Search Results

Overview

Uniprot IDO75947
Protein NameATP synthase peripheral stalk subunit d, mitochondrial
Gene NameATP5PD
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
109 AEWVSLSKARIVEYE
117 ARIVEYEKEMEKMKN
121 EYEKEMEKMKNLIPF
149 ETKLDKKKYPYWPHQ
32 KAIASSLKSWNETLT
63 YYKANVAKAGLVDDF
72 GLVDDFEKKFNALKV
78 EKKFNALKVPVPEDK
85 KVPVPEDKYTAQVDA
95 AQVDAEEKEDVKSCA
99 AEEKEDVKSCAEWVS

Function

Subunit d, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (PubMed:37244256). ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel (PubMed:37244256). These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk (PubMed:37244256). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (Probable). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). Part of the complex F(0) domain (PubMed:37244256). Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements (By similarity)

Protein Sequence

10 MAGRKLALKT 20 IDWVAFAEII 30 PQNQKAIASS 40 LKSWNETLTS 50 RLAALPENPP 60 AIDWAYYKAN 70 VAKAGLVDDF 80 EKKFNALKVP 90 VPEDKYTAQV 100 DAEEKEDVKS 110 CAEWVSLSKA 120 RIVEYEKEME 130 KMKNLIPFDQ 140 MTIEDLNEAF 150 PETKLDKKKY 160 PYWPHQPIEN L

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005743 mitochondrial inner membrane
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0045259 proton-transporting ATP synthase complex
Molecular Function GO:0015078 proton transmembrane transporter activity
Biological Process GO:0015986 proton motive force-driven ATP synthesis
Biological Process GO:0042776 proton motive force-driven mitochondrial ATP synthesis

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[3] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[5] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.