SELO_YEAST
ID SELO_YEAST Reviewed; 688 AA.
AC Q08968; D6W3E8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein adenylyltransferase SelO, mitochondrial {ECO:0000305};
DE EC=2.7.7.- {ECO:0000269|PubMed:30270044};
DE AltName: Full=Selenoprotein O {ECO:0000303|PubMed:30270044};
DE Short=SelO {ECO:0000303|PubMed:30270044};
DE Flags: Precursor;
GN Name=FMP40 {ECO:0000312|SGD:S000006143};
GN OrderedLocusNames=YPL222W {ECO:0000312|SGD:S000006143};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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 [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [6]
RP INDUCTION.
RX PubMed=17938904; DOI=10.1007/s00253-007-1234-z;
RA Cheraiti N., Sauvage F.-X., Salmon J.-M.;
RT "Acetaldehyde addition throughout the growth phase alleviates the
RT phenotypic effect of zinc deficiency in Saccharomyces cerevisiae.";
RL Appl. Microbiol. Biotechnol. 77:1093-1109(2008).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION
RP PHENOTYPE, DISULFIDE BOND, AND MUTAGENESIS OF ASP-348.
RX PubMed=30270044; DOI=10.1016/j.cell.2018.08.046;
RA Sreelatha A., Yee S.S., Lopez V.A., Park B.C., Kinch L.N., Pilch S.,
RA Servage K.A., Zhang J., Jiou J., Karasiewicz-Urbanska M., Lobocka M.,
RA Grishin N.V., Orth K., Kucharczyk R., Pawlowski K., Tomchick D.R.,
RA Tagliabracci V.S.;
RT "Protein AMPylation by an Evolutionarily Conserved Pseudokinase.";
RL Cell 175:809-821(2018).
CC -!- FUNCTION: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to
CC Tyr residues of target mitochondrial proteins (AMPylation)
CC (PubMed:30270044). Involved in redox homeostasis by regulating the
CC cellular response to oxidative stress (PubMed:30270044). Regulates
CC protein S-glutathionylation levels possibly by AMPylation of
CC deglutathionylation enzymes such as glutaredoxins (PubMed:30270044).
CC {ECO:0000269|PubMed:30270044}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-
CC tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136,
CC Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:83624;
CC Evidence={ECO:0000269|PubMed:30270044};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54289;
CC Evidence={ECO:0000269|PubMed:30270044};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q87VB1};
CC -!- INTERACTION:
CC Q08968; P33203: PRP40; NbExp=2; IntAct=EBI-29375, EBI-701;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:30270044}.
CC -!- INDUCTION: Induced in absence of non-fermentable carbon sources
CC including glycerol, lactate, and acetate (at protein level)
CC (PubMed:30270044). Expression is regulated by zinc levels
CC (PubMed:17938904). {ECO:0000269|PubMed:17938904,
CC ECO:0000269|PubMed:30270044}.
CC -!- PTM: Forms probably one or more intrachain disulfide bridges.
CC {ECO:0000269|PubMed:30270044}.
CC -!- DISRUPTION PHENOTYPE: Reduced growth and survival in presence of oxygen
CC reactive species. {ECO:0000269|PubMed:30270044}.
CC -!- MISCELLANEOUS: Present with 2430 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SELO family. {ECO:0000305}.
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DR EMBL; Z73578; CAA97937.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11214.1; -; Genomic_DNA.
DR PIR; S65241; S65241.
DR RefSeq; NP_015102.1; NM_001184036.1.
DR AlphaFoldDB; Q08968; -.
DR SMR; Q08968; -.
DR BioGRID; 35963; 55.
DR DIP; DIP-2001N; -.
DR IntAct; Q08968; 6.
DR MINT; Q08968; -.
DR STRING; 4932.YPL222W; -.
DR iPTMnet; Q08968; -.
DR MaxQB; Q08968; -.
DR PaxDb; Q08968; -.
DR PRIDE; Q08968; -.
DR EnsemblFungi; YPL222W_mRNA; YPL222W; YPL222W.
DR GeneID; 855879; -.
DR KEGG; sce:YPL222W; -.
DR SGD; S000006143; FMP40.
DR VEuPathDB; FungiDB:YPL222W; -.
DR eggNOG; KOG2542; Eukaryota.
DR HOGENOM; CLU_010245_2_1_1; -.
DR InParanoid; Q08968; -.
DR OMA; HVVNLNA; -.
DR BioCyc; YEAST:G3O-34111-MON; -.
DR PRO; PR:Q08968; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08968; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070733; F:protein adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0045454; P:cell redox homeostasis; IDA:UniProtKB.
DR GO; GO:0018117; P:protein adenylylation; IDA:UniProtKB.
DR HAMAP; MF_00692; SelO; 1.
DR InterPro; IPR003846; SelO.
DR PANTHER; PTHR32057; PTHR32057; 1.
DR Pfam; PF02696; SelO; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Disulfide bond; Magnesium; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:30270044"
FT CHAIN 24..688
FT /note="Protein adenylyltransferase SelO, mitochondrial"
FT /id="PRO_0000121401"
FT ACT_SITE 338
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 132..135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 168..169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 339
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1"
FT BINDING 348
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:30270044"
FT MUTAGEN 348
FT /note="D->A: Loss of catalytic activity. Loss of ATP
FT binding. Reduced survival and growth in response to
FT reactive oxygen species."
FT /evidence="ECO:0000269|PubMed:30270044"
SQ SEQUENCE 688 AA; 78313 MW; 7C56CD503ED24B1E CRC64;
MGEKRTIIKA LKNSAASHFI KKLTADTSLS SIQEAINVVQ QYNATDPVRL KLFHTPRMVS
QGAHFAFCLP TKKPHYKPLL LSQNALDEFN LVQDQDLEKI LSGEKVYYSD SIFPYSTVYS
GFQFGSFAAQ LGDGRVVNLF DLKDKCSGQW QTFQLKGAGM TPFSRFADGK AVLRSSIREF
IMSEALHSIG IPSTRAMQLT LLPGTKAQRR NQEPCAVVCR FAPSWIRLGN FNLFRWRHDL
KGLIQLSDYC IEELFAGGTQ FEGKPDFNIF KRDFFPDTET KIDEQVEKDE TEVSTMTGDN
ISTLSKYDEF FRHVVSLNAN TVAHWQAYGF ANGVLNTDNT SIMGLTIDYG PFAFLDKFEP
SFTPNHDDTA KRYSFANQPS IIWWNLQQFA KDLACLLGPE ARDLELLLKG ELNSVDDALE
KTMIERVQKL VELSANEYKY VFTTRYAQIM SQRLGVDLDL EKCMSSTNLK DIEHAAEKAK
EFCDVIVEPL LDILQATKVD YNNFFIHLQN YKGPFFIKDK SDTATLFGAF DEEYLGMFFN
SKQLQQMAET EEAFAAGEKV FDANGELRLL NEKLQEIRNW TQDYLTLVPP TETAARASLA
KKANPLFVPR SWVLEEVVDD LMYSQRDGLQ DPSSELDTSA LKKLYLMSVN PYDRTKWDVT
LRPELETKWA DLSHQDDAKF MMQASCSS
