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 27-MAR-2024, entry version 195. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 179. DR DIP; DIP-6271N; -. DR IntAct; P40494; 37. DR MINT; P40494; -. DR STRING; 4932.YIL095W; -. DR GlyGen; P40494; 9 sites, 1 O-linked glycan (9 sites). DR iPTMnet; P40494; -. DR MaxQB; P40494; -. DR PaxDb; 4932-YIL095W; -. DR PeptideAtlas; P40494; -. DR EnsemblFungi; YIL095W_mRNA; YIL095W; YIL095W. DR GeneID; 854713; -. DR KEGG; sce:YIL095W; -. DR AGR; SGD:S000001357; -. 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 OrthoDB; 168953at2759; -. DR BioCyc; YEAST:G3O-31354-MONOMER; -. DR BioGRID-ORCS; 854713; 0 hits in 13 CRISPR screens. 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:0016310; P:phosphorylation; IEA:UniProtKB-KW. 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 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 //