Reviewed, UniProtKB/Swiss-Prot Q06548 (APK1A_ARATH)

Names and origin

Protein names

Recommended name:
    Protein kinase APK1A, chloroplastic
    EC=2.7.11.1

Gene names

Name:	APK1A
Ordered Locus Names:	At1g07570
ORF Names:	F22G5.5

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	410 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Possible bi-functional kinase. In vitro, it exhibits serine/threonine activity. In vivo, can phosphorylate tyrosine residues of limited substrates.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subcellular location	Plastid › chloroplast Potential.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 1 protein kinase domain.
Sequence caution	The sequence AAF79545.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay. Source: TAIR
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Ref.1 Inferred from direct assay. Source: TAIR protein tyrosine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 38	38	Chloroplast Potential
	Chain	39 – 410	372	Protein kinase APK1A, chloroplastic		PRO_0000024302
Regions
	Domain	68 – 352	285	Protein kinase
	Nucleotide binding	74 – 82	9	ATP By similarity
Sites
	Active site	203	1	Proton acceptor By similarity
	Binding site	106	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q06548-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 5BAB28D9E0065082	FASTA	410	45,519
	10 20 30 40 50 60 MGICLSAQVK AESSGASTKY DAKDIGSLGS KASSVSVRPS PRTEGEILQS PNLKSFSFAE 70 80 90 100 110 120 LKSATRNFRP DSVLGEGGFG CVFKGWIDEK SLTASRPGTG LVIAVKKLNQ DGWQGHQEWL 130 140 150 160 170 180 AEVNYLGQFS HRHLVKLIGY CLEDEHRLLV YEFMPRGSLE NHLFRRGLYF QPLSWKLRLK 190 200 210 220 230 240 VALGAAKGLA FLHSSETRVI YRDFKTSNIL LDSEYNAKLS DFGLAKDGPI GDKSHVSTRV 250 260 270 280 290 300 MGTHGYAAPE YLATGHLTTK SDVYSFGVVL LELLSGRRAV DKNRPSGERN LVEWAKPYLV 310 320 330 340 350 360 NKRKIFRVID NRLQDQYSME EACKVATLSL RCLTTEIKLR PNMSEVVSHL EHIQSLNAAI 370 380 390 400 410 GGNMDKTDRR MRRRSDSVVS KKVNAGFARQ TAVGSTVVAY PRPSASPLYV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Novel protein kinase of Arabidopsis thaliana (APK1) that phosphorylates tyrosine, serine and threonine." Hirayama T., Oka A. Plant Mol. Biol. 20:653-662(1992) [PubMed: 1450380] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Web resources

Plant receptor kinase resource

Cross-references

Sequence databases
EMBL GenBank DDBJ	D12522 mRNA. Translation: BAA02092.1. AC022464 Genomic DNA. Translation: AAF79545.1. Sequence problems. BT004055 mRNA. Translation: AAO42086.1. BT005112 mRNA. Translation: AAO50645.1.
IPI	IPI00547844.
PIR	S28615.
RefSeq	NP_172237.1. NP_973778.1.
UniGene	At.348 Rra.28547
3D structure databases
SMR	Q06548. Positions 58-358.
ModBase	Search...
Proteomic databases
PRIDE	Q06548.
Genome annotation databases
GeneID	837271.
GenomeReviews	Gene locus AT1G07570 in contig CT485782_GR.
KEGG	ath:AT1G07570.
NMPDR	fig|3702.1.peg.941.
Organism-specific databases
GeneFarm	1710. 129.
TAIR	At1g07570.
Phylogenomic databases
eggNOG	KOG1187.
HOGENOM	HBG755340.
InParanoid	Q06548.
OMA	TECEILQ.
PhylomeDB	Q06548.
Enzyme and pathway databases
BRENDA	2.7.10.2. 302. 2.7.11.1. 302.
Gene expression databases
ArrayExpress	Q06548.
Genevestigator	Q06548.
GermOnline	AT1G07570. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR008271. Ser/Thr_prot_kinase_AS. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

APK1A_ARATH

Accession

Primary (citable) accession number: Q06548
Secondary accession number(s): Q9LNY0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	February 9, 2010
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)