ATP5H_RAT
ID ATP5H_RAT Reviewed; 161 AA.
AC P31399;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=ATP synthase subunit d, mitochondrial {ECO:0000305};
DE Short=ATPase subunit d;
DE AltName: Full=ATP synthase peripheral stalk subunit d {ECO:0000305};
GN Name=Atp5pd {ECO:0000312|RGD:620083}; Synonyms=Atp5h, Atp5jd;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1531750; DOI=10.1016/0006-291x(92)91849-l;
RA Motojima K., Imanaka T.;
RT "cDNA cloning for and preparation of antibodies against subunit d of H(+)-
RT ATP synthase in rat mitochondria.";
RL Biochem. Biophys. Res. Commun. 182:1130-1138(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7509337; DOI=10.1093/oxfordjournals.jbchem.a124242;
RA Higuti T., Kuroiwa K., Miyazaki S., Toda H., Kakuno T., Sakiyama F.;
RT "The complete amino acid sequence of subunit d of rat liver mitochondrial
RT H(+)-ATP synthase.";
RL J. Biochem. 114:714-717(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary, and Testis;
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 [4]
RP PROTEIN SEQUENCE OF 33-41; 59-71; 79-95; 100-111 AND 149-161, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE ATP SYNTHASE
RP COMPLEX.
RX PubMed=17575325; DOI=10.1074/mcp.m700097-mcp200;
RA Meyer B., Wittig I., Trifilieff E., Karas M., Schaegger H.;
RT "Identification of two proteins associated with mammalian ATP synthase.";
RL Mol. Cell. Proteomics 6:1690-1699(2007).
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
CC F(0) - containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. Part of the complex
CC F(0) domain and the peripheric stalk, which acts as a stator to hold
CC the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC relative to the rotary elements.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(0) seems to have nine
CC subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP
CC synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME,
CC ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C,
CC ATP5PO, ATP5MG, ATP5MK and ATP5MJ. {ECO:0000269|PubMed:17575325}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the ATPase d subunit family. {ECO:0000305}.
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DR EMBL; D10021; BAA00911.1; -; mRNA.
DR EMBL; D13120; BAA02422.1; -; mRNA.
DR EMBL; BC059139; AAH59139.1; -; mRNA.
DR EMBL; BC078846; AAH78846.1; -; mRNA.
DR PIR; JS0739; JS0739.
DR RefSeq; NP_062256.1; NM_019383.2.
DR AlphaFoldDB; P31399; -.
DR SMR; P31399; -.
DR BioGRID; 566012; 3.
DR CORUM; P31399; -.
DR IntAct; P31399; 2.
DR MINT; P31399; -.
DR STRING; 10116.ENSRNOP00000004836; -.
DR CarbonylDB; P31399; -.
DR iPTMnet; P31399; -.
DR PhosphoSitePlus; P31399; -.
DR World-2DPAGE; 0004:P31399; -.
DR jPOST; P31399; -.
DR PaxDb; P31399; -.
DR PRIDE; P31399; -.
DR GeneID; 641434; -.
DR KEGG; rno:641434; -.
DR CTD; 10476; -.
DR RGD; 620083; Atp5pd.
DR VEuPathDB; HostDB:ENSRNOG00000003626; -.
DR eggNOG; KOG3366; Eukaryota.
DR HOGENOM; CLU_130600_0_0_1; -.
DR InParanoid; P31399; -.
DR OMA; VSKGRWA; -.
DR OrthoDB; 1299717at2759; -.
DR PhylomeDB; P31399; -.
DR Reactome; R-RNO-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-RNO-8949613; Cristae formation.
DR PRO; PR:P31399; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003626; Expressed in heart and 19 other tissues.
DR Genevisible; P31399; RN.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IDA:RGD.
DR GO; GO:0000274; C:mitochondrial proton-transporting ATP synthase, stator stalk; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0015078; F:proton transmembrane transporter activity; TAS:RGD.
DR GO; GO:0046034; P:ATP metabolic process; IDA:RGD.
DR GO; GO:1901653; P:cellular response to peptide; IEP:RGD.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; ISO:RGD.
DR Gene3D; 6.10.280.70; -; 1.
DR InterPro; IPR008689; ATP_synth_F0_dsu_mt.
DR InterPro; IPR036228; ATP_synth_F0_dsu_sf_mt.
DR PANTHER; PTHR12700; PTHR12700; 1.
DR Pfam; PF05873; Mt_ATP-synt_D; 1.
DR PIRSF; PIRSF005514; ATPase_F0_D_mt; 1.
DR SUPFAM; SSF161065; SSF161065; 1.
PE 1: Evidence at protein level;
KW Acetylation; CF(0); Direct protein sequencing; Hydrogen ion transport;
KW Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P13620"
FT CHAIN 2..161
FT /note="ATP synthase subunit d, mitochondrial"
FT /id="PRO_0000071675"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P13620"
FT MOD_RES 32
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX2"
FT MOD_RES 48
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX2"
FT MOD_RES 63
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX2"
FT MOD_RES 78
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX2"
FT MOD_RES 78
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX2"
FT MOD_RES 85
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX2"
FT MOD_RES 85
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX2"
FT MOD_RES 95
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX2"
FT MOD_RES 95
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX2"
FT MOD_RES 117
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75947"
FT MOD_RES 144
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX2"
FT MOD_RES 144
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX2"
FT MOD_RES 149
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX2"
FT MOD_RES 149
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX2"
FT CONFLICT 79
FT /note="I -> D (in Ref. 1; BAA00911)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="P -> L (in Ref. 1; BAA00911)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 161 AA; 18763 MW; 285F075DE5641261 CRC64;
MAGRKLALKT IDWVSFVEIM PQNQKAIGNA LKSWNETFHT RLASLSEKPP AIDWAYYRAN
VDKPGLVDDF KNKYNALKIP VPEDKYTALV DAEEKEDVKN CAQFVTGSQA RVREYEKQLE
KIKNMIPFDQ MTIDDLNEVF PETKLDKRKY PYWPHQPIEN L
