AIF1_YEAST
ID AIF1_YEAST Reviewed; 378 AA.
AC P52923; D6W1P9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Apoptosis-inducing factor 1;
DE EC=1.-.-.-;
DE AltName: Full=Cercosporin and photosensitizer-detoxification protein 1;
GN Name=AIF1; Synonyms=CPD1; OrderedLocusNames=YNR074C; ORFNames=N3815;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8904342;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<289::aid-yea909>3.0.co;2-m;
RA Levesque H., Lepingle A., Nicaud J.-M., Gaillardin C.;
RT "Sequencing of a 9.2 kb telomeric fragment from the right arm of
RT Saccharomyces cerevisiae chromosome XIV.";
RL Yeast 12:289-295(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
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 [4]
RP FUNCTION.
RX PubMed=11409174; DOI=10.1007/s002940100189;
RA Ververidis P., Davrazou F., Diallinas G., Georgakopoulos D., Kanellis A.K.,
RA Panopoulos N.;
RT "A novel putative reductase (Cpd1p) and the multidrug exporter Snq2p are
RT involved in resistance to cercosporin and other singlet oxygen-generating
RT photosensitizers in Saccharomyces cerevisiae.";
RL Curr. Genet. 39:127-136(2001).
RN [5]
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15381687; DOI=10.1083/jcb.200404138;
RA Wissing S., Ludovico P., Herker E., Buettner S., Engelhardt S.M.,
RA Decker T., Link A., Proksch A., Rodrigues F., Corte-Real M.,
RA Froehlich K.-U., Manns J., Cande C., Sigrist S.J., Kroemer G., Madeo F.;
RT "An AIF orthologue regulates apoptosis in yeast.";
RL J. Cell Biol. 166:969-974(2004).
RN [7]
RP FUNCTION.
RX PubMed=15939758; DOI=10.1083/jcb.200410064;
RA Vachova L., Palkova Z.;
RT "Physiological regulation of yeast cell death in multicellular colonies is
RT triggered by ammonia.";
RL J. Cell Biol. 169:711-717(2005).
CC -!- FUNCTION: Putative FAD-dependent oxidoreductase involved in the
CC resistance to cercosporin and other singlet oxygen-generating
CC photosensitizers. Translocates from mitochondria to the nucleus under
CC apoptotic conditions, where it degrades DNA and induces apoptosis.
CC {ECO:0000269|PubMed:11409174, ECO:0000269|PubMed:15381687,
CC ECO:0000269|PubMed:15939758}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}. Nucleus
CC {ECO:0000269|PubMed:15381687}. Note=Translocates from mitochondrion to
CC the nucleus upon apoptosis induction.
CC -!- MISCELLANEOUS: Present with 1560 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; X86790; CAA60487.1; -; Genomic_DNA.
DR EMBL; Z71689; CAA96357.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10615.1; -; Genomic_DNA.
DR PIR; S54056; S54056.
DR RefSeq; NP_014472.1; NM_001183251.1.
DR AlphaFoldDB; P52923; -.
DR SMR; P52923; -.
DR BioGRID; 35900; 67.
DR DIP; DIP-4250N; -.
DR IntAct; P52923; 4.
DR STRING; 4932.YNR074C; -.
DR iPTMnet; P52923; -.
DR MaxQB; P52923; -.
DR PaxDb; P52923; -.
DR PRIDE; P52923; -.
DR EnsemblFungi; YNR074C_mRNA; YNR074C; YNR074C.
DR GeneID; 855811; -.
DR KEGG; sce:YNR074C; -.
DR SGD; S000005357; AIF1.
DR VEuPathDB; FungiDB:YNR074C; -.
DR eggNOG; KOG1336; Eukaryota.
DR HOGENOM; CLU_019845_2_0_1; -.
DR InParanoid; P52923; -.
DR OMA; VSQLPFW; -.
DR BioCyc; YEAST:G3O-33378-MON; -.
DR PRO; PR:P52923; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P52923; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IBA:GO_Central.
DR GO; GO:0019646; P:aerobic electron transport chain; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:SGD.
DR GO; GO:0000304; P:response to singlet oxygen; IMP:SGD.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Apoptosis; FAD; Flavoprotein; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nucleus; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..378
FT /note="Apoptosis-inducing factor 1"
FT /id="PRO_0000203486"
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 12..16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 283
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 378 AA; 41335 MW; C0E078B3B0072C1C CRC64;
MTINTKNIVV VGAGVFGVSV ANHLYRELGG TYAIKLVTAS NYVYFLPSAV RLTVSKDYTK
SILPLKNVLD SGIEVIKDTA ASFDDKEVVL GSDRAIKFDI LVLATGSKWA DPIGSTYTFG
DNYKEYFERE ASRISDADHI LFLGGGFVNC ELAGELLFKY LEEIRSGKKR ISIIHNSDKL
LPDSGLYNDT LRKNVTDYLS KNGITLYLNT VGASLDTSPK RIFLGEGSSK YIDADLIYRG
VGISPNVPVN SISDLCDKKG FIQVEKNFRV KAVEAGNVFA IGDVTNFRYH GLVKRDNWVD
VLTRNVISSL QEGTEASLVD ADCLETGHAP SGVSLGPNAG FGQFPLPLLG TINIPSFLIS
RAKSKNLFSD KMEPLFKK
