ID   ATP68_HUMAN             Reviewed;          58 AA.
AC   P56378; B2R588; G3V5Q3; Q86TT7;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   24-JAN-2024, entry version 165.
DE   RecName: Full=ATP synthase subunit ATP5MJ, mitochondrial {ECO:0000305};
DE   AltName: Full=6.8 kDa mitochondrial proteolipid protein {ECO:0000303|PubMed:24330338};
DE            Short=MLQ {ECO:0000303|PubMed:24330338};
DE   AltName: Full=ATP synthase membrane subunit 6.8PL {ECO:0000312|HGNC:HGNC:1188};
GN   Name=ATP5MJ {ECO:0000312|HGNC:HGNC:1188};
GN   Synonyms=ATP5MPL, C14orf2, MP68; ORFNames=PRO1574;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Umbilical cord blood;
RX   PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA   Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA   He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA   Wang Y.-X., Chen S.-J., Chen Z.;
RT   "Identification of genes expressed in human CD34(+) hematopoietic
RT   stem/progenitor cells by expressed sequence tags and efficient full-length
RT   cDNA cloning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal liver;
RA   Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J.,
RA   Liu M., He F.;
RT   "Functional prediction of the coding sequences of 121 new genes deduced by
RT   analysis of cDNA clones from human fetal liver.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Neuroblastoma;
RA   Li W.B., Gruber C., Jessee J., Polayes D.;
RT   "Full-length cDNA libraries and normalization.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Synovium;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung;
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   [8]
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   [9]
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).
RN   [10]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=24330338; DOI=10.1111/gtc.12121;
RA   Fujikawa M., Ohsakaya S., Sugawara K., Yoshida M.;
RT   "Population of ATP synthase molecules in mitochondria is limited by
RT   available 6.8-kDa proteolipid protein (MLQ).";
RL   Genes Cells 19:153-160(2014).
CC   -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC       Complex V) produces ATP from ADP in the presence of a proton gradient
CC       across the membrane which is generated by electron transport complexes
CC       of the respiratory chain. F-type ATPases consist of two structural
CC       domains, F(1) - containing the extramembraneous catalytic core and F(0)
CC       - containing the membrane proton channel, linked together by a central
CC       stalk and a peripheral stalk. During catalysis, ATP synthesis in the
CC       catalytic domain of F(1) is coupled via a rotary mechanism of the
CC       central stalk subunits to proton translocation (Probable). Minor
CC       subunit required to maintain the ATP synthase population in the
CC       mitochondria (PubMed:24330338). {ECO:0000269|PubMed:24330338,
CC       ECO:0000305}.
CC   -!- SUBUNIT: Component of an ATP synthase complex composed of ATP5PB,
CC       ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8,
CC       ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ.
CC       {ECO:0000250|UniProtKB:P14790}.
CC   -!- INTERACTION:
CC       P56378-2; P02654: APOC1; NbExp=3; IntAct=EBI-17870477, EBI-1220105;
CC       P56378-2; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-17870477, EBI-7062247;
CC       P56378-2; Q9Y6C9: MTCH2; NbExp=3; IntAct=EBI-17870477, EBI-6164522;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC       {ECO:0000269|PubMed:24330338}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P56378-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P56378-2; Sequence=VSP_047043;
CC   -!- SIMILARITY: Belongs to the small mitochondrial proteolipid family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAW81849.1; Type=Erroneous gene model prediction; 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; AF054175; AAC39909.1; -; mRNA.
DR   EMBL; AF116639; AAF71062.1; -; mRNA.
DR   EMBL; BX161388; CAD61878.1; -; mRNA.
DR   EMBL; AK312099; BAG35035.1; -; mRNA.
DR   EMBL; AL132712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471061; EAW81849.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CH471061; EAW81850.1; -; Genomic_DNA.
DR   EMBL; BC000429; AAH00429.1; -; mRNA.
DR   EMBL; BC001944; AAH01944.1; -; mRNA.
DR   CCDS; CCDS45169.1; -. [P56378-2]
DR   CCDS; CCDS9986.1; -. [P56378-1]
DR   RefSeq; NP_001120865.1; NM_001127393.1. [P56378-2]
DR   RefSeq; NP_004885.1; NM_004894.2. [P56378-1]
DR   PDB; 8H9F; EM; 2.69 A; P=1-58.
DR   PDB; 8H9J; EM; 3.26 A; P=1-58.
DR   PDB; 8H9M; EM; 3.00 A; P=1-58.
DR   PDB; 8H9Q; EM; 3.47 A; P=1-58.
DR   PDB; 8H9S; EM; 2.53 A; P=1-58.
DR   PDB; 8H9T; EM; 2.77 A; P=1-58.
DR   PDB; 8H9U; EM; 2.61 A; P=1-58.
DR   PDB; 8H9V; EM; 3.02 A; P=1-58.
DR   PDBsum; 8H9F; -.
DR   PDBsum; 8H9J; -.
DR   PDBsum; 8H9M; -.
DR   PDBsum; 8H9Q; -.
DR   PDBsum; 8H9S; -.
DR   PDBsum; 8H9T; -.
DR   PDBsum; 8H9U; -.
DR   PDBsum; 8H9V; -.
DR   AlphaFoldDB; P56378; -.
DR   EMDB; EMD-34565; -.
DR   SMR; P56378; -.
DR   BioGRID; 114928; 28.
DR   ComplexPortal; CPX-6151; Mitochondrial proton-transporting ATP synthase complex.
DR   IntAct; P56378; 5.
DR   STRING; 9606.ENSP00000401770; -.
DR   iPTMnet; P56378; -.
DR   PhosphoSitePlus; P56378; -.
DR   BioMuta; C14orf2; -.
DR   EPD; P56378; -.
DR   jPOST; P56378; -.
DR   MassIVE; P56378; -.
DR   MaxQB; P56378; -.
DR   PaxDb; 9606-ENSP00000401770; -.
DR   PeptideAtlas; P56378; -.
DR   ProteomicsDB; 33590; -.
DR   ProteomicsDB; 56916; -. [P56378-1]
DR   Pumba; P56378; -.
DR   TopDownProteomics; P56378-1; -. [P56378-1]
DR   Antibodypedia; 47448; 160 antibodies from 24 providers.
DR   DNASU; 9556; -.
DR   Ensembl; ENST00000286953.8; ENSP00000286953.4; ENSG00000156411.10. [P56378-1]
DR   Ensembl; ENST00000414262.6; ENSP00000401770.2; ENSG00000156411.10. [P56378-2]
DR   Ensembl; ENST00000554880.5; ENSP00000452133.1; ENSG00000156411.10. [P56378-1]
DR   Ensembl; ENST00000557040.5; ENSP00000450894.1; ENSG00000156411.10. [P56378-1]
DR   GeneID; 9556; -.
DR   KEGG; hsa:9556; -.
DR   MANE-Select; ENST00000286953.8; ENSP00000286953.4; NM_004894.3; NP_004885.1.
DR   UCSC; uc001yoi.5; human. [P56378-1]
DR   AGR; HGNC:1188; -.
DR   CTD; 9556; -.
DR   DisGeNET; 9556; -.
DR   GeneCards; ATP5MJ; -.
DR   HGNC; HGNC:1188; ATP5MJ.
DR   HPA; ENSG00000156411; Low tissue specificity.
DR   MIM; 604573; gene.
DR   neXtProt; NX_P56378; -.
DR   OpenTargets; ENSG00000156411; -.
DR   VEuPathDB; HostDB:ENSG00000156411; -.
DR   eggNOG; ENOG502SVSA; Eukaryota.
DR   GeneTree; ENSGT00390000016760; -.
DR   HOGENOM; CLU_198465_0_0_1; -.
DR   InParanoid; P56378; -.
DR   OMA; RSDISHF; -.
DR   OrthoDB; 4827571at2759; -.
DR   PhylomeDB; P56378; -.
DR   TreeFam; TF338412; -.
DR   PathwayCommons; P56378; -.
DR   SignaLink; P56378; -.
DR   BioGRID-ORCS; 9556; 62 hits in 1129 CRISPR screens.
DR   ChiTaRS; ATP5MPL; human.
DR   GenomeRNAi; 9556; -.
DR   Pharos; P56378; Tbio.
DR   PRO; PR:P56378; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; P56378; Protein.
DR   Bgee; ENSG00000156411; Expressed in left ventricle myocardium and 212 other cell types or tissues.
DR   ExpressionAtlas; P56378; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; NAS:ComplexPortal.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; NAS:ComplexPortal.
DR   InterPro; IPR012574; ATP5MJ.
DR   PANTHER; PTHR15233:SF1; ATP SYNTHASE SUBUNIT ATP5MJ, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR15233; MITOCHONDRIAL PROTEOLIPID; 1.
DR   Pfam; PF08039; Mit_proteolip; 1.
DR   Genevisible; P56378; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Membrane; Mitochondrion;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..58
FT                   /note="ATP synthase subunit ATP5MJ, mitochondrial"
FT                   /id="PRO_0000064393"
FT   TRANSMEM        20..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1
FT                   /note="M -> MKLYGTRGSDISHFQCQM (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_047043"
FT   VARIANT         9
FT                   /note="I -> V (in dbSNP:rs1053419)"
FT                   /id="VAR_014526"
FT   TURN            6..13
FT                   /evidence="ECO:0007829|PDB:8H9M"
FT   HELIX           14..18
FT                   /evidence="ECO:0007829|PDB:8H9M"
FT   TURN            19..21
FT                   /evidence="ECO:0007829|PDB:8H9V"
FT   HELIX           22..40
FT                   /evidence="ECO:0007829|PDB:8H9M"
SQ   SEQUENCE   58 AA;  6662 MW;  1B8A63046C0383F6 CRC64;
     MLQSIIKNIW IPMKPYYTKV YQEIWIGMGL MGFIVYKIRA ADKRSKALKA SAPAPGHH
//