ATIF1_MOUSE
ID ATIF1_MOUSE Reviewed; 106 AA.
AC O35143; Q9D879;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=ATPase inhibitor, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase F1 subunit epsilon {ECO:0000250|UniProtKB:Q9UII2};
DE AltName: Full=Inhibitor of F(1)F(o)-ATPase;
DE Short=IF(1);
DE Short=IF1;
DE Flags: Precursor;
GN Name=Atp5if1 {ECO:0000250|UniProtKB:Q9UII2};
GN Synonyms=Atpi, Atpif1 {ECO:0000312|MGI:MGI:1196457}, If1;
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 [MRNA].
RC STRAIN=DBA/1;
RX PubMed=9497501; DOI=10.1046/j.1365-2567.1997.00370.x;
RA Yamada E., Ishiguro N., Miyaishi O., Takeuchi A., Nakashima I., Iwata H.,
RA Isobe K.;
RT "Differential display analysis of murine collagen-induced arthritis:
RT cloning of the cDNA-encoding murine ATPase inhibitor.";
RL Immunology 92:571-576(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Small intestine;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Lung, and Testis;
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).
RN [7]
RP FUNCTION.
RX PubMed=23135403; DOI=10.1038/nature11536;
RA Shah D.I., Takahashi-Makise N., Cooney J.D., Li L., Schultz I.J.,
RA Pierce E.L., Narla A., Seguin A., Hattangadi S.M., Medlock A.E.,
RA Langer N.B., Dailey T.A., Hurst S.N., Faccenda D., Wiwczar J.M.,
RA Heggers S.K., Vogin G., Chen W., Chen C., Campagna D.R., Brugnara C.,
RA Zhou Y., Ebert B.L., Danial N.N., Fleming M.D., Ward D.M., Campanella M.,
RA Dailey H.A., Kaplan J., Paw B.H.;
RT "Mitochondrial Atpif1 regulates haem synthesis in developing
RT erythroblasts.";
RL Nature 491:608-612(2012).
RN [8]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-103, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion
CC when the mitochondrial membrane potential falls below a threshold and
CC the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of
CC the mitochondrial matrix. Required to avoid the consumption of cellular
CC ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase (By
CC similarity). Indirectly acts as a regulator of heme synthesis in
CC erythroid tissues: regulates heme synthesis by modulating the
CC mitochondrial pH and redox potential, allowing FECH to efficiently
CC catalyze the incorporation of iron into protoporphyrin IX to produce
CC heme (PubMed:23135403). {ECO:0000250|UniProtKB:P01096,
CC ECO:0000269|PubMed:23135403}.
CC -!- SUBUNIT: Homodimer; represents the active form and is present at a pH
CC value below 6.5. Homotetramer; represents the inactive form and is
CC present at a pH value above 7.0 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- DOMAIN: Forms an alpha-helical dimer with monomers associated via an
CC antiparallel alpha-helical coiled coil composed of residues 74-106,
CC leaving each N-terminal inhibitory region (residues 26-52) accessible
CC for interaction with an F1 catalytic domain. The inhibitory N-terminal
CC region (residues 26-52) binds the alpha(ADP-bound)-beta(ADP-bound)
CC (ATP5F1A-ATP5F1B) interface of F1-ATPase, and also contact the central
CC gamma subunit (ATP5F1C). This dimeric state is favored by pH values
CC below 7.0, and at higher values the dimers associate to form inactive
CC homotetramer, where the inhibitory region is occluded, masking its
CC inhibitory activity (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATPase inhibitor family. {ECO:0000305}.
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DR EMBL; AF002718; AAB69647.1; -; mRNA.
DR EMBL; AK008346; BAB25618.1; -; mRNA.
DR EMBL; AK152389; BAE31177.1; -; mRNA.
DR EMBL; AL805897; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466552; EDL30101.1; -; Genomic_DNA.
DR EMBL; BC012680; AAH12680.1; -; mRNA.
DR CCDS; CCDS18727.1; -.
DR RefSeq; NP_031538.2; NM_007512.4.
DR AlphaFoldDB; O35143; -.
DR SMR; O35143; -.
DR BioGRID; 198273; 25.
DR IntAct; O35143; 2.
DR MINT; O35143; -.
DR STRING; 10090.ENSMUSP00000064282; -.
DR iPTMnet; O35143; -.
DR PhosphoSitePlus; O35143; -.
DR EPD; O35143; -.
DR jPOST; O35143; -.
DR PaxDb; O35143; -.
DR PeptideAtlas; O35143; -.
DR PRIDE; O35143; -.
DR ProteomicsDB; 277128; -.
DR TopDownProteomics; O35143; -.
DR Antibodypedia; 30912; 239 antibodies from 30 providers.
DR DNASU; 11983; -.
DR Ensembl; ENSMUST00000067496; ENSMUSP00000064282; ENSMUSG00000054428.
DR GeneID; 11983; -.
DR KEGG; mmu:11983; -.
DR UCSC; uc008vbl.3; mouse.
DR CTD; 11983; -.
DR MGI; MGI:1196457; Atpif1.
DR VEuPathDB; HostDB:ENSMUSG00000054428; -.
DR eggNOG; ENOG502S4JP; Eukaryota.
DR GeneTree; ENSGT00390000006264; -.
DR HOGENOM; CLU_147479_0_0_1; -.
DR InParanoid; O35143; -.
DR OMA; YFRARNK; -.
DR OrthoDB; 1566610at2759; -.
DR PhylomeDB; O35143; -.
DR TreeFam; TF320659; -.
DR BioGRID-ORCS; 11983; 7 hits in 59 CRISPR screens.
DR ChiTaRS; Atpif1; mouse.
DR PRO; PR:O35143; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O35143; protein.
DR Bgee; ENSMUSG00000054428; Expressed in paneth cell and 277 other tissues.
DR ExpressionAtlas; O35143; baseline and differential.
DR Genevisible; O35143; MM.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0043532; F:angiostatin binding; ISS:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; ISS:UniProtKB.
DR GO; GO:0042030; F:ATPase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0140260; F:mitochondrial proton-transporting ATP synthase complex binding; ISO:MGI.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0006783; P:heme biosynthetic process; IMP:UniProtKB.
DR GO; GO:0051882; P:mitochondrial depolarization; ISO:MGI.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; ISO:MGI.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0051346; P:negative regulation of hydrolase activity; ISS:UniProtKB.
DR GO; GO:1904925; P:positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization; ISO:MGI.
DR GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IMP:MGI.
DR GO; GO:1903052; P:positive regulation of proteolysis involved in protein catabolic process; ISO:MGI.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:MGI.
DR GO; GO:1903578; P:regulation of ATP metabolic process; ISO:MGI.
DR GO; GO:1903214; P:regulation of protein targeting to mitochondrion; ISO:MGI.
DR InterPro; IPR007648; ATPase_inhibitor_mt.
DR Pfam; PF04568; IATP; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Mitochondrion; Phosphoprotein; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 26..106
FT /note="ATPase inhibitor, mitochondrial"
FT /id="PRO_0000002548"
FT REGION 26..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 26..52
FT /note="N-terminal inhibitory region"
FT /evidence="ECO:0000250"
FT REGION 74..106
FT /note="Antiparallel alpha-helical coiled coil region"
FT /evidence="ECO:0000250"
FT COILED 60..106
FT /evidence="ECO:0000255"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UII2"
FT MOD_RES 103
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 93
FT /note="E -> D (in Ref. 1; AAB69647)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 106 AA; 12159 MW; 78C0FE0CD04FA2D3 CRC64;
MAGSALAVRA RFGVWGMKVL QTRGFVSDSS DSMDTGAGSI REAGGAFGKR EKAEEDRYFR
EKTKEQLAAL RKHHEDEIDH HSKEIERLQK QIERHKKKIQ QLKNNH
