PRK1_YEAST
ID PRK1_YEAST Reviewed; 810 AA.
AC P40494; D6VVJ2; Q02553;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Actin-regulating kinase PRK1;
DE EC=2.7.11.1 {ECO:0000269|PubMed:11739778, ECO:0000269|PubMed:12956961, ECO:0000269|PubMed:13679512, ECO:0000269|PubMed:9885245};
DE AltName: Full=p53-regulating kinase 1;
GN Name=PRK1; Synonyms=PAK1; OrderedLocusNames=YIL095W;
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 [MRNA].
RX PubMed=7597081; DOI=10.1073/pnas.92.13.6062;
RA Thiagalingam S., Kinzler K.W., Vogelstein B.;
RT "PAK1, a gene that can regulate p53 activity in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:6062-6066(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP ASP-158.
RX PubMed=9885245; DOI=10.1083/jcb.144.1.71;
RA Zeng G., Cai M.;
RT "Regulation of the actin cytoskeleton organization in yeast by a novel
RT serine/threonine kinase Prk1p.";
RL J. Cell Biol. 144:71-82(1999).
RN [5]
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 [6]
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-158.
RX PubMed=11739778; DOI=10.1091/mbc.12.12.3759;
RA Zeng G., Yu X., Cai M.;
RT "Regulation of yeast actin cytoskeleton-regulatory complex
RT Pan1p/Sla1p/End3p by serine/threonine kinase Prk1p.";
RL Mol. Biol. Cell 12:3759-3772(2001).
RN [8]
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 [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12956961; DOI=10.1016/s0960-9822(03)00579-7;
RA Henry K.R., D'Hondt K., Chang J.S., Nix D.A., Cope M.J., Chan C.S.,
RA Drubin D.G., Lemmon S.K.;
RT "The actin-regulating kinase Prk1p negatively regulates Scd5p, a suppressor
RT of clathrin deficiency, in actin organization and endocytosis.";
RL Curr. Biol. 13:1564-1569(2003).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-158.
RX PubMed=13679512; DOI=10.1091/mbc.e03-06-0362;
RA Huang B., Zeng G., Ng A.Y., Cai M.;
RT "Identification of novel recognition motifs and regulatory targets for the
RT yeast actin-regulating kinase Prk1p.";
RL Mol. Biol. Cell 14:4871-4884(2003).
RN [11]
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 [12]
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402 AND SER-484, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402; SER-428; SER-484;
RP THR-553 AND SER-556, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: Protein kinase involved in the regulation of actin
CC cytoskeleton organization and endocytosis (PubMed:9885245,
CC PubMed:10087264, PubMed:11694597, PubMed:11739778). Phosphorylates PAN1
CC which disrupts the interaction between PAN1 and END3, and between PAN1
CC and SLA1 (PubMed:9885245, PubMed:11739778, PubMed:13679512).
CC Phosphorylates SCD5 (PubMed:12956961, PubMed:13679512). Preferentially,
CC phosphorylates substrates on threonine residues in a [L/I/V/M]-x-x-
CC [Q/N/T/S]-x-T-G motif (PubMed:9885245, PubMed:11739778,
CC PubMed:12956961, PubMed:13679512). {ECO:0000269|PubMed:10087264,
CC ECO:0000269|PubMed:11694597, ECO:0000269|PubMed:11739778,
CC ECO:0000269|PubMed:12956961, ECO:0000269|PubMed:13679512,
CC ECO:0000269|PubMed:9885245}.
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 Evidence={ECO:0000305};
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; Evidence={ECO:0000269|PubMed:11739778,
CC ECO:0000269|PubMed:12956961, ECO:0000269|PubMed:13679512,
CC ECO:0000269|PubMed:9885245};
CC -!- SUBUNIT: Interacts with ABP1, which is required for proper actin patch
CC localization. {ECO:0000269|PubMed:11668184}.
CC -!- INTERACTION:
CC P40494; P15891: ABP1; NbExp=11; IntAct=EBI-9703, EBI-2036;
CC P40494; P80667: PEX13; NbExp=2; IntAct=EBI-9703, EBI-13206;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000269|PubMed:10087264, ECO:0000269|PubMed:14562095}.
CC Note=Cortical actin patches.
CC -!- DISRUPTION PHENOTYPE: Viable (PubMed:9885245). At the restrictive
CC temperature of 37 degrees Celsius, loss of asymmetric localization of
CC cortical actin patches and, delay in emergence and bud growth resulting
CC in the accumulation of unbudded cells (PubMed:9885245).
CC {ECO:0000269|PubMed:9885245}.
CC -!- MISCELLANEOUS: Present with 1323 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; U24167; AAA86529.1; -; mRNA.
DR EMBL; Z46728; CAA86699.2; -; Genomic_DNA.
DR EMBL; BK006942; DAA08458.1; -; Genomic_DNA.
DR PIR; S50889; S50889.
DR RefSeq; NP_012171.1; NM_001179443.1.
DR AlphaFoldDB; P40494; -.
DR BMRB; P40494; -.
DR SMR; P40494; -.
DR BioGRID; 34897; 172.
DR DIP; DIP-6271N; -.
DR IntAct; P40494; 37.
DR MINT; P40494; -.
DR STRING; 4932.YIL095W; -.
DR iPTMnet; P40494; -.
DR MaxQB; P40494; -.
DR PaxDb; P40494; -.
DR PRIDE; P40494; -.
DR EnsemblFungi; YIL095W_mRNA; YIL095W; YIL095W.
DR GeneID; 854713; -.
DR KEGG; sce:YIL095W; -.
DR SGD; S000001357; PRK1.
DR VEuPathDB; FungiDB:YIL095W; -.
DR eggNOG; KOG1989; Eukaryota.
DR GeneTree; ENSGT00940000176643; -.
DR HOGENOM; CLU_011638_2_0_1; -.
DR InParanoid; P40494; -.
DR OMA; QEFNYVQ; -.
DR BioCyc; YEAST:G3O-31354-MON; -.
DR Reactome; R-SCE-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:P40494; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40494; 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; IMP:SGD.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0120133; P:negative regulation of actin cortical patch assembly; IGI:SGD.
DR GO; GO:1900186; P:negative regulation of clathrin-dependent endocytosis; IMP:SGD.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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 ATP-binding; Cytoplasm; Cytoskeleton; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..810
FT /note="Actin-regulating kinase PRK1"
FT /id="PRO_0000086581"
FT DOMAIN 22..298
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 552..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..756
FT /note="Interaction with SH3 domain of ABP1"
FT COMPBIAS 552..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
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 402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 553
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 56
FT /note="K->A: Abolishes protein kinase activity."
FT /evidence="ECO:0000269|PubMed:10087264"
FT MUTAGEN 158
FT /note="D->Y: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:11739778,
FT ECO:0000269|PubMed:13679512, ECO:0000269|PubMed:9885245"
FT CONFLICT 786
FT /note="A -> R (in Ref. 1; AAA86529)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 810 AA; 91032 MW; AF710F930B39BC7E CRC64;
MNTPQISLYE PGTILTVGSH HAKIIKYLTS GGFAQVYTAE ISPPDPYSNA NIACLKRVIV
PHKQGLNTLR AEVDAMKLLR NNKHVVSYID SHAARSVNGI AYEVFVLMEF CERGGLIDFM
NTRLQNRLQE SEILEIMSQT VQGITAMHAL QPPLIHRDIK IENVLISHDG LYKVCDFGSV
SGVIRPPRNT QEFNYVQHDI LTNTTAQYRS PEMIDLYRGL PIDEKSDIWA LGVFLYKICY
YTTPFEKSGE AGILHARYQY PSFPQYSDRL KNLIRLMLME APSQRPNICQ VLEEVSRLQN
KPCPIRNFYL LRAMNQNANT QLAGEPSSTT YVPTQKFIPV QSLQSINQPP NMMPVTHVST
TPNLGTFPIS INDNNKTEVT AHAGLQVGSH SNLTSPLMKT KSVPLSDEFA SLYYKELHPF
QKSQTFKSVE SFQSPQRKSM PPLSLTPVNN DIFDRVSAIN RPNNYVDSET QTIDNMAVPN
LKLSPTITSK SLSSTKEIAA PDNINGSKIV RSLSSKLKKV ITGESRGNSP IKSRQNTGDS
IRSAFGKLRH GFTGNSVNNS RSASFDNNNV NGNGNNTNRR LVSSSTSSFP KFNSDTKRKE
ESDKNQRLEK RRSMPPSILS DFDQHERNNS RTGSRDYYRS HSPVKKTQAS AKTTSKPTLI
PDNGNVNINQ EKKESIQRRV HNLLKSSDDP VTYKSASGYG KYTDIGTETS NRHSSVRITP
ITEEKFKKTL KDGVLDIKTK SNGKDKSRPP RPPPKPLHLR TEIQKIRNFS RLQSKKLPIE
RISSEATETI VDVNVDDLEA DFRKRFPSKV
