ID   ARK1_YEAST              Reviewed;         638 AA.
AC   P53974; D6W1F9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 181.
DE   RecName: Full=Actin-regulating kinase 1;
DE            EC=2.7.11.1;
GN   Name=ARK1; OrderedLocusNames=YNL020C; ORFNames=N2823;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-56.
RX   PubMed=10087264; DOI=10.1083/jcb.144.6.1203;
RA   Cope M.J.T.V., Yang S., Shang C., Drubin D.G.;
RT   "Novel protein kinases Ark1p and Prk1p associate with and regulate the
RT   cortical actin cytoskeleton in budding yeast.";
RL   J. Cell Biol. 144:1203-1218(1999).
RN   [4]
RP   FUNCTION.
RX   PubMed=11694597; DOI=10.1091/mbc.12.11.3668;
RA   Watson H.A., Cope M.J.T.V., Groen A.C., Drubin D.G., Wendland B.;
RT   "In vivo role for actin-regulating kinases in endocytosis and yeast epsin
RT   phosphorylation.";
RL   Mol. Biol. Cell 12:3668-3679(2001).
RN   [5]
RP   INTERACTION WITH ABP1.
RX   PubMed=11668184; DOI=10.1074/jbc.m109848200;
RA   Fazi B., Cope M.J.T.V., Douangamath A., Ferracuti S., Schirwitz K.,
RA   Zucconi A., Drubin D.G., Wilmanns M., Cesareni G., Castagnoli L.;
RT   "Unusual binding properties of the SH3 domain of the yeast actin-binding
RT   protein Abp1: structural and functional analysis.";
RL   J. Biol. Chem. 277:5290-5298(2002).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478; SER-522 AND SER-535, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Involved in regulation of actin cytoskeleton organization and
CC       endocytosis. {ECO:0000269|PubMed:10087264,
CC       ECO:0000269|PubMed:11694597}.
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   -!- SUBUNIT: Interacts with ABP1, which is required for proper actin patch
CC       localization. {ECO:0000269|PubMed:11668184}.
CC   -!- INTERACTION:
CC       P53974; P15891: ABP1; NbExp=12; IntAct=EBI-9817, EBI-2036;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC       {ECO:0000269|PubMed:10087264, ECO:0000269|PubMed:14562095}.
CC       Note=Cortical actin patches.
CC   -!- MISCELLANEOUS: Present with 1551 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; Z71296; CAA95882.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10525.1; -; Genomic_DNA.
DR   PIR; S62932; S62932.
DR   RefSeq; NP_014378.1; NM_001182859.1.
DR   PDB; 2RPN; NMR; -; B=605-621.
DR   PDBsum; 2RPN; -.
DR   AlphaFoldDB; P53974; -.
DR   BMRB; P53974; -.
DR   SMR; P53974; -.
DR   BioGRID; 35806; 163.
DR   DIP; DIP-4381N; -.
DR   IntAct; P53974; 18.
DR   MINT; P53974; -.
DR   STRING; 4932.YNL020C; -.
DR   GlyGen; P53974; 12 sites, 1 O-linked glycan (12 sites).
DR   iPTMnet; P53974; -.
DR   MaxQB; P53974; -.
DR   PaxDb; 4932-YNL020C; -.
DR   PeptideAtlas; P53974; -.
DR   EnsemblFungi; YNL020C_mRNA; YNL020C; YNL020C.
DR   GeneID; 855711; -.
DR   KEGG; sce:YNL020C; -.
DR   AGR; SGD:S000004965; -.
DR   SGD; S000004965; ARK1.
DR   VEuPathDB; FungiDB:YNL020C; -.
DR   eggNOG; KOG1989; Eukaryota.
DR   GeneTree; ENSGT00940000176643; -.
DR   HOGENOM; CLU_011638_3_0_1; -.
DR   InParanoid; P53974; -.
DR   OMA; PLPEMWV; -.
DR   OrthoDB; 168953at2759; -.
DR   BioCyc; YEAST:G3O-33058-MONOMER; -.
DR   BioGRID-ORCS; 855711; 0 hits in 13 CRISPR screens.
DR   EvolutionaryTrace; P53974; -.
DR   PRO; PR:P53974; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53974; Protein.
DR   GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
DR   GO; GO:0000147; P:actin cortical patch assembly; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IMP:SGD.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; IMP:SGD.
DR   CDD; cd14037; STKc_NAK_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR22967:SF57; AUXILIN, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR22967; SERINE/THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Cytoskeleton; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..638
FT                   /note="Actin-regulating kinase 1"
FT                   /id="PRO_0000085635"
FT   DOMAIN          22..298
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          482..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          569..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..615
FT                   /note="Interaction with SH3 domain of ABP1"
FT   COMPBIAS        575..592
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..627
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        159
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         28..36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         56
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         478
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358,
FT                   ECO:0007744|PubMed:18407956"
FT   MOD_RES         522
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         535
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MUTAGEN         56
FT                   /note="K->A: Abolishes protein kinase activity."
FT                   /evidence="ECO:0000269|PubMed:10087264"
SQ   SEQUENCE   638 AA;  71373 MW;  139CA4CA1B6A181F CRC64;
     MNQPQIGTYN VGTQLTVGSH QVEIIKYLTS GGFAQVYSAL INPPDPHSNS SVACLKRVIV
     PDKPSLNTLR AEVDAMRLLK NNRYVVSYID SHAAKAMLHN GSYEVFVLME YCERGGLIDF
     MNTRLQNRLH EFEILQIMSQ VTQGVAAMHA LQPPLIHRDI KIENVLISAN NEYKLCDFGS
     VCGIIRPPRN SQELSYVQQD ILKNTTAQYR SPEMIDTFRG LPIDEKSDIW ALGIFLYKLC
     YYTTPFEKGG DLAILSGKFE FPLYPNYSEQ LKGLIRDILV QDPRHRPNVY QLLKRISIMQ
     NVPCPINDIQ VVQAPSSHLN LTELHQLSAT QNILSLNSPT TMENTMPNAT FQISMADNTT
     TAQMHPNRKP SQIAYDASFS NSAKGSQPLF DKSQNMYHAL DPPLVEPLAS SVSNNDNELK
     ANSATKLKQA IVSEAHTFRQ NNSIDFPLQN IIPQYEDSSS SSDESYSGDV DELKKTRSLG
     SYSTRGNIKK NQSVKESLTS SSLPGTSFTP TSTKVNLKHE NSPFKSTFVN TIDNSKDDLN
     KPSYEDLDVS KQNLKNSIQQ RMIDKLNSSE ESFNARKMSK VKLHEKGEID KPTMLKSSGP
     ISKDKKTKPT PPPKPSHLKP KPPPKPLLLA GRKLSLDK
//