SNF1_SCHPO
ID SNF1_SCHPO Reviewed; 576 AA.
AC O74536;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=SNF1-like protein kinase ssp2 {ECO:0000303|PubMed:22140232};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P06782};
GN Name=ssp2 {ECO:0000303|PubMed:22140232}; ORFNames=SPCC74.03c;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, AND IDENTIFICATION BY
RP 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).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=22140232; DOI=10.1128/ec.05268-11;
RA Matsuzawa T., Fujita Y., Tohda H., Takegawa K.;
RT "Snf1-like protein kinase Ssp2 regulates glucose derepression in
RT Schizosaccharomyces pombe.";
RL Eukaryot. Cell 11:159-167(2012).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, PHOSPHORYLATION AT THR-189 BY SSP1,
RP MUTAGENESIS OF THR-189, AND SUBCELLULAR LOCATION.
RX PubMed=22375066; DOI=10.1242/jcs.098533;
RA Valbuena N., Moreno S.;
RT "AMPK phosphorylation by Ssp1 is required for proper sexual differentiation
RT in fission yeast.";
RL J. Cell Sci. 125:2655-2664(2012).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 440-576 IN COMPLEX WITH AMK2 AND
RP CBS2, AND SUBUNIT.
RX PubMed=17289942; DOI=10.1126/science.1137503;
RA Townley R., Shapiro L.;
RT "Crystal structures of the adenylate sensor from fission yeast AMP-
RT activated protein kinase.";
RL Science 315:1726-1729(2007).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 440-576 IN COMPLEX WITH AMK2 AND
RP CBS2, AND SUBUNIT.
RX PubMed=17937917; DOI=10.1016/j.str.2007.07.017;
RA Jin X., Townley R., Shapiro L.;
RT "Structural insight into AMPK regulation: ADP comes into play.";
RL Structure 15:1285-1295(2007).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 25-351, AND DOMAIN.
RX PubMed=19474788; DOI=10.1038/nature08075;
RA Chen L., Jiao Z.H., Zheng L.S., Zhang Y.Y., Xie S.T., Wang Z.X., Wu J.W.;
RT "Structural insight into the autoinhibition mechanism of AMP-activated
RT protein kinase.";
RL Nature 459:1146-1149(2009).
CC -!- FUNCTION: Serine/threonine protein kinase essential for release from
CC glucose repression via the phosphorylation of scr1 upon glucose
CC deprivation (PubMed:22140232). Catalytic subunit of the AMP-activated
CC protein kinase complex also known as the SNF1 kinase complex (Snf1c), a
CC central regulator of cellular energy homeostasis, which, in response to
CC a fall in intracellular ATP levels, activates energy-producing pathways
CC and inhibits energy-consuming processes (PubMed:22375066). The complex
CC phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac
CC formation, leading to transcriptional activation through TBP
CC recruitment to the promoters (By similarity). Regulates proper cell
CC cycle exit and sexual differentiation (PubMed:22375066). Regulates also
CC ste11 levels under nitrogen deprivation (PubMed:22375066).
CC {ECO:0000250|UniProtKB:P06782, ECO:0000269|PubMed:22140232,
CC ECO:0000269|PubMed:22375066}.
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 Evidence={ECO:0000250|UniProtKB:P06782};
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; Evidence={ECO:0000250|UniProtKB:P06782};
CC -!- SUBUNIT: Component of the AMP-activated protein kinase complex also
CC known as the SNF1 kinase complex (Snf1c), a heterotrimeric complex
CC composed of a catalytic subunit alpha and 2 regulatory subunits beta
CC (amk2) and gamma (cbs2) (PubMed:17289942, PubMed:17937917).
CC {ECO:0000269|PubMed:17289942, ECO:0000269|PubMed:17937917}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22375066}. Nucleus
CC {ECO:0000269|PubMed:22140232, ECO:0000269|PubMed:22375066}.
CC Note=Nuclear translocation occurs under nitrogen and glucose starvation
CC conditions and depends on Thr-189 phosphorylation by ssp1
CC (PubMed:22375066). {ECO:0000269|PubMed:22375066}.
CC -!- DOMAIN: The regulatory domain (RS) also called auto-inhibitory domain
CC (AID) inhibits kinase activity of the protein kinase domain (KD)
CC (PubMed:19474788). {ECO:0000269|PubMed:19474788}.
CC -!- DOMAIN: The ubiquitin-associated domain (UBA) localized within the AID
CC dampens kinase activation, probably by restraining alpha-gamma
CC associations (By similarity). {ECO:0000250|UniProtKB:P06782}.
CC -!- PTM: Phosphorylation at Thr-189 by ssp1 is required for nuclear entry
CC in nutritionally stressed cells (PubMed:22375066).
CC {ECO:0000269|PubMed:22375066}.
CC -!- DISRUPTION PHENOTYPE: Prevents assimilation of glycerol and fails to
CC induce expression of glycerol dehydrogenase gld1 on glycerol medium
CC (PubMed:22140232). Leads to diminished mating efficiency
CC (PubMed:22375066). {ECO:0000269|PubMed:22140232,
CC ECO:0000269|PubMed:22375066}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
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DR EMBL; CU329672; CAA20833.1; -; Genomic_DNA.
DR PIR; T41587; T41587.
DR RefSeq; NP_588376.1; NM_001023367.2.
DR PDB; 2OOX; X-ray; 2.60 A; A/C=440-576.
DR PDB; 2OOY; X-ray; 2.88 A; A/C=440-576.
DR PDB; 2QR1; X-ray; 2.70 A; A/C=440-576.
DR PDB; 2QRC; X-ray; 2.70 A; A/C=440-576.
DR PDB; 2QRD; X-ray; 2.41 A; A/C=440-576.
DR PDB; 2QRE; X-ray; 3.01 A; A/C=440-576.
DR PDB; 3H4J; X-ray; 2.80 A; A/B=25-351.
DR PDBsum; 2OOX; -.
DR PDBsum; 2OOY; -.
DR PDBsum; 2QR1; -.
DR PDBsum; 2QRC; -.
DR PDBsum; 2QRD; -.
DR PDBsum; 2QRE; -.
DR PDBsum; 3H4J; -.
DR AlphaFoldDB; O74536; -.
DR SMR; O74536; -.
DR BioGRID; 275681; 228.
DR DIP; DIP-29520N; -.
DR IntAct; O74536; 2.
DR STRING; 4896.SPCC74.03c.1; -.
DR iPTMnet; O74536; -.
DR MaxQB; O74536; -.
DR PaxDb; O74536; -.
DR PRIDE; O74536; -.
DR EnsemblFungi; SPCC74.03c.1; SPCC74.03c.1:pep; SPCC74.03c.
DR GeneID; 2539109; -.
DR KEGG; spo:SPCC74.03c; -.
DR PomBase; SPCC74.03c; ssp2.
DR VEuPathDB; FungiDB:SPCC74.03c; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_3_1; -.
DR InParanoid; O74536; -.
DR OMA; MQRITIQ; -.
DR PhylomeDB; O74536; -.
DR BRENDA; 2.7.11.1; 5613.
DR Reactome; R-SPO-1632852; Macroautophagy.
DR Reactome; R-SPO-163680; AMPK inhibits chREBP transcriptional activation activity.
DR Reactome; R-SPO-176187; Activation of ATR in response to replication stress.
DR Reactome; R-SPO-200425; Carnitine metabolism.
DR Reactome; R-SPO-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-SPO-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-SPO-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-SPO-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR EvolutionaryTrace; O74536; -.
DR PRO; PR:O74536; -.
DR Proteomes; UP000002485; Chromosome III.
DR ExpressionAtlas; O74536; differential.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA: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; IDA:PomBase.
DR GO; GO:0061762; P:CAMKK-AMPK signaling cascade; IMP:PomBase.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0010514; P:induction of conjugation with cellular fusion; EXP:PomBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; ISO:PomBase.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:PomBase.
DR GO; GO:0075319; P:positive regulation of ascus development; IMP:CACAO.
DR GO; GO:0140648; P:positive regulation of cell cycle switching, mitotic to meiotic cell cycle; EXP:PomBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0032933; P:SREBP signaling pathway; IMP:PomBase.
DR CDD; cd14334; UBA_SNF1_fungi; 1.
DR InterPro; IPR032270; AMPK_C.
DR InterPro; IPR028375; KA1/Ssp2_C.
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 InterPro; IPR013896; SNF1_UBA.
DR InterPro; IPR015940; UBA.
DR Pfam; PF16579; AdenylateSensor; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08587; UBA_2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF103243; SSF103243; 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.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Carbohydrate metabolism; Cytoplasm; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..576
FT /note="SNF1-like protein kinase ssp2"
FT /id="PRO_0000086669"
FT DOMAIN 34..285
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:19474788"
FT DOMAIN 304..345
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 292..348
FT /note="Auto-inhibitory domain (AID)"
FT /evidence="ECO:0000269|PubMed:19474788"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 40..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 189
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22375066"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 189
FT /note="T->A: Impairs phosphorylation by ssp1 and nuclear
FT localization."
FT /evidence="ECO:0000269|PubMed:22375066"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:3H4J"
FT STRAND 34..43
FT /evidence="ECO:0007829|PDB:3H4J"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:3H4J"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:3H4J"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:3H4J"
FT HELIX 67..72
FT /evidence="ECO:0007829|PDB:3H4J"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:3H4J"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:3H4J"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:3H4J"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:3H4J"
FT HELIX 130..149
FT /evidence="ECO:0007829|PDB:3H4J"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:3H4J"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:3H4J"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:3H4J"
FT TURN 178..183
FT /evidence="ECO:0007829|PDB:3H4J"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:3H4J"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:3H4J"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:3H4J"
FT HELIX 210..226
FT /evidence="ECO:0007829|PDB:3H4J"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:3H4J"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:3H4J"
FT HELIX 256..263
FT /evidence="ECO:0007829|PDB:3H4J"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:3H4J"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:3H4J"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:3H4J"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:3H4J"
FT HELIX 306..314
FT /evidence="ECO:0007829|PDB:3H4J"
FT HELIX 320..326
FT /evidence="ECO:0007829|PDB:3H4J"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:3H4J"
FT HELIX 338..351
FT /evidence="ECO:0007829|PDB:3H4J"
FT STRAND 453..460
FT /evidence="ECO:0007829|PDB:2QRD"
FT HELIX 462..476
FT /evidence="ECO:0007829|PDB:2QRD"
FT STRAND 486..489
FT /evidence="ECO:0007829|PDB:2QR1"
FT HELIX 492..495
FT /evidence="ECO:0007829|PDB:2QRD"
FT STRAND 496..502
FT /evidence="ECO:0007829|PDB:2QRD"
FT HELIX 504..508
FT /evidence="ECO:0007829|PDB:2QRD"
FT STRAND 513..525
FT /evidence="ECO:0007829|PDB:2QRD"
FT STRAND 528..541
FT /evidence="ECO:0007829|PDB:2QRD"
FT TURN 545..547
FT /evidence="ECO:0007829|PDB:2OOX"
FT HELIX 562..575
FT /evidence="ECO:0007829|PDB:2QRD"
SQ SEQUENCE 576 AA; 65996 MW; E5857E8F171E7B50 CRC64;
MQPQEVDLME NSTMRNGARV LPPEAISKRH IGPYIIRETL GEGSFGKVKL ATHYKTQQKV
ALKFISRQLL KKSDMHMRVE REISYLKLLR HPHIIKLYDV ITTPTDIVMV IEYAGGELFD
YIVEKKRMTE DEGRRFFQQI ICAIEYCHRH KIVHRDLKPE NLLLDDNLNV KIADFGLSNI
MTDGNFLKTS CGSPNYAAPE VINGKLYAGP EVDVWSCGIV LYVMLVGRLP FDDEFIPNLF
KKVNSCVYVM PDFLSPGAQS LIRRMIVADP MQRITIQEIR RDPWFNVNLP DYLRPMEEVQ
GSYADSRIVS KLGEAMGFSE DYIVEALRSD ENNEVKEAYN LLHENQVIQE KSHLSKSKRV
DSFLSVSPPA FSEYTSELQK KSKQELIDPT LEGPRWTVSD PPTYAKQTID SNICVLVPTA
EKNKLEMRTL ADAASAVDTS QSTRKKSRRN KWHFGVRCRG DAPEILLAVY RALQRAGAQF
TVPKPVNGKY RSDMYTIKSR WEIPHCKREG KNTYAYIELQ LYEVMPGCFM LDVKSNGYKD
IYSHPERTAD HGMDDLKSSF PFLDLCAMLV CKLFSA
