Q75JK0 (ZAK1_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity protein kinase zakA
EC=2.7.12.1

Alternative name(s):
Zaphod K Kinase 1
Short name=Zaphod kinase 1
Zaphod kinase A

Gene names

Name:	zakA
Synonyms:	zak1
ORF Names:	DDB_G0276025

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	781 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. ZakA negatively regulates prestalk differentiation by regulating expression of ecmB. Phosphorylates Y-214 of gsk3/gskA, in vitro. Ref.3 Ref.4 Ref.5
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.5
Developmental stage	Expression is first seen at 5 hours of development during aggregation, reaching peak expression at slug stage (15 hours). Ref.3
Post-translational modification	N-terminal serine/threonine domain is capable of autophosphorylation, in vitro, but to a lower extent than the tyrosine kinase domain. May function as a negative regulator of the tyrosine kinase domain. C-terminal tyrosine kinase domain is capable of autophosphorylation, in vitro.
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	cAMP-mediated signaling Inferred from mutant phenotype Ref.4. Source: UniProtKB cell fate specification Inferred from mutant phenotype Ref.3. Source: UniProtKB positive regulation of kinase activity Inferred from mutant phenotype Ref.3. Source: UniProtKB protein autophosphorylation Inferred from direct assay Ref.3. Source: dictyBase regulation of aggregation involved in sorocarp development Inferred from mutant phenotype Ref.5. Source: dictyBase regulation of cell fate specification Inferred from mutant phenotype Ref.5. Source: dictyBase regulation of positive chemotaxis to cAMP Inferred from mutant phenotype Ref.5. Source: dictyBase sorocarp morphogenesis Inferred from mutant phenotype Ref.3. Source: dictyBase sporulation resulting in formation of a cellular spore Inferred from mutant phenotype Ref.3. Source: dictyBase
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cAMP-dependent protein kinase activity Inferred from mutant phenotype Ref.4. Source: UniProtKB protein serine/threonine/tyrosine kinase activity Inferred from electronic annotation. Source: EC protein tyrosine kinase activity Inferred from direct assay Ref.3. Source: dictyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 781	781	Dual specificity protein kinase zakA		PRO_0000328187
Regions
	Domain	9 – 317	309	Protein kinase 1
	Domain	379 – 654	276	Protein kinase 2
	Nucleotide binding	15 – 23	9	ATP By similarity
	Nucleotide binding	385 – 393	9	ATP By similarity
	Compositional bias	171 – 210	40	Poly-Asn
	Compositional bias	337 – 340	4	Poly-Asp
	Compositional bias	672 – 681	10	Poly-Asn
	Compositional bias	758 – 776	19	Poly-Asn
Sites
	Active site	132	1	Proton acceptor By similarity
	Active site	507	1	Proton acceptor By similarity
	Binding site	44	1	ATP By similarity
	Binding site	406	1	ATP By similarity
Experimental info
	Sequence conflict	261	1	G → S in AAF14631. Ref.3
	Sequence conflict	759	1	D → G in AAF14631. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q75JK0 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: F7AC84F07398782C	FASTA	781	89,690
	10 20 30 40 50 60 MHYHNKDDWE EISFIGEGQY GRVIKCRKKN GFILNEQVDY VAIKIISKDK FKRNETDILE 70 80 90 100 110 120 KIRLFNIPRY YSHAEDDNFI YIYMEYIEGE NLANILKTKK QGRFKESRII SMIADLVETL 130 140 150 160 170 180 SFLHKHHVIH RDIKTANLVL DKNKNLKLID FGASTIQNKK QFEQYLNETT NNNNNPNNNN 190 200 210 220 230 240 NNNNNNNNNN NNNNNNNNNN NNINNINNNN DLNGSGSGIS TYLNEQYKQS SFAIIGTFNY 250 260 270 280 290 300 MAPEVKRNYR ATRKSDVWSL GCTIIEMAGG DLSQKLNGIP IIPDHLSDTL KDFLNHCLVI 310 320 330 340 350 360 DPKKRSYMEE LLSHKLIVHI IGPNKSKNYG VEPKFKDDDD FEEIENEKDN YLSSRFPAKF 370 380 390 400 410 420 APQYEKPKWE IEFEELEFDK DDSEGGAGNF GDVKKGLLNE TEVAIKFVKK AHCEAITVCD 430 440 450 460 470 480 TFYHEVLILS NLRHPNIVQF MAACIKYGEK ETNHCIVSEW MSGGNLTQFL MNNHKVLENN 490 500 510 520 530 540 PHLRVKLLTD IAKGILYLHK QHIIHRDLTS NNVLLDFKRE ILPNQLYGSN EFTAKVCDFG 550 560 570 580 590 600 LSSNQSESKK LRGGSIHYMA PENLNGSPIN EKSDIYSFGL LVWQMFSYAP PNTIYSPKEM 610 620 630 640 650 660 ASMVSDPKQN YRPQIPFNVP LKFKELITQC WDRNPLNRPK DFSIIIEKLK EIGLTYNRSS 670 680 690 700 710 720 SNVSPINSPL INNNNNNYNN NHLNSLSSSL NSSPTYYAKT FGDSNSNIDV YHSADSITPI 730 740 750 760 770 780 VSSPPIIKID LTQDDWDSKL KQLDLEHENK SLISISINDN NNNNINNNNT NNNNVNDLGY C

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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.
[3]	"The novel tyrosine kinase ZAK1 activates GSK3 to direct cell fate specification." Kim L., Liu J., Kimmel A.R. Cell 99:399-408(1999) [PubMed: 10571182] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-759, FUNCTION, DEVELOPMENTAL STAGE, AUTOPHOSPHORYLATION.
[4]	"Proteomic and microarray analyses of the Dictyostelium Zak1-GSK-3 signaling pathway reveal a role in early development." Strmecki L., Bloomfield G., Araki T., Dalton E., Skelton J., Schilde C., Harwood A., Williams J.G., Ivens A., Pears C. Eukaryot. Cell 6:245-252(2007) [PubMed: 17085634] [Abstract] Cited for: FUNCTION.
[5]	"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: FUNCTION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000014 Genomic DNA. Translation: EAL69312.1. AF200688 mRNA. Translation: AAF14631.1.
RefSeq	XP_643301.1. XM_638209.1.
3D structure databases
HSSP	HSSP built from PDB template 2EVA based on UniProtKB O43318.
ProteinModelPortal	Q75JK0.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0185184; DDB0185184; DDB_G0276025.
GeneID	8620347.
GenomeReviews	Gene locus zakA in contig CM000151_GR.
KEGG	ddi:DDB_G0276025.
Organism-specific databases
dictyBase	DDB_G0276025. zakA.
Phylogenomic databases
eggNOG	KOG0192.
GeneTree	EPrGT00050000000319.
HOGENOM	HBG077009.
OMA	YERADAS.
ProtClustDB	CLSZ2430920.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. 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. 2 hits. PF07714. Pkinase_Tyr. 1 hit. [Graphical view]
PRINTS	PR00109. TYRKINASE.
SMART	SM00220. S_TKc. 2 hits. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 2 hits.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. 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

ZAK1_DICDI

Accession

Primary (citable) accession number: Q75JK0
Secondary accession number(s): Q552C7, Q9U478

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	July 5, 2004
Last modified:	December 14, 2011
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)