AIF1_SCHPO
ID AIF1_SCHPO Reviewed; 611 AA.
AC Q10499; O14004;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Apoptosis-inducing factor 1;
DE EC=1.-.-.-;
GN Name=aif1; ORFNames=SPAC26F1.14c, SPAC29A4.01c;
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 REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
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 (By
CC similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Note=Binds 1 [2Fe-2S] cluster.;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Translocates from mitochondrion to the nucleus upon apoptosis
CC induction. {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 1560 molecules/cell in log phase SD medium.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB55362.4; -; Genomic_DNA.
DR PIR; T38406; T38406.
DR RefSeq; XP_001713117.2; XM_001713065.2.
DR AlphaFoldDB; Q10499; -.
DR SMR; Q10499; -.
DR STRING; 4896.SPAC26F1.14c.1; -.
DR SwissPalm; Q10499; -.
DR MaxQB; Q10499; -.
DR PaxDb; Q10499; -.
DR EnsemblFungi; SPAC26F1.14c.1; SPAC26F1.14c.1:pep; SPAC26F1.14c.
DR PomBase; SPAC26F1.14c; aif1.
DR VEuPathDB; FungiDB:SPAC26F1.14c; -.
DR eggNOG; KOG1336; Eukaryota.
DR HOGENOM; CLU_003291_4_2_1; -.
DR InParanoid; Q10499; -.
DR OMA; IATYPYH; -.
DR PRO; PR:Q10499; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:PomBase.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:PomBase.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; ISO:PomBase.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IBA:GO_Central.
DR Gene3D; 2.102.10.10; -; 1.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Apoptosis; FAD; Flavoprotein; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion outer membrane; Nucleus;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..611
FT /note="Apoptosis-inducing factor 1"
FT /id="PRO_0000116625"
FT DOMAIN 56..154
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 97
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 99
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 117
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 120
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ SEQUENCE 611 AA; 66566 MW; 3885A888830EDC76 CRC64;
MLLRFFINQP RFIQFTFLRN KKDRILGLQL GKQPFRMSSS SGLKQQGLAQ KKKFQLEFDP
SSVSKNGTKT EAKVVGTEFG VLLVRARNTY FATAGKCSHY GAPLAKGVVT SDGHIVCPWH
GACFNAATGD VEDTPAIAAL RTFPVTEEGD GSLWIEVEDK NDNGASVLQP EGCWRNKATE
VYNKGSVETE VTAPHVCIIG GGKGASVAAE YLREKNFKGK ITIFTREDEV PYDRPKLSKS
LLHDISKLAL RSKEYYDDLD ISFHFNTDVT KIDLAEKKIY CGSDEKPTES YTKLILATGG
EPNKLPIPGL DSKNVYLLRS IADASKLAAV TTEAGDKKNI VIIGSSFIGL ELAVVLKDHN
VSVIGMESIP FEKVMGKEVG TALKALHEQN GIAFYLENSI KEVKTSSNDS SKAEHIVLKD
GQSIPADVVI LAAGVKPNLR YLGNAVSLEK DGGVKVDEHC RVLGAEDVYA VGDIAHAPFA
GLPSSGEKSH TRIEHWDVAG NLGRVAADHI LFGNKAGYTT KSFTPYFWSA QGKQLRYCGN
NAAEGFDDVV IQGSLSDYKF ACFFTKGEKV VGVCSIMKDP VVSQCARLFI KDAMPSKSQL
KENFDVLSIP L
