECIFICITY: Expressed, at low levels, in seedlings, roots,
CC stems, leaves, flowers and siliques. However, at protein level, not
CC observed in older leaves, flowers and siliques.
CC {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; AL132978; CAB62119.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78627.1; -; Genomic_DNA.
DR EMBL; BT000931; AAN41331.1; -; mRNA.
DR PIR; T45864; T45864.
DR RefSeq; NP_566929.1; NM_114871.3.
DR AlphaFoldDB; Q8H106; -.
DR SMR; Q8H106; -.
DR IntAct; Q8H106; 4.
DR STRING; 3702.AT3G50110.1; -.
DR iPTMnet; Q8H106; -.
DR PaxDb; Q8H106; -.
DR PRIDE; Q8H106; -.
DR ProteomicsDB; 224830; -.
DR EnsemblPlants; AT3G50110.1; AT3G50110.1; AT3G50110.
DR GeneID; 824173; -.
DR Gramene; AT3G50110.1; AT3G50110.1; AT3G50110.
DR KEGG; ath:AT3G50110; -.
DR Araport; AT3G50110; -.
DR TAIR; locus:2083168; AT3G50110.
DR eggNOG; KOG2283; Eukaryota.
DR HOGENOM; CLU_021394_1_0_1; -.
DR OMA; YTWLKED; -.
DR OrthoDB; 639380at2759; -.
DR PhylomeDB; Q8H106; -.
DR BioCyc; ARA:AT3G50110-MON; -.
DR PRO; PR:Q8H106; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8H106; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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; 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; SSF52799; SSF52799; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Lipid metabolism; Phospholipid metabolism; Phosphoprotein;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..632
FT /note="Phosphatidylinositol 3,4,5-trisphosphate 3-
FT phosphatase and protein-tyrosine-phosphatase PTEN2B"
FT /id="PRO_0000435169"
FT DOMAIN 189..368
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT DOMAIN 375..502
FT /note="C2 tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 307
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LT75"
FT CONFLICT 377..380
FT /note="Missing (in Ref. 1; CAB62119)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 632 AA; 70073 MW; B1BDD935DD63083F CRC64;
METDPANSSS KSPAVVSEKD VLIPEPSENT VGVVQDPVSA EREAHEDSIS TEASVAKVDD
TQMPASSTGS EPLSKTDDIV PCPPGSSPRE SPPSIFSSSG LSSWAKSFKF QQQDPNRTDS
GMSAFTRFTS ELGLHLPTKG SEEVGDSRSS NTQVGGAFES LTKAVVDSSR GAVKAMQVKA
RHIVSQNKRR YQEGEFDLDM TYITENIIAM GFPAGDISSG LFGFFEGLYR NHMEEVIKFF
ETHHKDKYKV YNLCSERLYD ASRFEGKVAS FPFDDHNCPP IQLIPSFCQS AYTWLKEDIQ
NVVVVHCKAG MARTGLMICC LLLYLKFFPT AEEAIDYYNQ KRCLDGKALV LPSQIRYVKY
YERVQNQFDG KVPPERRCML RGFRLINCPY WIRPAITISN HTDILFSTKK HQKTKDLGPE
DFWIKAPKKG VVVFAIPGEA GLTELAGDFK IHFQDSDGDF YCWLNTTLTD NRTMLKGSDF
DGFDKRKLPA PGFHVEIVMI EPDNSQPTKS KSDSTQQQSQ SSSSADSSKL KSNEKDDDVF
SDSDGEEEGN SQSYSTNEKT ASSMHTTSKP HQINEPPKRD DPSANRSVTS SSSSGHYNPI
PNNSLAVSDI KAIAADASVF SFGDEEEDYE SD
