RLPHL_ARATH
ID RLPHL_ARATH Reviewed; 311 AA.
AC Q8LEC0; Q9SR61;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Tyrosine-protein phosphatase At3g09960;
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q9SR62};
GN OrderedLocusNames=At3g09960 {ECO:0000312|Araport:AT3G09960};
GN ORFNames=F8A24.22 {ECO:0000312|EMBL:AC015985},
GN T22K18.23 {ECO:0000312|EMBL:AAF04427.1};
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].
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.
CC -!- FUNCTION: Protein phosphatase that dephosphorylates specifically
CC tyrosine-phosphorylated peptides; especially active on dual-
CC phosphorylated substrates containing a phosphothreonine-X-
CC phosphotyrosine motif. {ECO:0000250|UniProtKB:Q9SR62}.
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;
CC Evidence={ECO:0000250|UniProtKB:Q9SR62};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:Q9SR62};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000250|UniProtKB:Q9SR62};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9SR62}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF04427.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC010927; AAF04427.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC015985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002686; AEE74841.1; -; Genomic_DNA.
DR EMBL; AY085511; AAM62735.1; -; mRNA.
DR RefSeq; NP_566363.1; NM_111831.5.
DR AlphaFoldDB; Q8LEC0; -.
DR SMR; Q8LEC0; -.
DR STRING; 3702.AT3G09960.1; -.
DR PaxDb; Q8LEC0; -.
DR PRIDE; Q8LEC0; -.
DR ProteomicsDB; 179371; -.
DR EnsemblPlants; AT3G09960.1; AT3G09960.1; AT3G09960.
DR GeneID; 820157; -.
DR Gramene; AT3G09960.1; AT3G09960.1; AT3G09960.
DR KEGG; ath:AT3G09960; -.
DR Araport; AT3G09960; -.
DR TAIR; locus:2100113; AT3G09960.
DR eggNOG; KOG0374; Eukaryota.
DR HOGENOM; CLU_880984_0_0_1; -.
DR InParanoid; Q8LEC0; -.
DR OMA; KETWMEY; -.
DR OrthoDB; 1008380at2759; -.
DR PhylomeDB; Q8LEC0; -.
DR PRO; PR:Q8LEC0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8LEC0; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd07421; MPP_Rhilphs; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041768; RLPH.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..311
FT /note="Tyrosine-protein phosphatase At3g09960"
FT /id="PRO_0000447244"
FT ACT_SITE 82
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9SR62"
FT BINDING 14
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SR62"
FT BINDING 16
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SR62"
FT BINDING 16
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9SR62"
FT BINDING 48
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SR62"
FT BINDING 48
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SR62"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9SR62"
FT BINDING 81
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SR62"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9SR62"
FT BINDING 215
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SR62"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9SR62"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9SR62"
FT BINDING 268
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SR62"
SQ SEQUENCE 311 AA; 35085 MW; 0573DA23565E56F9 CRC64;
MMTQKPRTVI CVGDIHGNIS KLNKLWLNLQ SDIQNSDFSS ALVIFLGDYC DRGPETRKVI
DFLISLPEKH PDQTHVFLAG NHDFAFAGFL GLLPRPSDGS EFKETWKEYS KSEEREGWYK
GEGFENMHLQ SRRWAGKIRV QFDYSAYGVL YNGSIYDAAS TFESYGVPHG SSDLIKAVPE
SHKKFLTNMV WVHKEDDVCI ETEEGLTHCK LIAVHAGLET KNNVEEQLKL LRDKDTSIPR
IQPLTGRKTV WGIPQELDDK KTIVVSGHHG KLHIDGLRLI IDEGGGYTDT PLAAIVLPSK
KIIRDTDNFS N
