HAL5_YEAST
ID HAL5_YEAST Reviewed; 855 AA.
AC P38970; D6VW22;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Serine/threonine-protein kinase HAL5;
DE EC=2.7.11.1;
DE AltName: Full=Halotolerance protein 5;
GN Name=HAL5; OrderedLocusNames=YJL165C; ORFNames=J0531;
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].
RA Kron S.J.;
RT "Saccharomyces cerevisiae HAL5 gene, mRNA.";
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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.
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 [5]
RP FUNCTION.
RX PubMed=15126631; DOI=10.1242/jcs.01050;
RA Munson A.M., Haydon D.H., Love S.L., Fell G.L., Palanivel V.R.,
RA Rosenwald A.G.;
RT "Yeast ARL1 encodes a regulator of K+ influx.";
RL J. Cell Sci. 117:2309-2320(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; SER-72; SER-358; SER-391
RP AND SER-395, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [7]
RP FUNCTION.
RX PubMed=17548466; DOI=10.1128/mcb.01375-06;
RA Perez-Valle J., Jenkins H., Merchan S., Montiel V., Ramos J., Sharma S.,
RA Serrano R., Yenush L.;
RT "Key role for intracellular K+ and protein kinases Sat4/Hal4 and Hal5 in
RT the plasma membrane stabilization of yeast nutrient transporters.";
RL Mol. Cell. Biol. 27:5725-5736(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-19, AND
RP IDENTIFICATION BY 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-68; SER-160; SER-324; SER-336
RP AND SER-395, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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-68; SER-72; SER-273; SER-277;
RP SER-324; SER-333; SER-336 AND SER-395, AND IDENTIFICATION BY MASS
RP 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: Protein kinase involved in salt tolerance and pH sensitivity,
CC probably by regulating plasma membrane potential and cation influx.
CC Positively controls the TRK1-TRK2 potassium transport system in
CC response to potassium starvation. Stabilizes TRK1 in the plasma
CC membrane by preventing its vacuolar sorting and degradation. Also
CC stabilizes other plasma membrane nutrient transporters like CAN1, FUR4
CC and HXT1. May itself be subject to regulation by ARL1.
CC {ECO:0000269|PubMed:10207057, ECO:0000269|PubMed:15126631,
CC ECO:0000269|PubMed:17548466}.
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. NPR/HAL subfamily. HAL5 sub-subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA50395.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U15300; AAA50395.1; ALT_FRAME; mRNA.
DR EMBL; Z49440; CAA89460.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08638.1; -; Genomic_DNA.
DR PIR; S56948; S56948.
DR RefSeq; NP_012370.1; NM_001181598.1.
DR AlphaFoldDB; P38970; -.
DR SMR; P38970; -.
DR BioGRID; 33594; 221.
DR DIP; DIP-6399N; -.
DR IntAct; P38970; 5.
DR MINT; P38970; -.
DR STRING; 4932.YJL165C; -.
DR iPTMnet; P38970; -.
DR MaxQB; P38970; -.
DR PaxDb; P38970; -.
DR PRIDE; P38970; -.
DR EnsemblFungi; YJL165C_mRNA; YJL165C; YJL165C.
DR GeneID; 853274; -.
DR KEGG; sce:YJL165C; -.
DR SGD; S000003701; HAL5.
DR VEuPathDB; FungiDB:YJL165C; -.
DR eggNOG; KOG0590; Eukaryota.
DR GeneTree; ENSGT00940000176608; -.
DR HOGENOM; CLU_016904_0_0_1; -.
DR InParanoid; P38970; -.
DR OMA; FQSGAMG; -.
DR BioCyc; YEAST:G3O-31605-MON; -.
DR PRO; PR:P38970; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P38970; protein.
DR GO; GO:0005886; C:plasma membrane; 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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:SGD.
DR GO; GO:0008104; P:protein localization; IGI: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; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..855
FT /note="Serine/threonine-protein kinase HAL5"
FT /id="PRO_0000085988"
FT DOMAIN 503..837
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 688
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 509..517
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 546
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 855 AA; 95455 MW; 4F23A97996489F39 CRC64;
MGDEKLSRHT SLKRARSLSE SIKGLFKPSG ISGSNNAAAP SSRPGQDQAH SHQTARIITS
NVSSPSISPV HSPVLQAAPK HHKLGVPNIA KLSLSPSREP SLNSENEMFS QESFISEKDE
DEANLLERED LQNKKEEKAR AKHVRSKEAY VPHHRYTVGS DEVERQPRER LKNFPQNAGS
SNPANSNANH VLDQENNFSI DAMLDYDEES KLRRRNSLGV RNHSNRTRSR KNSLSTPRSP
PMKNGNGGMN SNATNNVGNG TGNRIYMRGR NHSDSISASS LPKFQEIECK CILDLGHFKV
FENGYHEHSL RVLPIITNNK NVDSGDEKDA DASVNSGDDG DNDSEANMHK QKSVFSLSGL
FKSHKDGNQQ QQQQQQQEEN GEQINLEKAF SIIPSQRFIK SQTLKKSRTS NLKNGNNDEL
MKNDGKNIPQ IVNPNAAVGV EELKLINALS EKIRKGLKSE NTKGNNGEGR SNSNKQEDSD
DTEGKAGTTN DDTSHKPCSQ KYGKSIGVVG AGAYGVVKIC ARCKTAKDVL PYSTYSNGKK
LFFAVKELKP KPGDQIDKFC TRLTSEFIIG HSLSHPHFEA NAMIAGNVSR TTPPKHVFNA
PNILKILDLM EYSNSFVEVM EFCASGDLYS LLTRNNISNE SNNGSSRLIQ TVKEGSGSPL
HPLEADCFMK QLLNGVQYMH DHGIAHCDLK PENILFQPNG LLKICDFGTS SVFQTAWEKH
VHFQSGAMGS EPYVAPEEFI RDAEYDPRLV DCWSCGIVYC TMVMGQYLWK IAIPEKDSLF
KSFLSEIKDD GQFYLFEELR HVSSELNRLR KIALYRTFQV DPTKRITIEQ LLQSSWMRKT
KCCVVYRHLH TKVSK
