WIN1_SCHPO
ID WIN1_SCHPO Reviewed; 1436 AA.
AC O74304; Q9P7R1; Q9UTP1; Q9UTR3;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=MAP kinase kinase kinase win1;
DE EC=2.7.11.25;
GN Name=win1; ORFNames=SPAC1006.09, SPAC1250.06c, SPAPJ730.01;
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], AND FUNCTION.
RX PubMed=9693384; DOI=10.1091/mbc.9.8.2325;
RA Samejima I., Mackie S., Warbrick E., Weisman R., Fantes P.A.;
RT "The fission yeast mitotic regulator win1+ encodes an MAP kinase kinase
RT kinase that phosphorylates and activates Wis1 MAP kinase kinase in response
RT to high osmolarity.";
RL Mol. Biol. Cell 9:2325-2335(1998).
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 INTERACTION WITH TEA4.
RX PubMed=15936270; DOI=10.1016/j.cub.2005.04.061;
RA Tatebe H., Shimada K., Uzawa S., Morigasaki S., Shiozaki K.;
RT "Wsh3/Tea4 is a novel cell-end factor essential for bipolar distribution of
RT Tea1 and protects cell polarity under environmental stress in S. pombe.";
RL Curr. Biol. 15:1006-1015(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND THR-226, AND
RP 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: Involved in a signal transduction pathway that is activated
CC by changes in the osmolarity of the extracellular environment.
CC Activates the wis1 MAP kinase kinase by phosphorylation.
CC {ECO:0000269|PubMed:9693384}.
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 -!- SUBUNIT: Interacts with tea4. {ECO:0000269|PubMed:15936270}.
CC -!- INTERACTION:
CC O74304; O60132: tea4; NbExp=2; IntAct=EBI-1099995, EBI-1099982;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
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; AJ223190; CAA11161.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB60239.1; -; Genomic_DNA.
DR PIR; T37556; T37556.
DR PIR; T50298; T50298.
DR PIR; T50457; T50457.
DR RefSeq; NP_594856.2; NM_001020285.2.
DR AlphaFoldDB; O74304; -.
DR SMR; O74304; -.
DR BioGRID; 279426; 11.
DR IntAct; O74304; 1.
DR STRING; 4896.SPAC1006.09.1; -.
DR iPTMnet; O74304; -.
DR MaxQB; O74304; -.
DR PaxDb; O74304; -.
DR PRIDE; O74304; -.
DR EnsemblFungi; SPAC1006.09.1; SPAC1006.09.1:pep; SPAC1006.09.
DR GeneID; 2542988; -.
DR KEGG; spo:SPAC1006.09; -.
DR PomBase; SPAC1006.09; win1.
DR VEuPathDB; FungiDB:SPAC1006.09; -.
DR eggNOG; KOG4645; Eukaryota.
DR HOGENOM; CLU_001999_2_0_1; -.
DR InParanoid; O74304; -.
DR OMA; CQNLIHY; -.
DR PhylomeDB; O74304; -.
DR BRENDA; 2.7.11.25; 5613.
DR Reactome; R-SPO-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-SPO-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-SPO-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-SPO-5676590; NIK-->noncanonical NF-kB signaling.
DR PRO; PR:O74304; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:1990315; C:Mcs4 RR-MAPKKK complex; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase 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; IPR017441; Protein_kinase_ATP_BS.
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; 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; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1436
FT /note="MAP kinase kinase kinase win1"
FT /id="PRO_0000086816"
FT DOMAIN 1120..1406
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 56..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..1123
FT /note="Interaction with tea4"
FT COMPBIAS 61..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1244
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1126..1134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 226
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1436 AA; 163273 MW; D55736C3D99D0AAB CRC64;
MENILDPSVV NSHILENGSR RSSINPILDS ELRDKTFEKA HRRSLTLLSS FTSSMLELPN
NGKEENHRRP SVARSSSDRS KASAKEDLFS EAFRMAEQPP AEALTISTPV DPINIDELDR
AYAVSPSDTS NLLHPPTSSS SIPIPIKNAG HSNLDHPIRP SLQSSISSNR IIKSPGIKED
DYMHRGRSIS SPMIDVEHIN STAVPSKTKN LPEKPKRSHK LRNSITFAKI EDHPERKSQL
RRLSSSLKCF DPEYDYNDPS LSIRRDSSTY YFSNVNETYD EEDSDLDSET STVNWVQSVL
NLPSLLSDDL MANPKNKERF EWQYMLTSVL TGDIVRSEKL RLRKIASSRE GRNSDYSDNL
WMEIWCWLTH RSVDSYRENL KHLRTGMVDV LLAIMNFHWD ESNELTPIVA VDNMLQKLDK
YERLYPSRRS ILQEHSLYAS ESFQHKLDVL TAYSNVTHAL EIQVNIIRSW VGNEEMDITK
NTTNSINNVS QISNGPFVER FYRETGLIRA FEQRIMTNMN SVLSKVCNTI VTYADDLKSY
GLPLIADDYM RLLSFPFRLI KEFLNLRLSC AENITSISLF TIDSLLDDLR NTMKVAVHII
QQHTVLIKPF RDDSKFVDEN QSLNNILVAS LKFYFNLLHR KVRNGCALLH FKETEILEGE
WDFLLAVCPH IEHGFQIMSK SLSSLVGEIL TNINRYLKDQ LQGPDTDDSA LITSFYIKVL
DCVRIRFRKL MSFTRILKAH LENSCEYVIK ENSLSLLIQR LEESNHVLTY TASIEHEGAY
VIVPGHLVDS PNILREVLSM TFNKGDNNFE SVPPYAVVLA PDSSICWNGH VTDLDIPEVS
ISIAPNCVRL VTLATANQLS VIEDYFISIV GDTVSLVDSA KANSSKINKQ MTKIKRNSLK
LALSLLDVIQ TIRTRYHGMN CQNLIHYSFS YAIEFAQRLM RLSILDASSI GLIRRKMIQL
AISWVGFIYE DCSPTDRNTF RWTVTALEFA MIMTYGSNIL MIDKKSFEEL KEKVGKCVAL
LLLHFDVMGT KHAGRSMDQQ AGDIPARLVR NNSDRSRLSD NELASFVKEE VMHRIIELES
NRRDRLYKSQ LIGRVLDDTT KENRLLKELA SSKSNITIRW QQGGLIGSGS FGTVYRAVNL
DTGDLMAVKE VALHKPRISR PMIKRIKGEM LVLELFDHPN VVSYYGIEVH REKVNIFMEL
CQGSSLFEFL RYGRIEDELV IQVYVLQLLE GLAYIHSCGV SHQDVKPENI LFDHNGIMKF
TDFGSAKMSG SASTKIFEQL TQQEEEEFEK DSEFLQHLDQ NRGYSLTGTP TYMAPELILG
NPSERVGAMD IWSLGCVIVE MATGSPPWPR LDNHFSLMYH IAAHNPPIIP ADDQLSPLGQ
NFLKRCFVSD PNQRATAAEL LMDPWVYPLR AGTEFDLMNS SVVESAPSTN GAPLEL
