HAL4_SCHPO
ID HAL4_SCHPO Reviewed; 636 AA.
AC O14019;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Serine/threonine-protein kinase hal4;
DE EC=2.7.11.1;
DE AltName: Full=Halotolerance protein 4;
DE AltName: Full=Serine/threonine-protein kinase ppk10;
GN Name=hal4; Synonyms=ppk10, sat4; ORFNames=SPAC29A4.16;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP IDENTIFICATION.
RX PubMed=15821139; DOI=10.1128/ec.4.4.799-813.2005;
RA Bimbo A., Jia Y., Poh S.L., Karuturi R.K.M., den Elzen N., Peng X.,
RA Zheng L., O'Connell M., Liu E.T., Balasubramanian M.K., Liu J.;
RT "Systematic deletion analysis of fission yeast protein kinases.";
RL Eukaryot. Cell 4:799-813(2005).
RN [3]
RP FUNCTION.
RX PubMed=16164595; DOI=10.1111/j.1365-2443.2005.00891.x;
RA Thornton G., Wilkinson C.R., Toone W.M., Jones N.;
RT "A novel pathway determining multidrug sensitivity in Schizosaccharomyces
RT pombe.";
RL Genes Cells 10:941-951(2005).
RN [4]
RP FUNCTION, AND INTERACTION WITH STY1.
RX PubMed=15870269; DOI=10.1128/mcb.25.10.3945-3955.2005;
RA Wang L.-Y., Shimada K., Morishita M., Shiozaki K.;
RT "Response of fission yeast to toxic cations involves cooperative action of
RT the stress-activated protein kinase Spc1/Sty1 and the Hal4 protein
RT kinase.";
RL Mol. Cell. Biol. 25:3945-3955(2005).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; THR-238; THR-241 AND
RP SER-299, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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:15870269,
CC ECO:0000269|PubMed:16164595}.
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 -!- SUBUNIT: Interacts with sty1. {ECO:0000269|PubMed:15870269}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
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; CU329670; CAB10142.1; -; Genomic_DNA.
DR PIR; T38473; T38473.
DR RefSeq; NP_594866.1; NM_001020295.2.
DR AlphaFoldDB; O14019; -.
DR SMR; O14019; -.
DR BioGRID; 279252; 4.
DR STRING; 4896.SPAC29A4.16.1; -.
DR iPTMnet; O14019; -.
DR MaxQB; O14019; -.
DR PaxDb; O14019; -.
DR PRIDE; O14019; -.
DR EnsemblFungi; SPAC29A4.16.1; SPAC29A4.16.1:pep; SPAC29A4.16.
DR GeneID; 2542804; -.
DR KEGG; spo:SPAC29A4.16; -.
DR PomBase; SPAC29A4.16; hal4.
DR VEuPathDB; FungiDB:SPAC29A4.16; -.
DR eggNOG; KOG0590; Eukaryota.
DR HOGENOM; CLU_000288_127_1_1; -.
DR InParanoid; O14019; -.
DR OMA; QSWINGY; -.
DR PhylomeDB; O14019; -.
DR PRO; PR:O14019; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
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; IBA:GO_Central.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IMP:PomBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
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; 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; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..636
FT /note="Serine/threonine-protein kinase hal4"
FT /id="PRO_0000085986"
FT DOMAIN 351..623
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 181..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 481
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 357..365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 385
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 238
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 241
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 636 AA; 69115 MW; 744C62F52976BB67 CRC64;
MGEKDKLHEI SSKFASLGLG SLKSTPKARE TTEPPPPSSQ QPPSTPNGKE AASPSALKQN
VRPSLNSVQQ TPASIDAVAS SSNVSLQSQQ PLSKPVVSSK PNQTTAMPPP SNNPSRHVSS
TSNKPAAVSP NPAAHHAELP SGSVPPSASV SRANSTATTT PHKAGVVSNP AAANVHVLSV
AASPNPSTPS NGPAPVSTTA TPSRNPVTRL QRIFSQNSVS RQNSRTGRGA AVANTEETNS
TGGSETGGAA NSSSTSNPSS AKWSRFTVYD DASHTHQLRP ARRQEKLGKM LKDFLAGNSK
KREEERIAKE AADAQHQLSL VQSWINGYGQ EKLADKKDPA KVSASFVEKY GRCQEVIGRG
AFGVVRIAHK VDPQNSGSET LYAVKEFRRK PAESQKKYTK RLTSEFCISS SLRHPNVIHT
LDLIQDGKGD YCEVMELCSG GDLYTLIMAA GRLEPMEADC FFKQLMRGVD YLHDMGVAHR
DLKPENLLLT VSGSLKITDF GNGECFRMAW EKEAHMTCGL CGSAPYIAPE EYTESEFDPR
AVDVWACGVI YMAMRTGRHL WRVAKKSEDE YYSRYLMDRK NESGYEPIEM LERSRCRNTL
YNILHPNPTY RLTAKQIMKS EWVRSITLCE AGNAGL
