ATP5S_HUMAN
ID ATP5S_HUMAN Reviewed; 215 AA.
AC Q99766; A8K1U3; D9N156; Q8WWX3; Q96F77;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=ATP synthase subunit s, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase-coupling factor B;
DE Short=FB;
DE AltName: Full=Distal membrane arm assembly complex 2-like protein {ECO:0000312|HGNC:HGNC:18799};
DE AltName: Full=Mitochondrial ATP synthase regulatory component factor B;
DE Flags: Precursor;
GN Name=DMAC2L {ECO:0000312|HGNC:HGNC:18799};
GN Synonyms=ATP5S {ECO:0000312|HGNC:HGNC:18799}, ATPW;
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 2), AND VARIANT LEU-18.
RC TISSUE=Brain;
RX PubMed=9110174; DOI=10.1101/gr.7.4.353;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, SUBUNIT,
RP AND VARIANT LEU-18.
RX PubMed=11744738; DOI=10.1074/jbc.m111256200;
RA Belogrudov G.I., Hatefi Y.;
RT "Factor B and the mitochondrial ATP synthase complex.";
RL J. Biol. Chem. 277:6097-6103(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-18.
RC TISSUE=Hippocampus;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-18.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT LEU-18.
RC TISSUE=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 [7]
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 [8]
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: Involved in regulation of mitochondrial membrane ATP
CC synthase. Necessary for H(+) conduction of ATP synthase. Facilitates
CC energy-driven catalysis of ATP synthesis by blocking a proton leak
CC through an alternative proton exit pathway.
CC {ECO:0000250|UniProtKB:P22027}.
CC -!- SUBUNIT: Homotetramer. Associates with ATP synthase.
CC {ECO:0000250|UniProtKB:P22027}.
CC -!- INTERACTION:
CC Q99766-3; Q03828: EVX2; NbExp=3; IntAct=EBI-13309711, EBI-17280301;
CC Q99766-3; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-13309711, EBI-6426443;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P22027}.
CC Mitochondrion inner membrane {ECO:0000250|UniProtKB:P22027}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q99766-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99766-2; Sequence=VSP_040059, VSP_040062;
CC Name=3;
CC IsoId=Q99766-3; Sequence=VSP_040060, VSP_040061;
CC -!- SIMILARITY: Belongs to the ATP synthase subunit s family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-16 is the initiator.
CC {ECO:0000305}.
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DR EMBL; U79253; AAB50202.1; -; mRNA.
DR EMBL; AY052377; AAL13058.1; -; mRNA.
DR EMBL; AK290008; BAF82697.1; -; mRNA.
DR EMBL; AL359397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW65718.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65722.1; -; Genomic_DNA.
DR EMBL; BC011549; AAH11549.1; -; mRNA.
DR RefSeq; NP_001003803.1; NM_001003803.2.
DR RefSeq; NP_001003805.1; NM_001003805.2.
DR RefSeq; NP_056499.2; NM_015684.3.
DR RefSeq; XP_011534958.1; XM_011536656.2. [Q99766-2]
DR AlphaFoldDB; Q99766; -.
DR SMR; Q99766; -.
DR BioGRID; 118006; 18.
DR IntAct; Q99766; 18.
DR STRING; 9606.ENSP00000308334; -.
DR iPTMnet; Q99766; -.
DR PhosphoSitePlus; Q99766; -.
DR BioMuta; ATP5S; -.
DR DMDM; 313104249; -.
DR EPD; Q99766; -.
DR jPOST; Q99766; -.
DR MassIVE; Q99766; -.
DR MaxQB; Q99766; -.
DR PaxDb; Q99766; -.
DR PeptideAtlas; Q99766; -.
DR PRIDE; Q99766; -.
DR ProteomicsDB; 78466; -. [Q99766-1]
DR ProteomicsDB; 78467; -. [Q99766-2]
DR ProteomicsDB; 78468; -. [Q99766-3]
DR Antibodypedia; 56666; 150 antibodies from 24 providers.
DR DNASU; 27109; -.
DR Ensembl; ENST00000245448.11; ENSP00000245448.7; ENSG00000125375.18.
DR Ensembl; ENST00000554204.7; ENSP00000451583.3; ENSG00000125375.18.
DR GeneID; 27109; -.
DR KEGG; hsa:27109; -.
DR UCSC; uc001wxv.4; human. [Q99766-1]
DR CTD; 27109; -.
DR DisGeNET; 27109; -.
DR GeneCards; DMAC2L; -.
DR HGNC; HGNC:18799; DMAC2L.
DR HPA; ENSG00000125375; Low tissue specificity.
DR MIM; 618579; gene.
DR neXtProt; NX_Q99766; -.
DR VEuPathDB; HostDB:ENSG00000125375; -.
DR eggNOG; KOG3864; Eukaryota.
DR HOGENOM; CLU_1969785_0_0_1; -.
DR InParanoid; Q99766; -.
DR OrthoDB; 1395428at2759; -.
DR PhylomeDB; Q99766; -.
DR TreeFam; TF315274; -.
DR PathwayCommons; Q99766; -.
DR Reactome; R-HSA-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-HSA-8949613; Cristae formation.
DR SignaLink; Q99766; -.
DR BioGRID-ORCS; 27109; 12 hits in 1074 CRISPR screens.
DR ChiTaRS; ATP5S; human.
DR GeneWiki; ATP5S; -.
DR GenomeRNAi; 27109; -.
DR Pharos; Q99766; Tbio.
DR PRO; PR:Q99766; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q99766; protein.
DR Bgee; ENSG00000125375; Expressed in sperm and 205 other tissues.
DR ExpressionAtlas; Q99766; baseline and differential.
DR Genevisible; Q99766; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015078; F:proton transmembrane transporter activity; NAS:UniProtKB.
DR GO; GO:0006754; P:ATP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1902600; P:proton transmembrane transport; NAS:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR026063; ATP5S/ATP5SL.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR13382:SF10; PTHR13382:SF10; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP synthesis; CF(0); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Leucine-rich repeat; Magnesium;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Repeat; Transit peptide; Transport.
FT TRANSIT 1..40
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P22027"
FT CHAIN 41..215
FT /note="ATP synthase subunit s, mitochondrial"
FT /id="PRO_0000002538"
FT REPEAT 77..102
FT /note="LRR 1"
FT /evidence="ECO:0000250|UniProtKB:P22027"
FT REPEAT 103..131
FT /note="LRR 2"
FT /evidence="ECO:0000250|UniProtKB:P22027"
FT REPEAT 132..156
FT /note="LRR 3"
FT /evidence="ECO:0000250|UniProtKB:P22027"
FT REPEAT 157..188
FT /note="LRR 4"
FT /evidence="ECO:0000250|UniProtKB:P22027"
FT REGION 16..76
FT /note="N-terminal domain"
FT /evidence="ECO:0000250|UniProtKB:P22027"
FT BINDING 74
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P22027"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P22027"
FT VAR_SEQ 121..136
FT /note="EGLEHVEKIRLCKCHY -> GNYPIVLLIENADDLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9110174"
FT /id="VSP_040059"
FT VAR_SEQ 122..127
FT /note="GLEHVE -> TSNICC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040060"
FT VAR_SEQ 128..215
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040061"
FT VAR_SEQ 137..215
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9110174"
FT /id="VSP_040062"
FT VARIANT 18
FT /note="P -> L (in dbSNP:rs2275592)"
FT /evidence="ECO:0000269|PubMed:11744738,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9110174, ECO:0000269|Ref.5"
FT /id="VAR_060296"
SQ SEQUENCE 215 AA; 24866 MW; DFDCDE6D81E5DC62 CRC64;
MCCAVSEQRL TCADQMMPFG KISQQLCGVK KLPWSCDSRY FWGWLNAVFN KVDYDRIRDV
GPDRAASEWL LRCGAMVRYH GQERWQKDYN HLPTGPLDKY KIQAIDATDS CIMSIGFDHM
EGLEHVEKIR LCKCHYIEDD CLLRLSQLEN LQKTILEMEI ISCGNITDKG IIALRHLRNL
KYLLLSDLPG VREKENLVQA FKTALPSLEL KLQLK
