ARKA_DICDI
ID ARKA_DICDI Reviewed; 1460 AA.
AC Q54HC6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Ankyrin repeat-containing protein kinase A;
DE EC=2.7.11.1;
DE AltName: Full=Ankyrin repeat-containing protein kinase 1;
GN Name=arkA; Synonyms=arck-1; ORFNames=DDB_G0289555;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP SUBCELLULAR LOCATION, FUNCTION, DEVELOPMENTAL STAGE, INTERACTION WITH
RP 14-3-3 PROTEIN, AND DISRUPTION PHENOTYPE.
RX PubMed=14597204; DOI=10.1016/j.ydbio.2003.07.012;
RA Aubry L., Lee S., Ravanel K., Firtel R.A.;
RT "The novel ankyrin-repeat containing kinase ARCK-1 acts as a suppressor of
RT the Spalten signaling pathway during Dictyostelium development.";
RL Dev. Biol. 263:308-322(2003).
CC -!- FUNCTION: Involved in the development of the fruiting body.
CC Overexpression phenocopies the spnA null phenotype.
CC {ECO:0000269|PubMed:14597204}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:14597204}. Membrane {ECO:0000269|PubMed:14597204}.
CC Nucleus {ECO:0000269|PubMed:14597204}. Note=Localized in the
CC subcortical region of the cell with some enrichment in cell
CC protrusions. In developed cells, colocalized with spnA. May translocate
CC to the nucleus in response to a regulatory signal.
CC -!- DEVELOPMENTAL STAGE: Not detected during axenic growth. Induced during
CC aggregation with 2 peaks, one at 8 hours at the end of aggregation and
CC one at 15 hours during later morphogenesis. Preferentially expressed in
CC a subclass of prestalk cells. {ECO:0000269|PubMed:14597204}.
CC -!- DISRUPTION PHENOTYPE: Null cells show weak and late developmental
CC defects. {ECO:0000269|PubMed:14597204}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000143; EAL62663.1; -; Genomic_DNA.
DR RefSeq; XP_636166.1; XM_631074.1.
DR AlphaFoldDB; Q54HC6; -.
DR SMR; Q54HC6; -.
DR STRING; 44689.DDB0229363; -.
DR PaxDb; Q54HC6; -.
DR PRIDE; Q54HC6; -.
DR EnsemblProtists; EAL62663; EAL62663; DDB_G0289555.
DR GeneID; 8627199; -.
DR KEGG; ddi:DDB_G0289555; -.
DR dictyBase; DDB_G0289555; arkA.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_250812_0_0_1; -.
DR InParanoid; Q54HC6; -.
DR Reactome; R-DDI-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-DDI-170968; Frs2-mediated activation.
DR Reactome; R-DDI-3295583; TRP channels.
DR Reactome; R-DDI-392517; Rap1 signalling.
DR Reactome; R-DDI-430116; GP1b-IX-V activation signalling.
DR Reactome; R-DDI-5213460; RIPK1-mediated regulated necrosis.
DR Reactome; R-DDI-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-DDI-5673000; RAF activation.
DR Reactome; R-DDI-5674135; MAP2K and MAPK activation.
DR Reactome; R-DDI-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-DDI-5675482; Regulation of necroptotic cell death.
DR Reactome; R-DDI-5689880; Ub-specific processing proteases.
DR Reactome; R-DDI-9013424; RHOV GTPase cycle.
DR PRO; PR:Q54HC6; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0030863; C:cortical cytoskeleton; IDA:dictyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd00029; C1; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00109; C1; 1.
DR SMART; SM00568; GRAM; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW ANK repeat; ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Kinase;
KW Membrane; Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..1460
FT /note="Ankyrin repeat-containing protein kinase A"
FT /id="PRO_0000354055"
FT TRANSMEM 1293..1313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 653..724
FT /note="GRAM"
FT REPEAT 814..843
FT /note="ANK 1"
FT REPEAT 852..883
FT /note="ANK 2"
FT REPEAT 887..920
FT /note="ANK 3"
FT REPEAT 924..955
FT /note="ANK 4"
FT REPEAT 959..988
FT /note="ANK 5"
FT DOMAIN 1112..1375
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ZN_FING 499..551
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..667
FT /note="Interaction with 14-3-3 protein"
FT REGION 551..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1434..1460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1425..1460
FT /evidence="ECO:0000255"
FT COMPBIAS 57..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1231
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1118..1126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1460 AA; 161727 MW; 551CB02BD6FA6A3A CRC64;
MSIKLPLSNI NSGGNSNNSS SSNSTSNNNI NINIGNGIPT NIEKMTFEDS ETQKLNIKQQ
SNNNTSTSVC VSSIHSSSPI SSPTSHQVNK SSGSLPPVIK RSPTTTHHHN SSGSNSSSSS
SGSNNNNNQI KTSNGMNKPN PTGFLFGSKP RENSQNKIDD NKGVNLAVST SNSSNNFHKS
HSESNIININ APPVETVNME EIYNNIPSSI SMENIRENEN NNNSSNNNSN NNNNNNNNNN
NSNNINNVNG NKSSLASSTS SISSLSSVST LSTSNAATNT NTNANTTSTT KTTSTVRSTS
PTQFKPRVEF DENNPNAIIL SRQRCKSISS PSDFRLNPPS NVHMPTSSLS TSTSTTNVNG
LLLPNGVGGV SMSFTPSGLP MTPPTNSSQV DTLQMSTESI TIQPSSLDSS SESVSDGLQS
VSGSPVTASP SPTISNNTNA TTTNNNNNTN TNNNNNNNNN QHNHHHHQHS HSQQHDVYQI
KKENFPSSPT SPTLLPSETH DFSSEYSSNP GGKCAICRKP LWSFPISDKS RRCRDCSLVV
HRACVPLATE CPSAKKSPSK LSVPNGNQSN SSSSSSSSSS SSSSSNSSSS NTKGHSRTPS
SPSVSSIPGF QLTSNASQNL HVNSHTLSLL VNGATIDSNH YKRNKKSLEA GARDFHFIFR
GCGIPLDEFP LDSYVCGLYS YFAHGRLYLT ESYVCFYDGF VFDRTKERTK IIKVSNIASI
EKRSSGLNPS AIKIKTFDDQ SFIFTHFMHR EVAFDDLEGL LIHQESLHFA HSIVANNFPG
MNEAIRGQTK RLLSRARLDG HYQIHSKIRC PMPSKEILLM SAIKNNNLDM VVTLLNYYCQ
VNSDEINSVD SKGYTPLHNA VFSECSDQIF MHLLNQKEVR VRERNMDGNT PLHYFCQKFK
SPECQRIVQA MIEKGANINE QNYNGETPLH KAIFNHSVRL LMVYILLKNN ANVNIVNNAG
ESPLHYAVRL GRLDVAKMLL AAGADPTIIS LRDRKTALAL AVDYDVCPEI SDLLRRLDTI
TTSLEMYELE KFQASLVVEE LQKENVVARL DEKLLDKIGC TDKEERRKFL SLKSNRLLIH
HPARTQGAKI ILKEMETMDI KNGKLIISET ELEYTEKIGS GASGKVFKGI YRGRVVAIKV
LKSADDEMTR EDFLKEFGVL ASLESHTIVG LYGVVLEPKI CLVMEYCSNG SIYHSIRKNP
PSWERFFSFV QQMLAGINAL HQSTPQVLHR DIKTLNFLVN HNNKVKVADF GLSRFNTESN
QETLNKTRGT SVYCAPEVFE GKEYNERSDM YSMGIVMWEI VYCVVYGCYM IPYQEYNKMF
NAFQVALLVN SSKRVLRPTI PIGVPQVLKD LIYCLWDHDV SSRPTATEAM TALAVCEKEY
KQNKAQWELV ITKKEPTPLP RVAPLPAFPG YRQFYEQNLD IKPIPEEEQI YQEAMEKQRR
NQEASANRNQ KNKELLNNNN
