Q552C6 (ZAK2_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity protein kinase zak2
EC=2.7.12.1

Alternative name(s):
Tyrosine-protein kinase 4
Zaphod K Kinase 2
Short name=Zaphod kinase 2

Gene names

Name:	zak2
Synonyms:	DpyK4, pyk4
ORF Names:	DDB_G0276187

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	635 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Positive regulator of gsk3/gskA activity required for cell pattern formation and a downstream effector of carC. The kinases, gsk3/gskA, zakA and zak2, form part of a signaling pathway that responds to extracellular cyclic AMP. The pathway has a role in transcriptional regulation; required to direct prespore/spore fates during development. Zak2 negatively regulates prestalk differentiation by regulating expression of ecmA. Phosphorylates Y-214 of gsk3/gskA, in vitro. Ref.2
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Tissue specificity	ZakA and zak2 are coexpressed in prestalk cell population, zakA is enriched in pstB populations and zak1 in pstA populations. ZakA and zak2 are coexpressed in prespore cells, zakA expression levels are 10 fold higher than zak2. Ref.2
Developmental stage	Expressed during the growth phase and throughout the major developmental stages. Ref.2
Post-translational modification	C-terminal tyrosine kinase domain is capable of autophosphorylation, in vitro.
Disruption phenotype	Abnormal morphology of the terminal fruiting body; the sorus, or large spore mass atop an elongated stalk of vacuolated cells, does not form and the stalk structure is expanded. Ref.2
Miscellaneous	'Zaphod' is a fictional ex-president of the galaxy with 2 heads.
Sequence similarities	In the N-terminal section; belongs to the protein kinase superfamily. Ser/Thr protein kinase family. In the C-terminal section; belongs to the protein kinase superfamily. TKL Tyr protein kinase family. Contains 2 protein kinase domains.

Ontologies

Keywords
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	positive regulation of protein kinase activity Inferred from direct assay Ref.2. Source: dictyBase protein autophosphorylation Inferred from direct assay Ref.1. Source: dictyBase regulation of cell fate specification Inferred from mutant phenotype Ref.2. Source: dictyBase regulation of gene expression Inferred from direct assay Ref.2. Source: dictyBase sorocarp morphogenesis Inferred from mutant phenotype Ref.2. Source: dictyBase sporulation resulting in formation of a cellular spore Inferred from mutant phenotype Ref.2. Source: dictyBase
Molecular function	ATP binding Inferred by curator Ref.1. Source: dictyBase protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine/tyrosine kinase activity Inferred from electronic annotation. Source: EC protein tyrosine kinase activity Inferred from direct assay Ref.2Ref.1. Source: dictyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 635	635	Dual specificity protein kinase zak2		PRO_0000355202
Regions
	Domain	9 – 249	241	Protein kinase 1
	Domain	299 – 585	287	Protein kinase 2
	Nucleotide binding	15 – 23	9	ATP By similarity
	Nucleotide binding	305 – 313	9	ATP By similarity
	Compositional bias	589 – 627	39	Ser-rich
Sites
	Active site	124	1	Proton acceptor By similarity
	Active site	427	1	Proton acceptor By similarity
	Binding site	45	1	ATP By similarity
	Binding site	326	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q552C6 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 96FC2977A4771AF7	FASTA	635	72,979
	10 20 30 40 50 60 MNSHKKEEWE EISSIGSCNS KSRVLKCRKK NGLIENEKVD IVAVKIINKK FFKRNETDIL 70 80 90 100 110 120 EKIRLFNIPR YYSHAEDDNY IYIYMEYIED KKQLRFKESE IISMIADLTE TLSFLHKHQI 130 140 150 160 170 180 LHRDIKPSNI ILDKNGVLKL IDFGSSIIDQ QQDDGDNICK ESSFAITGTH TYMAPEVKKL 190 200 210 220 230 240 HRSTKKSDVW SLGCTVLEIV GGNPKKIFDG IPIIPNHVSE IMVDFIKRCL IIDPNKRSHM 250 260 270 280 290 300 EELLTHRLIS SMVGQNKNRE NNIEPKFNND YLSSKFPERF APRFEKPKWE IEFNELKFNK 310 320 330 340 350 360 DDTVGGDGFF SVVKKGYYNE TEVAIKLIKK AHGENVTVCD TFYHEVLIIS NLRHPNIVQF 370 380 390 400 410 420 IAACIKFDNK EVNHCIVSEW MSGGNLSQFI SNERKILEIN PHLRVKILLD IAKGMLYSHR 430 440 450 460 470 480 QGIIHRDLTS NNVLLNFRKK KLLNNNSSNN DEQFYDSDEI IAKVCDFGLS SNQSESKKLR 490 500 510 520 530 540 GGSIHYMAPE NLNGSPINEK SDIYSFGLLV WQMFSYASPN TIYSPKEMAS MVSDEKLNYR 550 560 570 580 590 600 PQIPFNVPLK FKELITQCWD RNPLNRPKDF SEIIDKLKDI NQIYFQDNSN ASTISSTAIT 610 620 630 TTISTISISN SGNSSYSTSD DSSTYGSGFY NSGFL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Classification of tyrosine kinases from Dictyostelium discoideum with two distinct, complete or incomplete catalytic domains." Adler K., Gerisch G., von Hugo U., Lupas A., Schweiger A. FEBS Lett. 395:286-292(1996) [PubMed: 8898113] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], AUTOPHOSPHORYLATION.
[2]	"Combinatorial cell-specific regulation of GSK3 directs cell differentiation and polarity in Dictyostelium." Kim L., Brzostowski J., Majithia A., Lee N.S., McMains V., Kimmel A.R. Development 138:421-430(2011) [PubMed: 21205787] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[3]	"Sequence and analysis of chromosome 2 of Dictyostelium discoideum." Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A., Noegel A.A. Nature 418:79-85(2002) [PubMed: 12097910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[4]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000014 Genomic DNA. Translation: EAL69393.1.
RefSeq	XP_643302.1. XM_638210.1.
3D structure databases
HSSP	HSSP built from PDB template 1ZYD based on UniProtKB P15442.
ProteinModelPortal	Q552C6.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0229958; DDB0229958; DDB_G0276187.
GeneID	8620348.
GenomeReviews	Gene locus pyk4 in contig CM000151_GR.
KEGG	ddi:DDB_G0276187.
Organism-specific databases
dictyBase	DDB_G0276187. zak2.
Phylogenomic databases
eggNOG	KOG0192.
GeneTree	EPrGT00050000000319.
HOGENOM	HBG077009.
OMA	APEYYYR.
PhylomeDB	Q552C6.
ProtClustDB	CLSZ2430920.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017442. Se/Thr_kinase-like_dom. IPR001245. Ser-Thr/Tyr_kinase. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. IPR008266. Tyr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. PF07714. Pkinase_Tyr. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 2 hits. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 2 hits.
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 2 hits. PS00108. PROTEIN_KINASE_ST. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ZAK2_DICDI

Accession

Primary (citable) accession number: Q552C6
Secondary accession number(s): Q75JK1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2008
Last sequence update:	May 24, 2005
Last modified:	December 14, 2011
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)