YVH1_PLAF7
ID YVH1_PLAF7 Reviewed; 575 AA.
AC O77334; Q8MVQ8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Dual specificity protein phosphatase YVH1 {ECO:0000303|PubMed:14698441};
DE Short=PfYVH1 {ECO:0000303|PubMed:14698441};
DE EC=3.1.3.16 {ECO:0000269|PubMed:14698441};
DE EC=3.1.3.48 {ECO:0000269|PubMed:14698441};
GN Name=YVH1 {ECO:0000303|PubMed:14698441};
GN ORFNames=PF3D7_0309000 {ECO:0000312|EMBL:CAB11119.3};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000312|Proteomes:UP000001450};
RN [1] {ECO:0000312|EMBL:AAM46812.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP INTERACTION WITH PES, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP MUTAGENESIS OF CYS-379; CYS-476 AND CYS-530.
RX PubMed=14698441; DOI=10.1016/j.molbiopara.2003.11.005;
RA Kumar R., Musiyenko A., Cioffi E., Oldenburg A., Adams B., Bitko V.,
RA Krishna S.S., Barik S.;
RT "A zinc-binding dual-specificity YVH1 phosphatase in the malaria parasite,
RT Plasmodium falciparum, and its interaction with the nuclear protein,
RT pescadillo.";
RL Mol. Biochem. Parasitol. 133:297-310(2004).
RN [2] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=10448855; DOI=10.1038/22964;
RA Bowman S., Lawson D., Basham D., Brown D., Chillingworth T., Churcher C.M.,
RA Craig A., Davies R.M., Devlin K., Feltwell T., Gentles S., Gwilliam R.,
RA Hamlin N., Harris D., Holroyd S., Hornsby T., Horrocks P., Jagels K.,
RA Jassal B., Kyes S., McLean J., Moule S., Mungall K.L., Murphy L.,
RA Oliver K., Quail M.A., Rajandream M.A., Rutter S., Skelton J., Squares R.,
RA Squares S., Sulston J.E., Whitehead S., Woodward J.R., Newbold C.,
RA Barrell B.G.;
RT "The complete nucleotide sequence of chromosome 3 of Plasmodium
RT falciparum.";
RL Nature 400:532-538(1999).
RN [3] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [4] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
CC -!- FUNCTION: Dual specificity protein phosphatase which dephosphorylates
CC both phosphotyrosine and phosphoserine residues.
CC {ECO:0000269|PubMed:14698441}.
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:14698441};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685;
CC Evidence={ECO:0000269|PubMed:14698441};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:14698441};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630;
CC Evidence={ECO:0000269|PubMed:14698441};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:14698441};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000269|PubMed:14698441};
CC -!- SUBUNIT: Interacts with PES. {ECO:0000269|PubMed:14698441}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14698441}. Nucleus
CC {ECO:0000269|PubMed:14698441}. Note=Localizes to the cytoplasm at the
CC ring stage, translocates to the nucleus in the trophozoite stage and
CC returns to the cytoplasm at the schizont stage.
CC {ECO:0000269|PubMed:14698441}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the parasite blood stage,
CC including in rings, trophozoites and schizonts (at protein level)
CC (PubMed:14698441). Expressed in gametocytes (at protein level)
CC (PubMed:14698441). {ECO:0000269|PubMed:14698441}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM46812.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF482703; AAM46812.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL844502; CAB11119.3; -; Genomic_DNA.
DR PIR; T18439; T18439.
DR RefSeq; XP_001351164.1; XM_001351128.1.
DR AlphaFoldDB; O77334; -.
DR SMR; O77334; -.
DR STRING; 5833.PFC0380w; -.
DR PRIDE; O77334; -.
DR EnsemblProtists; CAB11119; CAB11119; PF3D7_0309000.
DR GeneID; 814406; -.
DR KEGG; pfa:PF3D7_0309000; -.
DR VEuPathDB; PlasmoDB:PF3D7_0309000; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000078400; -.
DR VEuPathDB; PlasmoDB:Pf7G8_030014800; -.
DR VEuPathDB; PlasmoDB:PfCD01_030014400; -.
DR VEuPathDB; PlasmoDB:PfDd2_030014000; -.
DR VEuPathDB; PlasmoDB:PfGA01_030015600; -.
DR VEuPathDB; PlasmoDB:PfGB4_030014600; -.
DR VEuPathDB; PlasmoDB:PfGN01_030014600; -.
DR VEuPathDB; PlasmoDB:PfHB3_030012800; -.
DR VEuPathDB; PlasmoDB:PfIT_030013800; -.
DR VEuPathDB; PlasmoDB:PfKE01_030013400; -.
DR VEuPathDB; PlasmoDB:PfKH01_030013900; -.
DR VEuPathDB; PlasmoDB:PfKH02_030014500; -.
DR VEuPathDB; PlasmoDB:PfML01_030014000; -.
DR VEuPathDB; PlasmoDB:PfNF135_030014000; -.
DR VEuPathDB; PlasmoDB:PfNF166_030012300; -.
DR VEuPathDB; PlasmoDB:PfNF54_030014000; -.
DR VEuPathDB; PlasmoDB:PfSD01_030014100; -.
DR VEuPathDB; PlasmoDB:PfSN01_030014700; -.
DR VEuPathDB; PlasmoDB:PfTG01_030015400; -.
DR HOGENOM; CLU_524288_0_0_1; -.
DR InParanoid; O77334; -.
DR OMA; YPFAHPN; -.
DR PhylomeDB; O77334; -.
DR Proteomes; UP000001450; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IDA:GeneDB.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IDA:GeneDB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0046823; P:negative regulation of nucleocytoplasmic transport; IDA:GeneDB.
DR GO; GO:0070262; P:peptidyl-serine dephosphorylation; IDA:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:GeneDB.
DR GO; GO:0060284; P:regulation of cell development; IDA:GeneDB.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Metal-binding; Nucleus; Protein phosphatase;
KW Reference proteome; Zinc.
FT CHAIN 1..575
FT /note="Dual specificity protein phosphatase YVH1"
FT /id="PRO_0000455111"
FT DOMAIN 283..435
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 185..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 379
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT BINDING 476
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:14698441"
FT BINDING 530
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:14698441"
FT MUTAGEN 379
FT /note="C->S: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:14698441"
FT MUTAGEN 476
FT /note="C->S: Severe loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:14698441"
FT MUTAGEN 530
FT /note="C->S: Severe loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:14698441"
SQ SEQUENCE 575 AA; 67787 MW; 253DBEB648C1B810 CRC64;
MIVKVFDYIY ISNVYNANDI YELIKLNIGG VLTCFDCTCI EWCHHNDTNV TNKIFYKDIF
VNTKKDLIKC DVPIITNKSV NSDIIGGTHQ INNYYNEQNN NYHDNTYKEF TQTHKTNIDP
SQIKSDHINE ERKEHYDYII FPSDIINNTQ CNNNNLKDYI KSMLILKEDA YIDFDVIHMD
QLKNKHNNNN NNNNNNNNNN NNNNNNNNCC TFKNPDISNT SQHHVEHIQI HKSNSHSNIP
SDNINFCNKK YDKNLSRSVE ISEKDKHPEN SLLYEFVNKD KLNYKINQEE DTVSSEKNKL
CDNNNNNNMV HTRHIYNVCE LNKCLRENKL IPYNNIYKMK HLYLNILDTF DENILKHVNK
AHLFIDSVIQ KKKNILIHCM AGISRCSSII LSYVSKKNKK GIEYNFNLLK SKYPFAHPNE
NFYRQLLLYE KMNYTLDGCT DYHNIYKKIK MNRENLEELK ILNLKNDKQP IYNFRCKHCN
YVLFNDNEII KHDFKISKIK KNYGNSCTSI FIEKKEWILT ENKMKGVLNC PNVNCNIKLG
KWSWTGICCS CGYLQIPAFM INSSNVDRMN ISKTV
