ARK1_YEAST
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 03-AUG-2022, entry version 174.
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; 160.
DR DIP; DIP-4381N; -.
DR IntAct; P53974; 18.
DR MINT; P53974; -.
DR STRING; 4932.YNL020C; -.
DR iPTMnet; P53974; -.
DR MaxQB; P53974; -.
DR PaxDb; P53974; -.
DR PRIDE; P53974; -.
DR EnsemblFungi; YNL020C_mRNA; YNL020C; YNL020C.
DR GeneID; 855711; -.
DR KEGG; sce:YNL020C; -.
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; KAMLHNG; -.
DR BioCyc; YEAST:G3O-33058-MON; -.
DR Reactome; R-SCE-8856828; Clathrin-mediated endocytosis.
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:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; IMP:SGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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
