Reviewed, UniProtKB/Swiss-Prot Q54HC6 (ARKA_DICDI)

Names and origin

Protein names

Recommended name:
    Ankyrin repeat-containing protein kinase A
    EC=2.7.11.1
Alternative name(s):
    Ankyrin repeat-containing protein kinase 1

Gene names

Name:	arkA
Synonyms:	arck-1
ORF Names:	DDB_G0289555

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	1460 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in the development of the fruiting body. Overexpression phenocopies the spnA null phenotype. Ref.2
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subcellular location	Cytoplasm › cytoskeleton. Membrane. Nucleus. Note: Localized in the subcortical region of the cell with some enrichment in cell protrusions. In developed cells, colocalized with spnA. May translocate to the nucleus in response to a regulatory signal. Ref.2
Developmental stage	Not detected during axenic growth. Induced during aggregation with 2 peaks, one at 8 hours at the end of aggregation and one at 15 hours during later morphogenesis. Preferentially expressed in a subclass of prestalk cells. Ref.2
Disruption phenotype	Null cells show weak and late developmental defects. Ref.2
Sequence similarities	Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. Contains 5 ANK repeats. Contains 1 GRAM domain. Contains 1 phorbol-ester/DAG-type zinc finger. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Membrane Nucleus
Domain	ANK repeat Coiled coil Phorbol-ester binding Repeat Transmembrane Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	intracellular signaling cascade Inferred from electronic annotation. Source: InterPro ion transport Inferred from electronic annotation. Source: InterPro protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic membrane Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW diacylglycerol binding Inferred from electronic annotation. Source: UniProtKB-KW extracellular ligand-gated ion channel activity Inferred from electronic annotation. Source: InterPro protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding 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
	Chain	1 – 1460	1460	Ankyrin repeat-containing protein kinase A		PRO_0000354055
Regions
	Transmembrane	1293 – 1313	21	Potential
	Domain	653 – 724	72	GRAM
	Repeat	814 – 843	30	ANK 1
	Repeat	852 – 883	32	ANK 2
	Repeat	887 – 920	34	ANK 3
	Repeat	924 – 955	32	ANK 4
	Repeat	959 – 988	30	ANK 5
	Domain	1112 – 1375	264	Protein kinase
	Zinc finger	499 – 551	53	Phorbol-ester/DAG-type
	Nucleotide binding	1118 – 1126	9	ATP By similarity
	Region	467 – 667	201	Interaction with 14-3-3 protein
	Coiled coil	1425 – 1460	36	Potential
	Compositional bias	19 – 26	8	Poly-Ser
	Compositional bias	111 – 123	13	Poly-Ser
	Compositional bias	124 – 128	5	Poly-Asn
	Compositional bias	218 – 223	6	Poly-Asn
	Compositional bias	226 – 251	26	Poly-Asn
	Compositional bias	270 – 302	33	Thr-rich
	Compositional bias	444 – 460	17	Poly-Asn
	Compositional bias	462 – 471	10	Poly-His
	Compositional bias	569 – 590	22	Poly-Ser
	Compositional bias	1457 – 1460	4	Poly-Asn
Sites
	Active site	1231	1	Proton acceptor By similarity
	Binding site	1139	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54HC6-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 551CB02BD6FA6A3A	FASTA	1,460	161,727
	10 20 30 40 50 60 MSIKLPLSNI NSGGNSNNSS SSNSTSNNNI NINIGNGIPT NIEKMTFEDS ETQKLNIKQQ 70 80 90 100 110 120 SNNNTSTSVC VSSIHSSSPI SSPTSHQVNK SSGSLPPVIK RSPTTTHHHN SSGSNSSSSS 130 140 150 160 170 180 SGSNNNNNQI KTSNGMNKPN PTGFLFGSKP RENSQNKIDD NKGVNLAVST SNSSNNFHKS 190 200 210 220 230 240 HSESNIININ APPVETVNME EIYNNIPSSI SMENIRENEN NNNSSNNNSN NNNNNNNNNN 250 260 270 280 290 300 NSNNINNVNG NKSSLASSTS SISSLSSVST LSTSNAATNT NTNANTTSTT KTTSTVRSTS 310 320 330 340 350 360 PTQFKPRVEF DENNPNAIIL SRQRCKSISS PSDFRLNPPS NVHMPTSSLS TSTSTTNVNG 370 380 390 400 410 420 LLLPNGVGGV SMSFTPSGLP MTPPTNSSQV DTLQMSTESI TIQPSSLDSS SESVSDGLQS 430 440 450 460 470 480 VSGSPVTASP SPTISNNTNA TTTNNNNNTN TNNNNNNNNN QHNHHHHQHS HSQQHDVYQI 490 500 510 520 530 540 KKENFPSSPT SPTLLPSETH DFSSEYSSNP GGKCAICRKP LWSFPISDKS RRCRDCSLVV 550 560 570 580 590 600 HRACVPLATE CPSAKKSPSK LSVPNGNQSN SSSSSSSSSS SSSSSNSSSS NTKGHSRTPS 610 620 630 640 650 660 SPSVSSIPGF QLTSNASQNL HVNSHTLSLL VNGATIDSNH YKRNKKSLEA GARDFHFIFR 670 680 690 700 710 720 GCGIPLDEFP LDSYVCGLYS YFAHGRLYLT ESYVCFYDGF VFDRTKERTK IIKVSNIASI 730 740 750 760 770 780 EKRSSGLNPS AIKIKTFDDQ SFIFTHFMHR EVAFDDLEGL LIHQESLHFA HSIVANNFPG 790 800 810 820 830 840 MNEAIRGQTK RLLSRARLDG HYQIHSKIRC PMPSKEILLM SAIKNNNLDM VVTLLNYYCQ 850 860 870 880 890 900 VNSDEINSVD SKGYTPLHNA VFSECSDQIF MHLLNQKEVR VRERNMDGNT PLHYFCQKFK 910 920 930 940 950 960 SPECQRIVQA MIEKGANINE QNYNGETPLH KAIFNHSVRL LMVYILLKNN ANVNIVNNAG 970 980 990 1000 1010 1020 ESPLHYAVRL GRLDVAKMLL AAGADPTIIS LRDRKTALAL AVDYDVCPEI SDLLRRLDTI 1030 1040 1050 1060 1070 1080 TTSLEMYELE KFQASLVVEE LQKENVVARL DEKLLDKIGC TDKEERRKFL SLKSNRLLIH 1090 1100 1110 1120 1130 1140 HPARTQGAKI ILKEMETMDI KNGKLIISET ELEYTEKIGS GASGKVFKGI YRGRVVAIKV 1150 1160 1170 1180 1190 1200 LKSADDEMTR EDFLKEFGVL ASLESHTIVG LYGVVLEPKI CLVMEYCSNG SIYHSIRKNP 1210 1220 1230 1240 1250 1260 PSWERFFSFV QQMLAGINAL HQSTPQVLHR DIKTLNFLVN HNNKVKVADF GLSRFNTESN 1270 1280 1290 1300 1310 1320 QETLNKTRGT SVYCAPEVFE GKEYNERSDM YSMGIVMWEI VYCVVYGCYM IPYQEYNKMF 1330 1340 1350 1360 1370 1380 NAFQVALLVN SSKRVLRPTI PIGVPQVLKD LIYCLWDHDV SSRPTATEAM TALAVCEKEY 1390 1400 1410 1420 1430 1440 KQNKAQWELV ITKKEPTPLP RVAPLPAFPG YRQFYEQNLD IKPIPEEEQI YQEAMEKQRR 1450 1460 NQEASANRNQ KNKELLNNNN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"The novel ankyrin-repeat containing kinase ARCK-1 acts as a suppressor of the Spalten signaling pathway during Dictyostelium development." Aubry L., Lee S., Ravanel K., Firtel R.A. Dev. Biol. 263:308-322(2003) [PubMed: 14597204] [Abstract] Cited for: SUBCELLULAR LOCATION, FUNCTION, DEVELOPMENTAL STAGE, INTERACTION WITH 14-3-3 PROTEIN, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAFI02000143 Genomic DNA. Translation: EAL62663.1.
RefSeq	XP_636166.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3387740.
GenomeReviews	Gene locus arkA in contig CM000154_GR.
KEGG	ddi:DDB_0229363.
Organism-specific databases
dictyBase	DDB_G0289555. arkA.
Family and domain databases
InterPro	IPR002110. ANK. IPR004182. GRAM. IPR018000. Neurotransmitter_ion_chnl_CS. IPR002219. Prot_Kinase_C-like_PE/DAG_bd. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. [Graphical view]
Gene3D	G3DSA:1.25.40.20. ANK. 1 hit.
Pfam	PF00023. Ank. 5 hits. PF00130. C1_1. 1 hit. PF02893. GRAM. 1 hit. PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00248. ANK. 5 hits. SM00109. C1. 1 hit. SM00568. GRAM. 1 hit. [Graphical view]
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 3 hits. PS00236. NEUROTR_ION_CHANNEL. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. PS00479. ZF_DAG_PE_1. False negative. PS50081. ZF_DAG_PE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARKA_DICDI

Accession

Primary (citable) accession number: Q54HC6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2008
Last sequence update:	May 24, 2005
Last modified:	September 22, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)