DSP5_ARATH
ID DSP5_ARATH Reviewed; 204 AA.
AC Q9FFD7; Q8LDU6;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Tyrosine-protein phosphatase DSP5 {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 5 {ECO:0000303|PubMed:21409566};
DE Short=AtPFA-DSP5 {ECO:0000303|PubMed:21409566};
GN Name=DSP5 {ECO:0000305};
GN OrderedLocusNames=At5g16480 {ECO:0000312|Araport:AT5G16480};
GN ORFNames=MQK4.21 {ECO:0000312|EMBL:BAB09615.1};
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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., Quinitio C., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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).
CC -!- FUNCTION: Possesses low phosphotyrosine phosphatase activity in vitro.
CC Hydrolyzes O-methylfluorescein phosphate in vitro. Dephosphorylates the
CC phosphoinositides PI(3,5)P2. {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 -!- TISSUE SPECIFICITY: Highly expressed in flowers. Expressed at low
CC levels in roots, leaves, stems and siliques.
CC {ECO:0000269|PubMed:21409566}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
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DR EMBL; AB005242; BAB09615.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92298.1; -; Genomic_DNA.
DR EMBL; BT025778; ABF83668.1; -; mRNA.
DR EMBL; AY085793; AAM63010.1; -; mRNA.
DR RefSeq; NP_197152.1; NM_121653.4.
DR AlphaFoldDB; Q9FFD7; -.
DR SMR; Q9FFD7; -.
DR IntAct; Q9FFD7; 1.
DR STRING; 3702.AT5G16480.1; -.
DR PaxDb; Q9FFD7; -.
DR PRIDE; Q9FFD7; -.
DR DNASU; 831509; -.
DR EnsemblPlants; AT5G16480.1; AT5G16480.1; AT5G16480.
DR GeneID; 831509; -.
DR Gramene; AT5G16480.1; AT5G16480.1; AT5G16480.
DR KEGG; ath:AT5G16480; -.
DR Araport; AT5G16480; -.
DR TAIR; locus:2171317; AT5G16480.
DR eggNOG; KOG1572; Eukaryota.
DR HOGENOM; CLU_047845_5_1_1; -.
DR InParanoid; Q9FFD7; -.
DR OMA; GMATWKP; -.
DR OrthoDB; 1539111at2759; -.
DR PhylomeDB; Q9FFD7; -.
DR PRO; PR:Q9FFD7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFD7; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; Protein phosphatase; Reference proteome.
FT CHAIN 1..204
FT /note="Tyrosine-protein phosphatase DSP5"
FT /id="PRO_0000442995"
FT DOMAIN 19..168
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 111
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT CONFLICT 26
FT /note="E -> G (in Ref. 4; AAM63010)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 204 AA; 23596 MW; B8E537B7447449BA CRC64;
MGLIVDDDND GEVLIPPPNF SMVEDEIYRS GFPELENFGF LSTLNLRSII YLCPEPYPED
NLKSLASNNI KLFQFGIEGK TDPPTPMPKD TVLSALRVLV DVRNHPILIH CKRGKHRTGC
LVGCLRKVQN WCLSSVLEEY QKCAGLKWRQ RDLRFIEDFD VLRLKQCLYS IIYQYNGYGL
KRRKLLYQEE NVVQEQQKPQ ATKG
