ATP5H_BOVIN
ID ATP5H_BOVIN Reviewed; 161 AA.
AC P13620; Q3SX10;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 146.
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:0000250|UniProtKB:O75947}; Synonyms=ATP5H;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ACETYLATION AT ALA-2, AND PROTEIN SEQUENCE OF
RP 2-161.
RX PubMed=2890767; DOI=10.1016/0022-2836(87)90611-5;
RA Walker J.E., Runswick M.J., Poulter L.;
RT "ATP synthase from bovine mitochondria. The characterization and sequence
RT analysis of two membrane-associated sub-units and of the corresponding
RT cDNAs.";
RL J. Mol. Biol. 197:89-100(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
RX PubMed=17570365; DOI=10.1016/j.febslet.2007.05.079;
RA Chen R., Runswick M.J., Carroll J., Fearnley I.M., Walker J.E.;
RT "Association of two proteolipids of unknown function with ATP synthase from
RT bovine heart mitochondria.";
RL FEBS Lett. 581:3145-3148(2007).
RN [4]
RP IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
RX PubMed=25851905; DOI=10.1074/jbc.m115.645283;
RA Lee J., Ding S., Walpole T.B., Holding A.N., Montgomery M.G.,
RA Fearnley I.M., Walker J.E.;
RT "Organization of Subunits in the Membrane Domain of the Bovine F-ATPase
RT Revealed by Covalent Cross-linking.";
RL J. Biol. Chem. 290:13308-13320(2015).
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:17570365,
CC ECO:0000269|PubMed:25851905}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the ATPase d subunit family. {ECO:0000305}.
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DR EMBL; X06089; CAA29473.1; -; mRNA.
DR EMBL; BC104564; AAI04565.1; -; mRNA.
DR PIR; S00764; S00764.
DR RefSeq; NP_777149.1; NM_174724.4.
DR PDB; 2CLY; X-ray; 2.80 A; B/E=2-161.
DR PDB; 2WSS; X-ray; 3.20 A; U=2-119.
DR PDB; 4B2Q; EM; 37.00 A; U/u=5-124.
DR PDB; 5ARA; EM; 6.70 A; U=2-125.
DR PDB; 5ARE; EM; 7.40 A; U=2-125.
DR PDB; 5ARH; EM; 7.20 A; U=2-125.
DR PDB; 5ARI; EM; 7.40 A; U=2-125.
DR PDB; 5FIJ; EM; 7.40 A; U=2-125.
DR PDB; 5FIK; EM; 6.40 A; U=2-125.
DR PDB; 5FIL; EM; 7.10 A; U=2-125.
DR PDB; 6YY0; EM; 3.23 A; d=2-161.
DR PDB; 6ZBB; EM; 3.61 A; d=2-161.
DR PDB; 6ZIQ; EM; 4.33 A; d=2-161.
DR PDB; 6ZIT; EM; 3.49 A; d=2-161.
DR PDB; 6ZIU; EM; 6.02 A; d=2-161.
DR PDB; 6ZPO; EM; 4.00 A; d=2-161.
DR PDB; 6ZQM; EM; 3.29 A; d=2-161.
DR PDB; 6ZQN; EM; 4.00 A; d=2-161.
DR PDB; 7AJB; EM; 9.20 A; Ad/d=2-161.
DR PDB; 7AJC; EM; 11.90 A; Ad/d=2-161.
DR PDB; 7AJD; EM; 9.00 A; Ad/d=2-161.
DR PDB; 7AJE; EM; 9.40 A; Ad/d=2-161.
DR PDB; 7AJF; EM; 8.45 A; Ad/d=2-161.
DR PDB; 7AJG; EM; 10.70 A; Ad/d=2-161.
DR PDB; 7AJH; EM; 9.70 A; Ad/d=2-161.
DR PDB; 7AJI; EM; 11.40 A; Ad/d=2-161.
DR PDB; 7AJJ; EM; 13.10 A; Ad/d=2-161.
DR PDBsum; 2CLY; -.
DR PDBsum; 2WSS; -.
DR PDBsum; 4B2Q; -.
DR PDBsum; 5ARA; -.
DR PDBsum; 5ARE; -.
DR PDBsum; 5ARH; -.
DR PDBsum; 5ARI; -.
DR PDBsum; 5FIJ; -.
DR PDBsum; 5FIK; -.
DR PDBsum; 5FIL; -.
DR PDBsum; 6YY0; -.
DR PDBsum; 6ZBB; -.
DR PDBsum; 6ZIQ; -.
DR PDBsum; 6ZIT; -.
DR PDBsum; 6ZIU; -.
DR PDBsum; 6ZPO; -.
DR PDBsum; 6ZQM; -.
DR PDBsum; 6ZQN; -.
DR PDBsum; 7AJB; -.
DR PDBsum; 7AJC; -.
DR PDBsum; 7AJD; -.
DR PDBsum; 7AJE; -.
DR PDBsum; 7AJF; -.
DR PDBsum; 7AJG; -.
DR PDBsum; 7AJH; -.
DR PDBsum; 7AJI; -.
DR PDBsum; 7AJJ; -.
DR AlphaFoldDB; P13620; -.
DR SMR; P13620; -.
DR CORUM; P13620; -.
DR DIP; DIP-39020N; -.
DR IntAct; P13620; 2.
DR MINT; P13620; -.
DR STRING; 9913.ENSBTAP00000028282; -.
DR iPTMnet; P13620; -.
DR PaxDb; P13620; -.
DR PeptideAtlas; P13620; -.
DR PRIDE; P13620; -.
DR Ensembl; ENSBTAT00000028282; ENSBTAP00000028282; ENSBTAG00000021227.
DR Ensembl; ENSBTAT00000074726; ENSBTAP00000068634; ENSBTAG00000021227.
DR GeneID; 282710; -.
DR KEGG; bta:282710; -.
DR CTD; 10476; -.
DR VEuPathDB; HostDB:ENSBTAG00000021227; -.
DR VGNC; VGNC:97244; ATP5PD.
DR eggNOG; KOG3366; Eukaryota.
DR GeneTree; ENSGT00390000003582; -.
DR HOGENOM; CLU_130600_0_0_1; -.
DR InParanoid; P13620; -.
DR OMA; VSKGRWA; -.
DR OrthoDB; 1299717at2759; -.
DR TreeFam; TF314031; -.
DR Reactome; R-BTA-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-BTA-8949613; Cristae formation.
DR EvolutionaryTrace; P13620; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000021227; Expressed in tongue muscle and 104 other tissues.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0000274; C:mitochondrial proton-transporting ATP synthase, stator stalk; IBA:GO_Central.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:Ensembl.
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; IEA:Ensembl.
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 3D-structure; Acetylation; CF(0); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2890767"
FT CHAIN 2..161
FT /note="ATP synthase subunit d, mitochondrial"
FT /id="PRO_0000071672"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:2890767"
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 72
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 HELIX 13..17
FT /evidence="ECO:0007829|PDB:2CLY"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:2CLY"
FT HELIX 25..44
FT /evidence="ECO:0007829|PDB:2CLY"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:2CLY"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:2CLY"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:2CLY"
FT HELIX 101..122
FT /evidence="ECO:0007829|PDB:2CLY"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:6YY0"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:6YY0"
SQ SEQUENCE 161 AA; 18692 MW; 60ED98258E57C7E1 CRC64;
MAGRKLALKT IDWVAFGEII PRNQKAVANS LKSWNETLTS RLATLPEKPP AIDWAYYKAN
VAKAGLVDDF EKKFNALKVP IPEDKYTAQV DAEEKEDVKS CAEFLTQSKT RIQEYEKELE
KMRNIIPFDQ MTIEDLNEVF PETKLDKKKY PYWPHRPIET L
