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Y5520_ARATH
ID   Y5520_ARATH             Reviewed;         540 AA.
AC   Q9ASX5; Q9FHK3;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Uncharacterized aarF domain-containing protein kinase At5g05200, chloroplastic;
DE            EC=2.7.-.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=At5g05200; ORFNames=K2A11.7;
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=10470850; DOI=10.1093/dnares/6.3.183;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT   features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT   clones.";
RL   DNA Res. 6:183-195(1999).
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   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=16461379; DOI=10.1104/pp.105.076083;
RA   Ytterberg A.J., Peltier J.-B., van Wijk K.J.;
RT   "Protein profiling of plastoglobules in chloroplasts and chromoplasts. A
RT   surprising site for differential accumulation of metabolic enzymes.";
RL   Plant Physiol. 140:984-997(2006).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=22274653; DOI=10.1104/pp.111.193144;
RA   Lundquist P.K., Poliakov A., Bhuiyan N.H., Zybailov B., Sun Q.,
RA   van Wijk K.J.;
RT   "The functional network of the Arabidopsis plastoglobule proteome based on
RT   quantitative proteomics and genome-wide coexpression analysis.";
RL   Plant Physiol. 158:1172-1192(2012).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast, plastoglobule
CC       {ECO:0000269|PubMed:16461379, ECO:0000269|PubMed:22274653}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC       kinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB09696.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB018111; BAB09696.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED90840.1; -; Genomic_DNA.
DR   EMBL; AF361613; AAK32781.1; -; mRNA.
DR   EMBL; AY133554; AAM91384.1; -; mRNA.
DR   EMBL; AY063020; AAL34194.1; -; mRNA.
DR   EMBL; AY093317; AAM13316.1; -; mRNA.
DR   EMBL; AY035149; AAK59653.1; -; mRNA.
DR   EMBL; AY059866; AAL24348.1; -; mRNA.
DR   RefSeq; NP_568150.1; NM_120602.5.
DR   AlphaFoldDB; Q9ASX5; -.
DR   SMR; Q9ASX5; -.
DR   BioGRID; 15681; 1.
DR   STRING; 3702.AT5G05200.1; -.
DR   PaxDb; Q9ASX5; -.
DR   PRIDE; Q9ASX5; -.
DR   ProteomicsDB; 242832; -.
DR   EnsemblPlants; AT5G05200.1; AT5G05200.1; AT5G05200.
DR   GeneID; 830402; -.
DR   Gramene; AT5G05200.1; AT5G05200.1; AT5G05200.
DR   KEGG; ath:AT5G05200; -.
DR   Araport; AT5G05200; -.
DR   TAIR; locus:2156804; AT5G05200.
DR   eggNOG; KOG1235; Eukaryota.
DR   HOGENOM; CLU_006533_0_1_1; -.
DR   InParanoid; Q9ASX5; -.
DR   OMA; GCESFHA; -.
DR   OrthoDB; 790106at2759; -.
DR   PhylomeDB; Q9ASX5; -.
DR   PRO; PR:Q9ASX5; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9ASX5; baseline and differential.
DR   Genevisible; Q9ASX5; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0032592; C:integral component of mitochondrial membrane; IBA:GO_Central.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0010287; C:plastoglobule; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR   GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   InterPro; IPR004147; ABC1_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   Pfam; PF03109; ABC1; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chloroplast; Kinase; Nucleotide-binding; Plastid;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..58
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           59..540
FT                   /note="Uncharacterized aarF domain-containing protein
FT                   kinase At5g05200, chloroplastic"
FT                   /id="PRO_0000286525"
FT   DOMAIN          195..533
FT                   /note="Protein kinase"
FT   ACT_SITE        362
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         201..209
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   540 AA;  60314 MW;  BFA47FDE7E3D8C5F CRC64;
     MAVSAFRGTR LPLFHHSQFP VARTVSGTSK KMIGARNFKG FVLTAQYSQT QDLFTSRLQS
     QIEKLPKLVE DIVQTSINTG PRGVTRLVQG VQAFVGVGGE WLNDLSKSTS ASGGLPSELQ
     LGLLSPLYLR KLFERMGATY IKLGQFIASA PTLFPPEYVK EFQNCFDKAP PVPFEEIRKI
     LQEELGRPIE SVYEYVDPTP IASASIAQVH GARLRGSQED VVIKVLKPGI EDFLVADLNF
     IYVVSRIFEF LSPEFSRTSL VGIVKDIRES MLEEVDFNKE AQNIESFKRY LETMGLTGQA
     TAPRVYKYCS SRRVLTMERL YGVPLTDLDS IRSLVSSPEN SLITALNVWF GSLLACESFH
     ADVHAGNLWL LRDGRIGFLD FGIVGRISPK TWAAMEVFLA SIATEEYESM ASALIQMGAT
     NRDVDGKAFA KDLEKMFSSI QELDTEIVVA TARGTNSDTT AVAANVVMDE RQMNALFLDL
     VRVSESYGLK FPREFALLLK QLLYFDRYTR LLAPNLNMLQ DQRISIASNK RTNGYKDSFN
 
 
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