ID   HAL4_YEAST              Reviewed;         603 AA.
AC   P25333; D6VR17;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=Serine/threonine-protein kinase HAL4/SAT4;
DE            EC=2.7.11.1;
DE   AltName: Full=Halotolerance protein 4;
GN   Name=SAT4; Synonyms=HAL4; OrderedLocusNames=YCR008W;
GN   ORFNames=YCR046, YCR101, YCR8W;
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 [GENOMIC DNA].
RX   PubMed=1767593; DOI=10.1002/yea.320070614;
RA   Skala J., Purnelle B., Crouzet M., Aigle M., Goffeau A.;
RT   "The open reading frame YCR101 located on chromosome III from Saccharomyces
RT   cerevisiae is a putative protein kinase.";
RL   Yeast 7:651-655(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA   Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA   Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA   Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA   Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA   Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA   Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA   Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA   Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA   Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA   Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA   Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA   Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA   Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA   Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-240.
RX   PubMed=1580102; DOI=10.1002/yea.320080107;
RA   Biteau N., Fremaux C., Hebrard S., Menara A., Aigle M., Crouzet M.;
RT   "The complete sequence of a 10.8kb fragment to the right of the chromosome
RT   III centromere of Saccharomyces cerevisiae.";
RL   Yeast 8:61-70(1992).
RN   [5]
RP   FUNCTION.
RX   PubMed=10207057; DOI=10.1128/mcb.19.5.3328;
RA   Mulet J.M., Leube M.P., Kron S.J., Rios G., Fink G.R., Serrano R.;
RT   "A novel mechanism of ion homeostasis and salt tolerance in yeast: the Hal4
RT   and Hal5 protein kinases modulate the Trk1-Trk2 potassium transporter.";
RL   Mol. Cell. Biol. 19:3328-3337(1999).
RN   [6]
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   [7]
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   [8]
RP   IDENTIFICATION BY 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: Promotes K(+) uptake, by the potassium transporter TRK1-TRK2,
CC       which leads to the subsequent cellular resistance to toxic cations such
CC       as Na(+), Li(+) and Ca(2+). {ECO:0000269|PubMed:10207057}.
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   -!- MISCELLANEOUS: Present with 1030 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; S76380; AAB20894.1; -; Genomic_DNA.
DR   EMBL; X59720; CAA42325.1; -; Genomic_DNA.
DR   EMBL; Z11114; CAA77445.1; -; Genomic_DNA.
DR   EMBL; BK006937; DAA07486.1; -; Genomic_DNA.
DR   PIR; S17470; OKBY8W.
DR   RefSeq; NP_009934.1; NM_001178721.1.
DR   AlphaFoldDB; P25333; -.
DR   SMR; P25333; -.
DR   BioGRID; 30987; 247.
DR   DIP; DIP-4495N; -.
DR   IntAct; P25333; 5.
DR   MINT; P25333; -.
DR   STRING; 4932.YCR008W; -.
DR   iPTMnet; P25333; -.
DR   MaxQB; P25333; -.
DR   PaxDb; 4932-YCR008W; -.
DR   PeptideAtlas; P25333; -.
DR   EnsemblFungi; YCR008W_mRNA; YCR008W; YCR008W.
DR   GeneID; 850366; -.
DR   KEGG; sce:YCR008W; -.
DR   AGR; SGD:S000000601; -.
DR   SGD; S000000601; SAT4.
DR   VEuPathDB; FungiDB:YCR008W; -.
DR   eggNOG; KOG0590; Eukaryota.
DR   HOGENOM; CLU_000288_127_1_1; -.
DR   InParanoid; P25333; -.
DR   OMA; HEMGVCH; -.
DR   OrthoDB; 5318028at2759; -.
DR   BioCyc; YEAST:G3O-29325-MONOMER; -.
DR   BRENDA; 2.7.11.1; 984.
DR   BioGRID-ORCS; 850366; 0 hits in 13 CRISPR screens.
DR   PRO; PR:P25333; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P25333; Protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IDA: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; IBA:GO_Central.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IGI:SGD.
DR   GO; GO:0030003; P:intracellular monoatomic cation homeostasis; IMP:SGD.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0045807; P:positive regulation of endocytosis; IMP:SGD.
DR   GO; GO:0009249; P:protein lipoylation; IMP:SGD.
DR   GO; GO:0008104; P:protein localization; IGI:SGD.
DR   GO; GO:1903329; P:regulation of iron-sulfur cluster assembly; IMP:SGD.
DR   CDD; cd13994; STKc_HAL4_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; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24343; SERINE/THREONINE KINASE; 1.
DR   PANTHER; PTHR24343:SF537; SERINE_THREONINE-PROTEIN KINASE HAL4_SAT4; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..603
FT                   /note="Serine/threonine-protein kinase HAL4/SAT4"
FT                   /id="PRO_0000085987"
FT   DOMAIN          316..590
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          150..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..301
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        449
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         322..330
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         353
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   603 AA;  66666 MW;  9DD31B74C05EE212 CRC64;
     MTGMNDNNAA IPQQTPRKHA LSSKVMQLFR SGSRSSRQGK ASSNIQPPSN INTNVPSASK
     SAKFGLHTPT TATPRVVSNP SNTAGVSKPG MYMPEYYQSA SPSHSSSSAS LNNHIDINTS
     KSSSAASLTS SVSALSLSPT SAINISSKSL SPKFSHHSNS NTAITPAPTP TASNINNVNK
     ITNTSAPICG RFLVHKDGTH EHHLKNAKRQ EKLSTMIKNM VGASKLRGEA KSAVPDIIMD
     PKTTLKSNKN PPTLFAGFMK QVVDMDDKYP EGAPTSGALN CPERDIYRSD QKDSKNNTHN
     ITTTKKDRQC FAEKYGRCQE VLGKGAFGVV RICQKKNVSS QDGNKSEKLY AVKEFKRRTS
     ESAEKYSKRL TSEFCISSSL HHTNIVTTLD LFQDAKGEYC EVMEYCAGGD LFTLVVAAGK
     LEYMEADCFF KQLIRGVVYM HEMGVCHRDL KPENLLLTHD GVLKITDFGN SECFKMAWEK
     NIHLSGGVCG SSPYIAPEEY IKEEFDPRPV DIWACGVIYM AMRTGRQLWS SAEKDDPFYM
     NYLKGRKEKG GYEPIESLKR ARCRNVIYSM LDPVPYRRIN GKQILNSEWG REIKCCHNGR
     ALK
//