ATP14_YEAST
ID ATP14_YEAST Reviewed; 124 AA.
AC Q12349; D6VYU0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=ATP synthase subunit H, mitochondrial;
DE Flags: Precursor;
GN Name=ATP14; OrderedLocusNames=YLR295C; ORFNames=L8003.20;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=D273-10B/A/H/U;
RX PubMed=8702761; DOI=10.1074/jbc.271.34.20284;
RA Arselin G., Vaillier J., Graves P.-V., Velours J.;
RT "ATP synthase of yeast mitochondria. Isolation of the subunit h and
RT disruption of the ATP14 gene.";
RL J. Biol. Chem. 271:20284-20290(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
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. Part of the complex
CC F(0) domain. Minor subunit located with subunit a in the membrane.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. In yeast, the dimeric form
CC of ATP synthase consists of 17 polypeptides: alpha, beta, gamma, delta,
CC epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d, E (Tim11), f, g, h, i/j
CC and k.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- MISCELLANEOUS: Present with 6140 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ATPase h subunit family. {ECO:0000305}.
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DR EMBL; U51673; AAC49436.1; -; Genomic_DNA.
DR EMBL; U17243; AAB67340.1; -; Genomic_DNA.
DR EMBL; AY558215; AAS56541.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09606.1; -; Genomic_DNA.
DR PIR; S50379; S50379.
DR RefSeq; NP_013398.1; NM_001182183.1.
DR PDB; 6CP3; EM; 3.80 A; 6=33-124.
DR PDB; 6CP6; EM; 3.60 A; 6=33-124.
DR PDBsum; 6CP3; -.
DR PDBsum; 6CP6; -.
DR AlphaFoldDB; Q12349; -.
DR SMR; Q12349; -.
DR BioGRID; 31560; 149.
DR ComplexPortal; CPX-3281; Mitochondrial proton-transporting ATP synthase complex.
DR DIP; DIP-3030N; -.
DR IntAct; Q12349; 14.
DR MINT; Q12349; -.
DR STRING; 4932.YLR295C; -.
DR MoonDB; Q12349; Predicted.
DR TCDB; 3.A.2.1.3; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR MaxQB; Q12349; -.
DR PaxDb; Q12349; -.
DR PRIDE; Q12349; -.
DR EnsemblFungi; YLR295C_mRNA; YLR295C; YLR295C.
DR GeneID; 851002; -.
DR KEGG; sce:YLR295C; -.
DR SGD; S000004286; ATP14.
DR VEuPathDB; FungiDB:YLR295C; -.
DR eggNOG; ENOG502SDW5; Eukaryota.
DR HOGENOM; CLU_122989_1_0_1; -.
DR InParanoid; Q12349; -.
DR OMA; EGATRPW; -.
DR BioCyc; YEAST:G3O-32389-MON; -.
DR PRO; PR:Q12349; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12349; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IC:ComplexPortal.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IMP:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0042407; P:cristae formation; IMP:SGD.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0033615; P:mitochondrial proton-transporting ATP synthase complex assembly; IMP:SGD.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IDA:SGD.
DR InterPro; IPR019711; ATP_synth_F0_suH.
DR PANTHER; PTHR28207; PTHR28207; 1.
DR Pfam; PF10775; ATP_sub_h; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; CF(0); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transport.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT CHAIN 33..124
FT /note="ATP synthase subunit H, mitochondrial"
FT /id="PRO_0000002525"
FT REGION 89..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..116
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 124 AA; 14128 MW; 7AE196CFB250ACBB CRC64;
MFPIASRRIL LNASVLPLRL CNRNFTTTRI SYNVIQDLYL RELKDTKLAP STLQDAEGNV
KPWNPPQKPN LPELELQGPE ALKAYTEQNV ETAHVAKESE EGESEPIEED WLVLDDAEET
KESH
