DSP3_ARATH
ID DSP3_ARATH Reviewed; 203 AA.
AC Q681Z2; Q9M8S1;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Tyrosine-protein phosphatase DSP3 {ECO:0000305};
DE EC=3.1.3.48 {ECO:0000255|PROSITE-ProRule:PRU10044, ECO:0000269|PubMed:21409566};
DE AltName: Full=Protein PLANT AND FUNGI ATYPICAL DUAL-SPECIFICITY PHOSPHATASE 3 {ECO:0000303|PubMed:21409566};
DE Short=AtPFA-DSP3 {ECO:0000303|PubMed:21409566};
GN Name=DSP3 {ECO:0000305};
GN OrderedLocusNames=At3g02800 {ECO:0000312|Araport:AT3G02800};
GN ORFNames=F13E7.26 {ECO:0000312|EMBL:AAF26980.1};
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=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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-203.
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 FUNCTION.
RX PubMed=17976645; DOI=10.1016/j.jmb.2007.10.008;
RA Roma-Mateo C., Rios P., Tabernero L., Attwood T.K., Pulido R.;
RT "A novel phosphatase family, structurally related to dual-specificity
RT phosphatases, that displays unique amino acid sequence and substrate
RT specificity.";
RL J. Mol. Biol. 374:899-909(2007).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=21409566; DOI=10.1007/s00438-011-0611-6;
RA Roma-Mateo C., Sacristan-Reviriego A., Beresford N.J.,
RA Caparros-Martin J.A., Culianez-Macia F.A., Martin H., Molina M.,
RA Tabernero L., Pulido R.;
RT "Phylogenetic and genetic linkage between novel atypical dual-specificity
RT phosphatases from non-metazoan organisms.";
RL Mol. Genet. Genomics 285:341-354(2011).
RN [7]
RP INTERACTION WITH FLZ1, AND SUBCELLULAR LOCATION.
RX PubMed=24901469; DOI=10.1371/journal.pone.0099074;
RA Jamsheer K M., Laxmi A.;
RT "DUF581 is plant specific FCS-like zinc finger involved in protein-protein
RT interaction.";
RL PLoS ONE 9:E99074-E99074(2014).
CC -!- FUNCTION: Possesses phosphotyrosine phosphatase activity in vitro
CC (PubMed:21409566). Hydrolyzes para-nitrophenyl phosphate in vitro
CC (PubMed:17976645, PubMed:21409566). Hydrolyzes O-methylfluorescein
CC phosphate in vitro. Dephosphorylates the phosphoinositides PI(3,5)P2
CC (PubMed:21409566). {ECO:0000269|PubMed:17976645,
CC ECO:0000269|PubMed:21409566}.
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:21409566};
CC -!- SUBUNIT: Interacts with FLZ1. {ECO:0000269|PubMed:24901469}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24901469}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots, stems and flowers.
CC Expressed at low levels in leaves and siliques.
CC {ECO:0000269|PubMed:21409566}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF26980.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC018363; AAF26980.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE73861.1; -; Genomic_DNA.
DR EMBL; AK175475; BAD43238.1; -; mRNA.
DR EMBL; BT010502; AAQ65125.1; -; mRNA.
DR RefSeq; NP_186929.2; NM_111148.3.
DR AlphaFoldDB; Q681Z2; -.
DR SMR; Q681Z2; -.
DR STRING; 3702.AT3G02800.1; -.
DR PaxDb; Q681Z2; -.
DR PRIDE; Q681Z2; -.
DR EnsemblPlants; AT3G02800.1; AT3G02800.1; AT3G02800.
DR GeneID; 821239; -.
DR Gramene; AT3G02800.1; AT3G02800.1; AT3G02800.
DR KEGG; ath:AT3G02800; -.
DR Araport; AT3G02800; -.
DR TAIR; locus:2075527; AT3G02800.
DR eggNOG; KOG1572; Eukaryota.
DR HOGENOM; CLU_047845_5_1_1; -.
DR InParanoid; Q681Z2; -.
DR OMA; NAWDPIT; -.
DR OrthoDB; 1539111at2759; -.
DR PhylomeDB; Q681Z2; -.
DR PRO; PR:Q681Z2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q681Z2; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016791; F:phosphatase activity; IDA:TAIR.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR020428; PFA-DSPs.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR004861; Siw14-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF03162; Y_phosphatase2; 1.
DR PRINTS; PR01911; PFDSPHPHTASE.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Nucleus; Protein phosphatase; Reference proteome.
FT CHAIN 1..203
FT /note="Tyrosine-protein phosphatase DSP3"
FT /id="PRO_0000442993"
FT DOMAIN 20..169
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 112
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 203 AA; 23510 MW; 8D6E4BCDC6F05C80 CRC64;
MCLIMETDDH NGDVLAPPSN FSMVEDGIYR SGFPRPENFS FLKTLNLRSI IYLCPEPYPE
ENLKFLEANN IKLYQFGIEG KTDPPTPMPK DTVLDALKVL VDVRNHPILI HCKRGKHRTG
CLVGCLRKVQ SWCLSSVLEE YQKNAGLKWR QRDLNFIEAF DIVSLRQCLL SIMYQYHGYG
FKRRRLAYEE ENVKTPKPQA ARV
