ID ATP5H_HUMAN Reviewed; 161 AA. AC O75947; B2R5L6; Q9H3J4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 207. 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|HGNC:HGNC:845}; Synonyms=ATP5H; GN ORFNames=My032; 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 [MRNA] (ISOFORM 1). RC TISSUE=Thymus; RA Lee H.C., Park D.S., Lee C.M., Cho W.K., Ahn H.J., Lee M.Y., Hwang M.Y., RA Jin S.W., Sohn U.I.K.; RT "cDNA cloning, and chromosomal localization of a human F1F0-type ATPase RT subunit d."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Fetal brain; RA Mao Y.M., Xie Y., Ying K.; RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Uterus; 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]. 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, and Pancreas; 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 PROTEIN SEQUENCE OF 10-25; 33-58; 64-72; 79-109 AND 124-144. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-85; LYS-95; LYS-117 AND LYS-149, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [9] 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 [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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: 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 (By similarity). Interacts with CC FLVCR2; this interaction occurs in the absence of heme and is disrupted CC upon heme binding (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:P13620, ECO:0000250|UniProtKB:P31399, CC ECO:0000250|UniProtKB:Q9DCX2}. CC -!- INTERACTION: CC O75947; P24539: ATP5PB; NbExp=3; IntAct=EBI-724024, EBI-1044810; CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O75947-1; Sequence=Displayed; CC Name=2; CC IsoId=O75947-2; Sequence=VSP_000436; CC -!- SIMILARITY: Belongs to the ATPase d subunit family. {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; AF087135; AAC36338.1; -; mRNA. DR EMBL; AF070650; AAD20956.1; -; mRNA. DR EMBL; AF061735; AAG43146.1; -; mRNA. DR EMBL; AK312230; BAG35163.1; -; mRNA. DR EMBL; CH471099; EAW89228.1; -; Genomic_DNA. DR EMBL; BC032245; AAH32245.1; -; mRNA. DR EMBL; BC038092; AAH38092.1; -; mRNA. DR CCDS; CCDS11712.1; -. [O75947-1] DR CCDS; CCDS32727.1; -. [O75947-2] DR RefSeq; NP_001003785.1; NM_001003785.1. [O75947-2] DR RefSeq; NP_006347.1; NM_006356.2. [O75947-1] DR PDB; 8H9F; EM; 2.69 A; M=2-161. DR PDB; 8H9G; EM; 2.95 A; M=2-161. DR PDB; 8H9J; EM; 3.26 A; M=2-161. DR PDB; 8H9K; EM; 3.51 A; M=2-161. DR PDB; 8H9M; EM; 3.00 A; M=2-161. DR PDB; 8H9N; EM; 3.56 A; M=2-161. DR PDB; 8H9Q; EM; 3.47 A; M=2-161. DR PDB; 8H9R; EM; 3.97 A; M=2-161. DR PDB; 8H9S; EM; 2.53 A; M=2-161. DR PDB; 8H9T; EM; 2.77 A; M=2-161. DR PDB; 8H9U; EM; 2.61 A; M=2-161. DR PDB; 8H9V; EM; 3.02 A; M=2-161. DR PDBsum; 8H9F; -. DR PDBsum; 8H9G; -. DR PDBsum; 8H9J; -. DR PDBsum; 8H9K; -. DR PDBsum; 8H9M; -. DR PDBsum; 8H9N; -. DR PDBsum; 8H9Q; -. DR PDBsum; 8H9R; -. DR PDBsum; 8H9S; -. DR PDBsum; 8H9T; -. DR PDBsum; 8H9U; -. DR PDBsum; 8H9V; -. DR AlphaFoldDB; O75947; -. DR EMDB; EMD-34565; -. DR EMDB; EMD-34566; -. DR EMDB; EMD-34569; -. DR EMDB; EMD-34570; -. DR EMDB; EMD-34573; -. DR EMDB; EMD-34574; -. DR EMDB; EMD-34577; -. DR EMDB; EMD-34578; -. DR EMDB; EMD-34580; -. DR EMDB; EMD-34581; -. DR EMDB; EMD-34582; -. DR EMDB; EMD-34583; -. DR SMR; O75947; -. DR BioGRID; 115739; 230. DR ComplexPortal; CPX-6151; Mitochondrial proton-transporting ATP synthase complex. DR CORUM; O75947; -. DR IntAct; O75947; 100. DR MINT; O75947; -. DR STRING; 9606.ENSP00000301587; -. DR TCDB; 3.A.2.1.15; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily. DR CarbonylDB; O75947; -. DR GlyGen; O75947; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O75947; -. DR MetOSite; O75947; -. DR PhosphoSitePlus; O75947; -. DR SwissPalm; O75947; -. DR BioMuta; ATP5H; -. DR OGP; O75947; -. DR REPRODUCTION-2DPAGE; IPI00456049; -. DR CPTAC; CPTAC-29; -. DR CPTAC; CPTAC-30; -. DR EPD; O75947; -. DR jPOST; O75947; -. DR MassIVE; O75947; -. DR MaxQB; O75947; -. DR PaxDb; 9606-ENSP00000301587; -. DR PeptideAtlas; O75947; -. DR ProteomicsDB; 50308; -. [O75947-1] DR ProteomicsDB; 50309; -. [O75947-2] DR Pumba; O75947; -. DR TopDownProteomics; O75947-1; -. [O75947-1] DR TopDownProteomics; O75947-2; -. [O75947-2] DR Antibodypedia; 32083; 294 antibodies from 32 providers. DR DNASU; 10476; -. DR Ensembl; ENST00000301587.9; ENSP00000301587.4; ENSG00000167863.12. [O75947-1] DR Ensembl; ENST00000344546.8; ENSP00000344230.4; ENSG00000167863.12. [O75947-2] DR GeneID; 10476; -. DR KEGG; hsa:10476; -. DR MANE-Select; ENST00000301587.9; ENSP00000301587.4; NM_006356.3; NP_006347.1. DR UCSC; uc002jmn.2; human. [O75947-1] DR AGR; HGNC:845; -. DR CTD; 10476; -. DR DisGeNET; 10476; -. DR GeneCards; ATP5PD; -. DR HGNC; HGNC:845; ATP5PD. DR HPA; ENSG00000167863; Low tissue specificity. DR MIM; 618121; gene. DR neXtProt; NX_O75947; -. DR OpenTargets; ENSG00000167863; -. DR PharmGKB; PA25135; -. DR VEuPathDB; HostDB:ENSG00000167863; -. DR eggNOG; KOG3366; Eukaryota. DR GeneTree; ENSGT00390000003582; -. DR HOGENOM; CLU_130600_0_0_1; -. DR InParanoid; O75947; -. DR OMA; VSKGRWA; -. DR OrthoDB; 3108295at2759; -. DR PhylomeDB; O75947; -. DR TreeFam; TF314031; -. DR BioCyc; MetaCyc:HS09654-MONOMER; -. DR PathwayCommons; O75947; -. DR Reactome; R-HSA-163210; Formation of ATP by chemiosmotic coupling. DR Reactome; R-HSA-8949613; Cristae formation. DR SignaLink; O75947; -. DR SIGNOR; O75947; -. DR BioGRID-ORCS; 10476; 254 hits in 1148 CRISPR screens. DR ChiTaRS; ATP5H; human. DR GeneWiki; ATP5H; -. DR GenomeRNAi; 10476; -. DR Pharos; O75947; Tbio. DR PRO; PR:O75947; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; O75947; Protein. DR Bgee; ENSG00000167863; Expressed in heart right ventricle and 214 other cell types or tissues. DR ExpressionAtlas; O75947; baseline and differential. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB. 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:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro. 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; IDA:UniProtKB. 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; ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL; 1. DR PANTHER; PTHR12700:SF12; ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL; 1. DR Pfam; PF05873; Mt_ATP-synt_D; 1. DR PIRSF; PIRSF005514; ATPase_F0_D_mt; 1. DR SUPFAM; SSF161065; ATP synthase D chain-like; 1. DR UCD-2DPAGE; O75947; -. DR Genevisible; O75947; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; CF(0); KW Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane; KW Mitochondrion; Mitochondrion inner membrane; Reference proteome; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:25944712" FT CHAIN 2..161 FT /note="ATP synthase subunit d, mitochondrial" FT /id="PRO_0000071673" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:25944712" FT MOD_RES 32 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:0007744|PubMed:19608861" 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:0007744|PubMed:19608861" 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:0007744|PubMed:19608861" 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:0007744|PubMed:19608861" FT MOD_RES 149 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9DCX2" FT VAR_SEQ 74..97 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3" FT /id="VSP_000436" FT HELIX 14..18 FT /evidence="ECO:0007829|PDB:8H9G" FT HELIX 22..24 FT /evidence="ECO:0007829|PDB:8H9V" FT HELIX 25..43 FT /evidence="ECO:0007829|PDB:8H9G" FT HELIX 55..58 FT /evidence="ECO:0007829|PDB:8H9G" FT STRAND 63..65 FT /evidence="ECO:0007829|PDB:8H9G" FT HELIX 66..75 FT /evidence="ECO:0007829|PDB:8H9G" FT HELIX 87..123 FT /evidence="ECO:0007829|PDB:8H9G" FT HELIX 128..130 FT /evidence="ECO:0007829|PDB:8H9G" FT HELIX 133..139 FT /evidence="ECO:0007829|PDB:8H9G" FT HELIX 141..143 FT /evidence="ECO:0007829|PDB:8H9G" FT TURN 147..149 FT /evidence="ECO:0007829|PDB:8H9G" FT TURN 158..160 FT /evidence="ECO:0007829|PDB:8H9G" SQ SEQUENCE 161 AA; 18491 MW; E93020ADA1BA1694 CRC64; MAGRKLALKT IDWVAFAEII PQNQKAIASS LKSWNETLTS RLAALPENPP AIDWAYYKAN VAKAGLVDDF EKKFNALKVP VPEDKYTAQV DAEEKEDVKS CAEWVSLSKA RIVEYEKEME KMKNLIPFDQ MTIEDLNEAF PETKLDKKKY PYWPHQPIEN L //