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ZEUS1_ARATH
ID   ZEUS1_ARATH             Reviewed;         263 AA.
AC   Q0WW55; A0NAB2; A2P2R9; Q8LEB4; Q93ZP0;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Thymidylate kinase {ECO:0000305};
DE            Short=AtTMPK {ECO:0000303|PubMed:18036198};
DE            EC=2.7.4.9 {ECO:0000305};
DE   AltName: Full=Protein ZEUS1 {ECO:0000303|PubMed:18036198};
DE   Flags: Precursor;
GN   Name=ZEU1 {ECO:0000303|PubMed:18036198};
GN   OrderedLocusNames=At5g59440 {ECO:0000312|Araport:AT5G59440};
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;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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] (ISOFORM 2).
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] (ISOFORM 1).
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY,
RP   INDUCTION BY CELL CYCLE, AND DISRUPTION PHENOTYPE.
RX   PubMed=18036198; DOI=10.1111/j.1365-313x.2007.03372.x;
RA   Ronceret A., Gadea-Vacas J., Guilleminot J., Lincker F., Delorme V.,
RA   Lahmy S., Pelletier G., Chaboute M.E., Devic M.;
RT   "The first zygotic division in Arabidopsis requires de novo transcription
RT   of thymidylate kinase.";
RL   Plant J. 53:776-789(2008).
CC   -!- FUNCTION: Catalyzes the conversion of dTMP to dTDP (Probable). Involved
CC       in the regulation of DNA replication. Is essential to promote the first
CC       division of the zygote (PubMed:18036198). {ECO:0000269|PubMed:18036198,
CC       ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528,
CC         ChEBI:CHEBI:456216; EC=2.7.4.9; Evidence={ECO:0000305};
CC   -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion
CC       {ECO:0000269|PubMed:18036198}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC       {ECO:0000269|PubMed:18036198}. Nucleus, nucleoplasm
CC       {ECO:0000269|PubMed:18036198}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=AtTMPK.1 {ECO:0000303|PubMed:18036198};
CC         IsoId=Q0WW55-1; Sequence=Displayed;
CC       Name=2; Synonyms=AtTMPK.2 {ECO:0000303|PubMed:18036198};
CC         IsoId=Q0WW55-2; Sequence=VSP_058414;
CC   -!- TISSUE SPECIFICITY: Expressed in root, rosette leaves, flower buds,
CC       flowers and siliques. {ECO:0000269|PubMed:18036198}.
CC   -!- INDUCTION: Cell cycle regulated. Up-regulated at the G1/S phase
CC       transition and then decreases rapidly as cells progress into S-phase.
CC       Not up-regulated during the male and female gametophytic mitoses.
CC       {ECO:0000269|PubMed:18036198}.
CC   -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous, due to
CC       arrest of the embryo sac development soon after fertilization.
CC       {ECO:0000269|PubMed:18036198}.
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family. {ECO:0000305}.
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DR   EMBL; AB025604; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED97188.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97189.1; -; Genomic_DNA.
DR   EMBL; AY056422; AAL08278.1; -; mRNA.
DR   EMBL; AY081713; AAL87366.1; -; mRNA.
DR   EMBL; AK226501; BAE98643.1; -; mRNA.
DR   EMBL; AY085520; AAM62744.1; -; mRNA.
DR   RefSeq; NP_568907.2; NM_125335.4. [Q0WW55-2]
DR   RefSeq; NP_851222.1; NM_180891.4. [Q0WW55-1]
DR   AlphaFoldDB; Q0WW55; -.
DR   SMR; Q0WW55; -.
DR   STRING; 3702.AT5G59440.3; -.
DR   PRIDE; Q0WW55; -.
DR   ProteomicsDB; 232318; -. [Q0WW55-1]
DR   EnsemblPlants; AT5G59440.1; AT5G59440.1; AT5G59440. [Q0WW55-1]
DR   EnsemblPlants; AT5G59440.2; AT5G59440.2; AT5G59440. [Q0WW55-2]
DR   GeneID; 836063; -.
DR   Gramene; AT5G59440.1; AT5G59440.1; AT5G59440. [Q0WW55-1]
DR   Gramene; AT5G59440.2; AT5G59440.2; AT5G59440. [Q0WW55-2]
DR   KEGG; ath:AT5G59440; -.
DR   Araport; AT5G59440; -.
DR   eggNOG; KOG3327; Eukaryota.
DR   PhylomeDB; Q0WW55; -.
DR   BioCyc; ARA:AT5G59440-MON; -.
DR   BioCyc; MetaCyc:AT5G59440-MON; -.
DR   BRENDA; 2.7.4.9; 399.
DR   UniPathway; UPA00575; -.
DR   PRO; PR:Q0WW55; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q0WW55; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004550; F:nucleoside diphosphate kinase activity; IBA:GO_Central.
DR   GO; GO:0004798; F:thymidylate kinase activity; IBA:GO_Central.
DR   GO; GO:0009041; F:uridylate kinase activity; IBA:GO_Central.
DR   GO; GO:0006233; P:dTDP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006227; P:dUDP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00165; Thymidylate_kinase; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039430; Thymidylate_kin-like_dom.
DR   InterPro; IPR018095; Thymidylate_kin_CS.
DR   InterPro; IPR018094; Thymidylate_kinase.
DR   Pfam; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00041; DTMP_kinase; 1.
DR   PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Kinase; Mitochondrion;
KW   Nucleotide biosynthesis; Nucleotide-binding; Nucleus; Reference proteome;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..51
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           52..263
FT                   /note="Thymidylate kinase"
FT                   /id="PRO_0000436753"
FT   BINDING         66..74
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
FT   VAR_SEQ         1..39
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_058414"
FT   CONFLICT        45
FT                   /note="F -> C (in Ref. 5; AAM62744)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        149
FT                   /note="D -> Y (in Ref. 3; AAL08278/AAL87366)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   263 AA;  29550 MW;  04F853BF410C3EB7 CRC64;
     MKRICSVSSV QLFSRSFRAL ASPRSLNYPL QCIKRSSVRM ESSNFSSGVR TESSVKPRGA
     LIVLEGLDRS GKSTQCAKLL SFLNGLGHPT ELWRFPDRET SVGQMISAYL SNKSQLDDHT
     IHLLFSANRW EKRSLMEEKL KTGTTLIVDR YSYSGVAFSS AKGLDIEWCK APEIGLLAPD
     SVLYLDISPE RAAERGGYGD ERYERVEFQK KVADFYQTLG DSSWKIINAS DAMEEVEKKI
     QQVVLDQVKE CTEGKPLSLL WSS
 
 
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