RLPH2_ARATH
ID RLPH2_ARATH Reviewed; 309 AA.
AC Q9SR62; A0A178V7L4; Q8L8R0; Q8RXI9;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Tyrosine-protein phosphatase RLPH2;
DE EC=3.1.3.48 {ECO:0000269|PubMed:26742850, ECO:0000269|PubMed:29615518};
DE AltName: Full=Protein RHIZOBIALE-LIKE PHOSPHATASE 2 {ECO:0000303|PubMed:26742850};
GN Name=RLPH2 {ECO:0000303|PubMed:26742850};
GN OrderedLocusNames=At3g09970 {ECO:0000312|Araport:AT3G09970};
GN ORFNames=T22K18.22 {ECO:0000312|EMBL:AAF04426.1};
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;
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 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, SUBCELLULAR LOCATION, ACTIVITY REGULATION,
RP TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=26742850; DOI=10.1074/jbc.m115.683656;
RA Uhrig R.G., Labandera A.-M., Muhammad J., Samuel M., Moorhead G.B.;
RT "Rhizobiales-like phosphatase 2 from Arabidopsis thaliana is a novel
RT phospho-tyrosine-specific phospho-protein phosphatase (PPP) family protein
RT phosphatase.";
RL J. Biol. Chem. 291:5926-5934(2016).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ZINC AND PHOSPHATE
RP IONS, ACTIVE SITE, FUNCTION, MUTAGENESIS OF ARG-51; ARG-132; LYS-238 AND
RP ARG-245, AND CATALYTIC ACTIVITY.
RX PubMed=29615518; DOI=10.1126/scisignal.aan8804;
RA Labandera A.-M., Uhrig R.G., Colville K., Moorhead G.B., Ng K.K.S.;
RT "Structural basis for the preference of the Arabidopsis thaliana
RT phosphatase RLPH2 for tyrosine-phosphorylated substrates.";
RL Sci. Signal. 11:0-0(2018).
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:0000269|PubMed:26742850}.
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:0000269|PubMed:26742850, ECO:0000269|PubMed:29615518};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:29615518};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000269|PubMed:29615518};
CC -!- ACTIVITY REGULATION: Inhibited by the tyrosine phosphatase inhibitor
CC orthovanadate, but resistant to the serine/threonine phosphatase
CC inhibitors okadaic acid and microcystin. Inhibited by phosphate analogs
CC NaF and Na(3)VO(4), and the adenylates ATP and ADP. Inactivated by zinc
CC ions. {ECO:0000269|PubMed:26742850}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7-7.8. {ECO:0000269|PubMed:26742850};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26742850}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC siliques (at protein level). {ECO:0000269|PubMed:26742850}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. {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; AC010927; AAF04426.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74842.1; -; Genomic_DNA.
DR EMBL; AY080859; AAL87332.1; -; mRNA.
DR EMBL; AY150444; AAN12986.1; -; mRNA.
DR EMBL; AY088866; AAM67172.1; -; mRNA.
DR RefSeq; NP_566364.1; NM_111832.3.
DR PDB; 5VJV; X-ray; 1.95 A; A=1-309.
DR PDB; 5VJW; X-ray; 1.80 A; A=1-309.
DR PDBsum; 5VJV; -.
DR PDBsum; 5VJW; -.
DR AlphaFoldDB; Q9SR62; -.
DR SMR; Q9SR62; -.
DR STRING; 3702.AT3G09970.1; -.
DR PaxDb; Q9SR62; -.
DR PRIDE; Q9SR62; -.
DR ProteomicsDB; 189866; -.
DR EnsemblPlants; AT3G09970.1; AT3G09970.1; AT3G09970.
DR GeneID; 820158; -.
DR Gramene; AT3G09970.1; AT3G09970.1; AT3G09970.
DR KEGG; ath:AT3G09970; -.
DR Araport; AT3G09970; -.
DR TAIR; locus:2100098; AT3G09970.
DR eggNOG; KOG0374; Eukaryota.
DR HOGENOM; CLU_880984_0_0_1; -.
DR InParanoid; Q9SR62; -.
DR OrthoDB; 1008380at2759; -.
DR PhylomeDB; Q9SR62; -.
DR PRO; PR:Q9SR62; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SR62; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:TAIR.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:TAIR.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..309
FT /note="Tyrosine-protein phosphatase RLPH2"
FT /id="PRO_0000447243"
FT ACT_SITE 81
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:29615518,
FT ECO:0007744|PDB:5VJV"
FT BINDING 13
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29615518,
FT ECO:0007744|PDB:5VJV, ECO:0007744|PDB:5VJW"
FT BINDING 15
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29615518,
FT ECO:0007744|PDB:5VJV, ECO:0007744|PDB:5VJW"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29615518,
FT ECO:0007744|PDB:5VJV"
FT BINDING 47
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29615518,
FT ECO:0007744|PDB:5VJV, ECO:0007744|PDB:5VJW"
FT BINDING 47
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29615518,
FT ECO:0007744|PDB:5VJV, ECO:0007744|PDB:5VJW"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29615518,
FT ECO:0007744|PDB:5VJV"
FT BINDING 80
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29615518,
FT ECO:0007744|PDB:5VJV, ECO:0007744|PDB:5VJW"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29615518"
FT BINDING 213
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29615518,
FT ECO:0007744|PDB:5VJV, ECO:0007744|PDB:5VJW"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29615518"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29615518,
FT ECO:0007744|PDB:5VJV"
FT BINDING 266
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29615518,
FT ECO:0007744|PDB:5VJV, ECO:0007744|PDB:5VJW"
FT MUTAGEN 51
FT /note="R->A: Weak activity for the pTEpY peptide
FT HTGFLpTEpYVATR."
FT /evidence="ECO:0000269|PubMed:29615518"
FT MUTAGEN 132
FT /note="R->S: Weak activity for the pTEpY peptide
FT HTGFLpTEpYVATR. Weak activity for the pTEpY peptide
FT HTGFLpTEpYVATR; when associated with S-238."
FT /evidence="ECO:0000269|PubMed:29615518"
FT MUTAGEN 238
FT /note="K->S: Slight reduction in activity for the pTEpY
FT peptide HTGFLpTEpYVATR but strongly increased activity for
FT the TEpY peptide HTGFLTEpYVATR. Weak activity for the pTEpY
FT peptide HTGFLpTEpYVATR; when associated with S-132."
FT /evidence="ECO:0000269|PubMed:29615518"
FT MUTAGEN 245
FT /note="R->A: Weak activity for the pTEpY peptide
FT HTGFLpTEpYVATR."
FT /evidence="ECO:0000269|PubMed:29615518"
FT CONFLICT 122
FT /note="G -> R (in Ref. 4; AAM67172)"
FT /evidence="ECO:0000305"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:5VJW"
FT HELIX 18..31
FT /evidence="ECO:0007829|PDB:5VJW"
FT HELIX 34..38
FT /evidence="ECO:0007829|PDB:5VJW"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:5VJW"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:5VJW"
FT HELIX 55..68
FT /evidence="ECO:0007829|PDB:5VJW"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:5VJW"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:5VJW"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:5VJW"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:5VJW"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:5VJW"
FT HELIX 128..133
FT /evidence="ECO:0007829|PDB:5VJW"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:5VJW"
FT HELIX 157..162
FT /evidence="ECO:0007829|PDB:5VJW"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:5VJW"
FT HELIX 178..185
FT /evidence="ECO:0007829|PDB:5VJW"
FT STRAND 191..200
FT /evidence="ECO:0007829|PDB:5VJW"
FT STRAND 203..211
FT /evidence="ECO:0007829|PDB:5VJW"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:5VJW"
FT HELIX 222..230
FT /evidence="ECO:0007829|PDB:5VJW"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:5VJW"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:5VJW"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:5VJW"
FT STRAND 257..264
FT /evidence="ECO:0007829|PDB:5VJW"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:5VJW"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:5VJW"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:5VJW"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:5VJW"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:5VJW"
SQ SEQUENCE 309 AA; 34425 MW; 72C780F01185BB90 CRC64;
MAQKPRTVIC VGDIHGYISK LNNLWLNLQS AIDPSDFSSA LVIFLGDYCD RGPETRKVID
FLISLPEKHP DQTHVFLAGN HDFAFSGFLG LLPRPSDGSD LKDTWKEYSK SEETEGWYTG
EGFEDMHLQG RRWAGKIKAT FNSVKGMAYK GSIYDAGSTF ESYGVPHGSS DLMKAVPESH
KKFLTNMVWV HEEDDVCIET EEGLKHCKLI AVHAGLEKGN NVEEQLKLLR AKDTSISKIQ
HLSGRKNVWD IPQELDDKHT VVVSGHHGKL HIDGMRLIID EGGGFPDKPV AAIVLPSKKI
IRDTDNLSS
