ATIF1_HUMAN
ID ATIF1_HUMAN Reviewed; 106 AA.
AC Q9UII2; Q5JXL8; Q6IAQ7; Q9BSL9;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=ATPase inhibitor, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase F1 subunit epsilon {ECO:0000305};
DE AltName: Full=Inhibitor of F(1)F(o)-ATPase;
DE Short=IF(1);
DE Short=IF1;
DE Flags: Precursor;
GN Name=ATP5IF1 {ECO:0000312|HGNC:HGNC:871}; Synonyms=ATPI, ATPIF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RX PubMed=10664857; DOI=10.1271/bbb.63.2225;
RA Ichikawa N., Ushida S., Kawabata M., Masazumi Y.;
RT "Nucleotide sequence of cDNA coding the mitochondrial precursor protein of
RT the ATPase inhibitor from humans.";
RL Biosci. Biotechnol. Biochem. 63:2225-2227(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Dai F.Y., Yu L., Yang J., Zheng L.H., Wang X.K., Zhao S.Y.;
RT "Cloning and sequencing of a novel human cDNA homologous to bovine ATP
RT synthase inhibitor protein mRNA.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RA Yu L., Zhang P., Gao J.;
RT "Cloning and characterization of a novel human gene ASI.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Fetal liver;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Uterus;
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 [12]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 26-42, AND VARIABILITY IN MATURE
RP CHAIN LENGTH.
RC TISSUE=Leukemic T-cell;
RX PubMed=19892738; DOI=10.1073/pnas.0908958106;
RA Xu G., Shin S.B., Jaffrey S.R.;
RT "Global profiling of protease cleavage sites by chemoselective labeling of
RT protein N-termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12110673; DOI=10.1074/jbc.m204538200;
RA Aggeler R., Coons J., Taylor S.W., Ghosh S.S., Garcia J.J., Capaldi R.A.,
RA Marusich M.F.;
RT "A functionally active human F1F0 ATPase can be purified by immunocapture
RT from heart tissue and fibroblast cell lines. Subunit structure and activity
RT studies.";
RL J. Biol. Chem. 277:33906-33912(2002).
RN [14]
RP FUNCTION.
RX PubMed=15528193; DOI=10.1074/jbc.m405947200;
RA Burwick N.R., Wahl M.L., Fang J., Zhong Z., Moser T.L., Li B.,
RA Capaldi R.A., Kenan D.J., Pizzo S.V.;
RT "An Inhibitor of the F1 subunit of ATP synthase (IF1) modulates the
RT activity of angiostatin on the endothelial cell surface.";
RL J. Biol. Chem. 280:1740-1745(2005).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP FUNCTION.
RX PubMed=19559621; DOI=10.1016/j.tibs.2009.03.006;
RA Campanella M., Parker N., Tan C.H., Hall A.M., Duchen M.R.;
RT "IF(1): setting the pace of the F(1)F(o)-ATP synthase.";
RL Trends Biochem. Sci. 34:343-350(2009).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39 AND SER-63, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER PHE-25, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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.
CC Indirectly acts as a regulator of heme synthesis in erythroid tissues:
CC regulates heme synthesis by modulating the mitochondrial pH and redox
CC potential, allowing FECH to efficiently catalyze the incorporation of
CC iron into protoporphyrin IX to produce heme.
CC {ECO:0000269|PubMed:12110673, ECO:0000269|PubMed:15528193,
CC ECO:0000269|PubMed:19559621, 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 -!- INTERACTION:
CC Q9UII2; P01023: A2M; NbExp=3; IntAct=EBI-718459, EBI-640741;
CC Q9UII2; P07550: ADRB2; NbExp=3; IntAct=EBI-718459, EBI-491169;
CC Q9UII2; P06576: ATP5F1B; NbExp=2; IntAct=EBI-718459, EBI-356231;
CC Q9UII2; P28329-3: CHAT; NbExp=3; IntAct=EBI-718459, EBI-25837549;
CC Q9UII2; G5E9A7: DMWD; NbExp=3; IntAct=EBI-718459, EBI-10976677;
CC Q9UII2; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-718459, EBI-12593112;
CC Q9UII2; P50570-2: DNM2; NbExp=3; IntAct=EBI-718459, EBI-10968534;
CC Q9UII2; P22607: FGFR3; NbExp=3; IntAct=EBI-718459, EBI-348399;
CC Q9UII2; Q53GS7: GLE1; NbExp=3; IntAct=EBI-718459, EBI-1955541;
CC Q9UII2; P28799-2: GRN; NbExp=3; IntAct=EBI-718459, EBI-25860013;
CC Q9UII2; P06396: GSN; NbExp=3; IntAct=EBI-718459, EBI-351506;
CC Q9UII2; P01112: HRAS; NbExp=3; IntAct=EBI-718459, EBI-350145;
CC Q9UII2; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-718459, EBI-8472129;
CC Q9UII2; O14901: KLF11; NbExp=3; IntAct=EBI-718459, EBI-948266;
CC Q9UII2; P51608: MECP2; NbExp=3; IntAct=EBI-718459, EBI-1189067;
CC Q9UII2; I6L9F6: NEFL; NbExp=3; IntAct=EBI-718459, EBI-10178578;
CC Q9UII2; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-718459, EBI-2811583;
CC Q9UII2; Q99650: OSMR; NbExp=4; IntAct=EBI-718459, EBI-2804080;
CC Q9UII2; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-718459, EBI-79165;
CC Q9UII2; D3DTS7: PMP22; NbExp=3; IntAct=EBI-718459, EBI-25882629;
CC Q9UII2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-718459, EBI-5235340;
CC Q9UII2; O14656-2: TOR1A; NbExp=3; IntAct=EBI-718459, EBI-25847109;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12110673}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UII2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UII2-2; Sequence=VSP_041417;
CC Name=3;
CC IsoId=Q9UII2-3; Sequence=VSP_041418;
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 -!- PTM: Exhibits variability in chain length, mitochondria have distinct
CC pools of protein cleaved after the 24th, 25th, and 26th amino acid.
CC -!- SIMILARITY: Belongs to the ATPase inhibitor family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04955.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB029042; BAA88422.1; -; mRNA.
DR EMBL; AK316600; BAG38187.1; -; mRNA.
DR EMBL; DB030607; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL050386; CAI46227.1; -; mRNA.
DR EMBL; AF114836; AAP97235.1; -; mRNA.
DR EMBL; AY005470; AAF97495.1; -; Genomic_DNA.
DR EMBL; AL583540; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BT009849; AAP88851.1; -; mRNA.
DR EMBL; CR457097; CAG33378.1; -; mRNA.
DR EMBL; AL353622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07704.1; -; Genomic_DNA.
DR EMBL; BC004955; AAH04955.1; ALT_INIT; mRNA.
DR EMBL; BC009677; AAH09677.1; -; mRNA.
DR CCDS; CCDS319.1; -. [Q9UII2-1]
DR CCDS; CCDS320.1; -. [Q9UII2-2]
DR CCDS; CCDS44096.1; -. [Q9UII2-3]
DR PIR; JC7175; JC7175.
DR RefSeq; NP_057395.1; NM_016311.4. [Q9UII2-1]
DR RefSeq; NP_835497.1; NM_178190.2. [Q9UII2-2]
DR RefSeq; NP_835498.1; NM_178191.2. [Q9UII2-3]
DR AlphaFoldDB; Q9UII2; -.
DR SMR; Q9UII2; -.
DR BioGRID; 125063; 150.
DR CORUM; Q9UII2; -.
DR IntAct; Q9UII2; 59.
DR MINT; Q9UII2; -.
DR STRING; 9606.ENSP00000335203; -.
DR TCDB; 3.A.2.1.15; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR GlyGen; Q9UII2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UII2; -.
DR PhosphoSitePlus; Q9UII2; -.
DR BioMuta; ATPIF1; -.
DR DMDM; 12585262; -.
DR EPD; Q9UII2; -.
DR jPOST; Q9UII2; -.
DR MassIVE; Q9UII2; -.
DR MaxQB; Q9UII2; -.
DR PaxDb; Q9UII2; -.
DR PeptideAtlas; Q9UII2; -.
DR PRIDE; Q9UII2; -.
DR ProteomicsDB; 84524; -. [Q9UII2-1]
DR ProteomicsDB; 84525; -. [Q9UII2-2]
DR ProteomicsDB; 84526; -. [Q9UII2-3]
DR TopDownProteomics; Q9UII2-1; -. [Q9UII2-1]
DR TopDownProteomics; Q9UII2-2; -. [Q9UII2-2]
DR Antibodypedia; 30912; 239 antibodies from 30 providers.
DR DNASU; 93974; -.
DR Ensembl; ENST00000335514.10; ENSP00000335203.5; ENSG00000130770.18. [Q9UII2-1]
DR Ensembl; ENST00000465645.1; ENSP00000437337.1; ENSG00000130770.18. [Q9UII2-3]
DR Ensembl; ENST00000497986.5; ENSP00000435579.1; ENSG00000130770.18. [Q9UII2-2]
DR Ensembl; ENST00000642464.1; ENSP00000496122.1; ENSG00000285390.2. [Q9UII2-2]
DR Ensembl; ENST00000647074.2; ENSP00000494248.1; ENSG00000285390.2. [Q9UII2-1]
DR Ensembl; ENST00000647380.1; ENSP00000496605.1; ENSG00000285390.2. [Q9UII2-3]
DR GeneID; 93974; -.
DR KEGG; hsa:93974; -.
DR MANE-Select; ENST00000335514.10; ENSP00000335203.5; NM_016311.5; NP_057395.1.
DR UCSC; uc001bpp.4; human. [Q9UII2-1]
DR CTD; 93974; -.
DR DisGeNET; 93974; -.
DR GeneCards; ATP5IF1; -.
DR HGNC; HGNC:871; ATP5IF1.
DR HPA; ENSG00000130770; Low tissue specificity.
DR MIM; 614981; gene.
DR neXtProt; NX_Q9UII2; -.
DR OpenTargets; ENSG00000130770; -.
DR PharmGKB; PA25173; -.
DR VEuPathDB; HostDB:ENSG00000130770; -.
DR eggNOG; ENOG502S4JP; Eukaryota.
DR GeneTree; ENSGT00390000006264; -.
DR HOGENOM; CLU_147479_0_0_1; -.
DR InParanoid; Q9UII2; -.
DR OMA; YFRARNK; -.
DR OrthoDB; 1566610at2759; -.
DR PhylomeDB; Q9UII2; -.
DR TreeFam; TF320659; -.
DR PathwayCommons; Q9UII2; -.
DR SignaLink; Q9UII2; -.
DR SIGNOR; Q9UII2; -.
DR BioGRID-ORCS; 93974; 14 hits in 1076 CRISPR screens.
DR ChiTaRS; ATP5IF1; human.
DR GeneWiki; ATPIF1; -.
DR GenomeRNAi; 93974; -.
DR Pharos; Q9UII2; Tbio.
DR PRO; PR:Q9UII2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UII2; protein.
DR Bgee; ENSG00000130770; Expressed in left testis and 96 other tissues.
DR ExpressionAtlas; Q9UII2; baseline and differential.
DR Genevisible; Q9UII2; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0043532; F:angiostatin binding; IDA:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IDA:UniProtKB.
DR GO; GO:0042030; F:ATPase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:CAFA.
DR GO; GO:0004857; F:enzyme inhibitor activity; TAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0140260; F:mitochondrial proton-transporting ATP synthase complex binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; TAS:ParkinsonsUK-UCL.
DR GO; GO:0001525; P:angiogenesis; TAS:UniProtKB.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:ProtInc.
DR GO; GO:0006783; P:heme biosynthetic process; IMP:UniProtKB.
DR GO; GO:0051882; P:mitochondrial depolarization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; IMP:ParkinsonsUK-UCL.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IDA:UniProtKB.
DR GO; GO:0051346; P:negative regulation of hydrolase activity; IDA:UniProtKB.
DR GO; GO:1904925; P:positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization; IMP:ParkinsonsUK-UCL.
DR GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:1903052; P:positive regulation of proteolysis involved in protein catabolic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
DR GO; GO:1903578; P:regulation of ATP metabolic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903214; P:regulation of protein targeting to mitochondrion; IMP:ParkinsonsUK-UCL.
DR InterPro; IPR007648; ATPase_inhibitor_mt.
DR Pfam; PF04568; IATP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Direct protein sequencing;
KW Mitochondrion; Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:19892738,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 26..106
FT /note="ATPase inhibitor, mitochondrial"
FT /id="PRO_0000002547"
FT REGION 26..52
FT /note="N-terminal inhibitory region"
FT /evidence="ECO:0000250"
FT REGION 26..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..106
FT /note="Antiparallel alpha-helical coiled coil region"
FT /evidence="ECO:0000250"
FT COILED 63..106
FT /evidence="ECO:0000255"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 103
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35143"
FT VAR_SEQ 61..106
FT /note="AQSREQLAALKKHHEEEIVHHKKEIERLQKEIERHKQKIKMLKHDD -> HY
FT RLCFEISLG (in isoform 2)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_041417"
FT VAR_SEQ 61..106
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041418"
FT CONFLICT 60
FT /note="R -> RR (in Ref. 2; CAI46227)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 106 AA; 12249 MW; A6144431125D5A86 CRC64;
MAVTALAART WLGVWGVRTM QARGFGSDQS ENVDRGAGSI REAGGAFGKR EQAEEERYFR
AQSREQLAAL KKHHEEEIVH HKKEIERLQK EIERHKQKIK MLKHDD
