WIS4_SCHPO
ID WIS4_SCHPO Reviewed; 1401 AA.
AC O14299; P87062; Q92384;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=MAP kinase kinase kinase wis4;
DE EC=2.7.11.25;
DE AltName: Full=MAP kinase kinase kinase wak1;
DE AltName: Full=MAP kinase kinase kinase wik1;
GN Name=wis4; Synonyms=wak1, wik1; ORFNames=SPAC9G1.02;
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 [GENOMIC DNA].
RX PubMed=9321395; DOI=10.1093/emboj/16.20.6162;
RA Samejima I., Mackie S., Fantes P.A.;
RT "Multiple modes of activation of the stress-responsive MAP kinase pathway
RT in fission yeast.";
RL EMBO J. 16:6162-6170(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 96-1401.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9136929; DOI=10.1101/gad.11.8.1008;
RA Shieh J.C., Wilkinson M.G., Buck V., Morgan B.A., Makino K., Millar J.B.A.;
RT "The Mcs4 response regulator coordinately controls the stress-activated
RT Wak1-Wis1-Sty1 MAP kinase pathway and fission yeast cell cycle.";
RL Genes Dev. 11:1008-1022(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 457-543.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9188094; DOI=10.1091/mbc.8.3.409;
RA Shiozaki K., Shiozaki M., Russell P.;
RT "Mcs4 mitotic catastrophe suppressor regulates the fission yeast cell cycle
RT through the Wik1-Wis1-Spc1 kinase cascade.";
RL Mol. Biol. Cell 8:409-419(1997).
CC -!- FUNCTION: Involved in a signal transduction pathway that is activated
CC in under conditions of heat shock, oxidative stress or limited
CC nutrition. Unlike win1, it is not activated by changes in the
CC osmolarity of the extracellular environment. Activates the wis1 MAP
CC kinase kinase by phosphorylation.
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=2.7.11.25;
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=2.7.11.25;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA69030.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CU329670; CAB11500.1; -; Genomic_DNA.
DR EMBL; Y07750; CAA69030.1; ALT_INIT; Genomic_DNA.
DR EMBL; Y11989; CAA72718.1; -; Genomic_DNA.
DR EMBL; U81521; AAB39762.1; -; Genomic_DNA.
DR PIR; T39225; T39225.
DR RefSeq; NP_593557.1; NM_001018990.2.
DR AlphaFoldDB; O14299; -.
DR SMR; O14299; -.
DR BioGRID; 279318; 41.
DR IntAct; O14299; 2.
DR STRING; 4896.SPAC9G1.02.1; -.
DR iPTMnet; O14299; -.
DR MaxQB; O14299; -.
DR PaxDb; O14299; -.
DR PRIDE; O14299; -.
DR EnsemblFungi; SPAC9G1.02.1; SPAC9G1.02.1:pep; SPAC9G1.02.
DR GeneID; 2542873; -.
DR KEGG; spo:SPAC9G1.02; -.
DR PomBase; SPAC9G1.02; wis4.
DR VEuPathDB; FungiDB:SPAC9G1.02; -.
DR eggNOG; KOG4645; Eukaryota.
DR HOGENOM; CLU_001999_2_0_1; -.
DR InParanoid; O14299; -.
DR OMA; MIHFERE; -.
DR PhylomeDB; O14299; -.
DR BRENDA; 2.7.11.25; 5613.
DR Reactome; R-SPO-389357; CD28 dependent PI3K/Akt signaling.
DR PRO; PR:O14299; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:1990315; C:Mcs4 RR-MAPKKK complex; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA:PomBase.
DR GO; GO:0004672; F:protein kinase activity; IDA:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0000161; P:osmosensory signaling MAPK cascade; IBA:GO_Central.
DR GO; GO:0038066; P:p38MAPK cascade; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0051403; P:stress-activated MAPK cascade; IMP:PomBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017240; MAPKKK_Ssk2/Ssk22.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF037579; MAPKKK_SSK22; 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 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1401
FT /note="MAP kinase kinase kinase wis4"
FT /id="PRO_0000086818"
FT DOMAIN 1037..1306
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 67..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1161
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1043..1051
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1066
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 484..485
FT /note="RL -> SP (in Ref. 3; CAA72718)"
FT /evidence="ECO:0000305"
FT CONFLICT 1346
FT /note="D -> V (in Ref. 1; CAA69030)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1401 AA; 160538 MW; 529A989D2B627F3D CRC64;
MGLEHTFYPA EDRFEPLLEH SEPVNFVPKE NAKSYVRQGF ASPHQSLMDN LVDSTESTKR
SENFVSHIPL TPSHSGQSEK LMSTRTSHSP YISPTMSYTN HSPANLTRNS SFNHQHYSTT
LRSPPSMRGR GIDVNSSHYP HISRPRTSSD SQKMYTRAPV DYYYIQENPY FNNIDQDSIS
DKSLPSTNQS LHHSEEDTES DNDFSESIHP EFDIDVFYKV SNILYDESDL QDPEKRERLE
WHSMLSSVLK GDVMQTEKRR LRLTEPDGHS GTYISEVWLG LQAWLHGRLN ADQAEVIRKS
REGVEPVLRE VIDFQIQDEE TTKPPLEQVT EILEKVEQCK QFYISSREME ENVPLSASKE
FNYKLNALIS WSNVMESIQV ETLVLQKWVG NDEFDLTMRT PQFNYDGVEN TSSFVERIFR
QSGLQRTFEQ RTLTTLNRII HQAKQTISEN AQAFEEMKLP TYEDKLLPLV RFPIKLLEEA
LRLRLAYAKK IKGPNFLIVD SMLDDFKIAL SVAVRIKREY IKIASPSPGW SLPTNVDEDY
DNVLLDSLKF YFKLLTLKLS SGNKNLYFKE IDFLENEWAF LNEHIYWING GDIHMAGQFS
YLSNSLLLNV HRYVESHLNG PTERTAASLT NWYSTLLKNT QIRFRKILRF SETLNSRFEN
ASDFVISEGH LPDLVNRLST TGHFLAYTAN LERDGVFVIA DHTLSENPEA LKALLFSKDI
SNLETIQQNC SYVLILCPVH PIVWKGRIEK VDVPDFSVDL KTNRVRIIAS NKREHLQAAK
SVFQSISGDL VTLAVECRSS ITRVYKEFIR LSKLCMRISS TVVDCVSAVR EACSGVNCHD
LIYHVFSFAA EFGQRILRFL SFDSYWQTKL KRKITSLAVE WISFICDECD LMDRKTFRWG
VGALEFLMLM IRGNNILLID DAMFLKIREK VGKSMAFLLT HFDVLGAKSK VAAKLQREST
EVSSSPRLTS FGDVEEEALS IQLLQKETML RIDELEIERN NTLLERLAIG HVLDDSVFRN
RDFIKLASSF SNITIRWQQG HFVRSGMFGD VYTGVNMETG DLLAVKEIKL QDSRTFRSTV
DQIHNEMTVL ERLNHPNVVT YYGVEVHREK VYIFMEFCQG GSLADLLAHG RIEDENVLKV
YVVQLLEGLA YIHSQHILHR DIKPANILLD HRGMIKYSDF GSALYVSPPT DPEVRYEDIQ
PELQHLAGTP MYMAPEIILG TKKGDFGAMD IWSLGCVILE MMTGSTPWSE MDNEWAIMYH
VAAMHTPSIP QNEKISSLAR DFIEQCFERD PEQRPRAVDL LTHPWITDFR KKTIITMPPA
TITKKTSLSH TITEEKTAQL LAGRHDDSKA ETDSLAASYK EESALPVASN VGLRQPNELR
IDSINLPPAI VTPDTINYSV D
