AIFM3_MOUSE
ID AIFM3_MOUSE Reviewed; 605 AA.
AC Q3TY86; Q0VBD6; Q4VAA4; Q8BWV0;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Apoptosis-inducing factor 3;
DE EC=1.-.-.-;
DE AltName: Full=Apoptosis-inducing factor-like protein;
GN Name=Aifm3; Synonyms=Aifl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Hippocampus, and Visual cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=FVB/N; TISSUE=Brain, and Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Induces apoptosis through a caspase dependent pathway.
CC Reduces mitochondrial membrane potential (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Note=Does not translocate to the
CC nucleus upon induction of apoptosis. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3TY86-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TY86-2; Sequence=VSP_021306;
CC Name=3;
CC IsoId=Q3TY86-3; Sequence=VSP_021304, VSP_021305;
CC -!- DOMAIN: The Rieske domain induces apoptosis. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; AK049928; BAC33988.1; -; mRNA.
DR EMBL; AK158809; BAE34677.1; -; mRNA.
DR EMBL; BC096476; AAH96476.1; -; mRNA.
DR EMBL; BC120685; AAI20686.1; -; mRNA.
DR CCDS; CCDS28003.1; -. [Q3TY86-2]
DR CCDS; CCDS79430.1; -. [Q3TY86-1]
DR RefSeq; NP_001277999.1; NM_001291070.1. [Q3TY86-1]
DR RefSeq; NP_780387.2; NM_175178.4. [Q3TY86-2]
DR RefSeq; XP_006522655.1; XM_006522592.3. [Q3TY86-1]
DR AlphaFoldDB; Q3TY86; -.
DR SMR; Q3TY86; -.
DR STRING; 10090.ENSMUSP00000023448; -.
DR iPTMnet; Q3TY86; -.
DR PhosphoSitePlus; Q3TY86; -.
DR PaxDb; Q3TY86; -.
DR PeptideAtlas; Q3TY86; -.
DR PRIDE; Q3TY86; -.
DR ProteomicsDB; 296344; -. [Q3TY86-1]
DR ProteomicsDB; 296345; -. [Q3TY86-2]
DR ProteomicsDB; 296346; -. [Q3TY86-3]
DR Antibodypedia; 231; 217 antibodies from 30 providers.
DR DNASU; 72168; -.
DR Ensembl; ENSMUST00000023448; ENSMUSP00000023448; ENSMUSG00000022763. [Q3TY86-2]
DR Ensembl; ENSMUST00000115685; ENSMUSP00000111349; ENSMUSG00000022763. [Q3TY86-1]
DR GeneID; 72168; -.
DR KEGG; mmu:72168; -.
DR UCSC; uc007ykw.2; mouse. [Q3TY86-1]
DR UCSC; uc007ykx.2; mouse. [Q3TY86-3]
DR UCSC; uc007yky.2; mouse. [Q3TY86-2]
DR CTD; 150209; -.
DR MGI; MGI:1919418; Aifm3.
DR VEuPathDB; HostDB:ENSMUSG00000022763; -.
DR eggNOG; KOG1336; Eukaryota.
DR GeneTree; ENSGT00940000160448; -.
DR HOGENOM; CLU_003291_4_2_1; -.
DR InParanoid; Q3TY86; -.
DR OMA; IATYPYH; -.
DR OrthoDB; 405030at2759; -.
DR PhylomeDB; Q3TY86; -.
DR TreeFam; TF314028; -.
DR BioGRID-ORCS; 72168; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Aifm3; mouse.
DR PRO; PR:Q3TY86; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q3TY86; protein.
DR Bgee; ENSMUSG00000022763; Expressed in cerebellar cortex and 144 other tissues.
DR Genevisible; Q3TY86; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC-UCL.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:HGNC-UCL.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
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:0016651; F:oxidoreductase activity, acting on NAD(P)H; IBA:GO_Central.
DR GO; GO:0097194; P:execution phase of apoptosis; ISS:HGNC.
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; IPR028202; Reductase_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF14759; Reductase_C; 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 1: Evidence at protein level;
KW 2Fe-2S; Alternative splicing; Apoptosis; Electron transport; FAD;
KW Flavoprotein; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW Oxidoreductase; Reference proteome; Transport.
FT CHAIN 1..605
FT /note="Apoptosis-inducing factor 3"
FT /id="PRO_0000255661"
FT DOMAIN 70..165
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT REGION 18..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 111
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 128
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 131
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 201..205
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 235
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 240
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 270
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 467
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 514
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT VAR_SEQ 494..500
FT /note="RVAAQNM -> MASPEAS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_021304"
FT VAR_SEQ 501..605
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_021305"
FT VAR_SEQ 587..593
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021306"
FT CONFLICT 138
FT /note="S -> T (in Ref. 1; BAC33988)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 605 AA; 66792 MW; D4811CB2B2CD0739 CRC64;
MGGCFSKPKP VELKIEVVLP EKERGKEELS ASGKGSPRGY QGNGTARHFH AEERLPTPQP
YPSPQDCVEA TVCHVKDLEN GQMREVELGW GKVLLVKDNG EFHALGHKCP HYGAPLVKGV
LSRGRVRCPW HGACFNISTG DLEDFPGLDS LHKFQVKIEK EKVTIRASKQ ALQLQRRTKV
MAKCISPSAG HSSSTNVLIV GAGAAGLVCA ETLRQEGFSD RIVLCTLDRH LPYDRAKLSK
SLDAQPEQLA LRPKEFFRAY GIEMLTEAQV VTVDVRNKKV VFKDGFKLEY SKLLLAPGSS
PKTLTCKGKD VENVFTIRTP EDANRVLRLA RGRNAVVVGA GFLGMEVAAY LTEKAHSVSV
VELEETPFRR FLGERVGRAL MKMFENNRVK FYMQTEVSEL RAQEGKLQEV VLKSSKVLRA
DVCVLGIGAV PATGFLRQSG IGLDSRGFIP VNKMMQTNVP GVFAAGDAVT FPLAWRNNRK
VNIPHWQMAH AQGRVAAQNM LAQEAEINTV PYLWTAMFGK SLRYAGYGEG FDDVIIQGDL
EELKFVAFYT KSDEVIAVAS MNYDPIVSKV AEVLASGRAI RKREVELFML HSKTGDMSWL
TGKGS
