HAL4_YEAST
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 03-AUG-2022, entry version 177.
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}.
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; 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; 243.
DR DIP; DIP-4495N; -.
DR IntAct; P25333; 5.
DR MINT; P25333; -.
DR STRING; 4932.YCR008W; -.
DR iPTMnet; P25333; -.
DR MaxQB; P25333; -.
DR PaxDb; P25333; -.
DR PRIDE; P25333; -.
DR EnsemblFungi; YCR008W_mRNA; YCR008W; YCR008W.
DR GeneID; 850366; -.
DR KEGG; sce:YCR008W; -.
DR SGD; S000000601; SAT4.
DR VEuPathDB; FungiDB:YCR008W; -.
DR eggNOG; KOG0590; Eukaryota.
DR HOGENOM; CLU_000288_127_1_1; -.
DR InParanoid; P25333; -.
DR OMA; VRICHKK; -.
DR BioCyc; YEAST:G3O-29325-MON; -.
DR BRENDA; 2.7.11.1; 984.
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:0030003; P:cellular cation homeostasis; IMP:SGD.
DR GO; GO:0009594; P:detection of nutrient; IMP:SGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IGI:SGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
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:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:1903329; P:regulation of iron-sulfur cluster assembly; IMP:SGD.
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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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
