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Overview

Uniprot IDQ03265
Protein NameATP synthase F(1) complex subunit alpha, mitochondrial
Gene NameAtp5f1a
OrganismMus musculus

Kla Sites from experimental identification

Position Flanking peptide
126 FGNDKLIKEGDVVKR
161 LGNAIDGKGPIGSKT
167 GKGPIGSKTRRRVGL
175 TRRRVGLKAPGIIPR
194 EPMQTGIKAVDSLVP
230 IDTIINQKRFNDGTD
239 FNDGTDEKKKLYCIY
261 STVAQLVKRLTDADA
305 EYFRDNGKHALIIYD
316 IIYDDLSKQAVAYRQ
427 AAQTRAMKQVAGTMK
498 GVRGYLDKLEPSKIT
503 LDKLEPSKITKFENA
506 LEPSKITKFENAFLS
531 GNIRSDGKISEQSDA
539 ISEQSDAKLKEIVTN

Function

Subunit alpha, 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. ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk. 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 (By similarity). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). With the catalytic subunit beta (ATP5F1B), forms the catalytic core in the F(1) domain. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity)

Protein Sequence

10 MLSVRVAAAV 20 ARALPRRAGL 30 VSKNALGSSF 40 VGARNLHASN 50 TRLQKTGTAE 60 MSSILEERIL 70 GADTSVDLEE 80 TGRVLSIGDG 90 IARVHGLRNV 100 QAEEMVEFSS 110 GLKGMSLNLE 120 PDNVGVVVFG 130 NDKLIKEGDV 140 VKRTGAIVDV 150 PVGEELLGRV 160 VDALGNAIDG 170 KGPIGSKTRR 180 RVGLKAPGII 190 PRISVREPMQ 200 TGIKAVDSLV 210 PIGRGQRELI 220 IGDRQTGKTS 230 IAIDTIINQK 240 RFNDGTDEKK 250 KLYCIYVAIG 260 QKRSTVAQLV 270 KRLTDADAMK 280 YTIVVSATAS 290 DAAPLQYLAP 300 YSGCSMGEYF 310 RDNGKHALII 320 YDDLSKQAVA 330 YRQMSLLLRR 340 PPGREAYPGD 350 VFYLHSRLLE 360 RAAKMNDSFG 370 GGSLTALPVI 380 ETQAGDVSAY 390 IPTNVISITD 400 GQIFLETELF 410 YKGIRPAINV 420 GLSVSRVGSA 430 AQTRAMKQVA 440 GTMKLELAQY 450 REVAAFAQFG 460 SDLDAATQQL 470 LSRGVRLTEL 480 LKQGQYSPMA 490 IEEQVAVIYA 500 GVRGYLDKLE 510 PSKITKFENA 520 FLSHVISQHQ 530 SLLGNIRSDG 540 KISEQSDAKL 550 KEIVTNFLAG FEP

Gene Ontology

Classification GO ID Description
Cellular Component GO:0009986 cell surface
Biological Process GO:0006629 lipid metabolic process
Biological Process GO:0001937 negative regulation of endothelial cell proliferation
Biological Process GO:0043536 positive regulation of blood vessel endothelial cell migration
Biological Process GO:0015986 proton motive force-driven ATP synthesis
Biological Process GO:0042776 proton motive force-driven mitochondrial ATP synthesis
Biological Process GO:0045471 response to ethanol
Biological Process GO:0014850 response to muscle activity
Cellular Component GO:0016020 membrane
Cellular Component GO:0045121 membrane raft
Cellular Component GO:0005743 mitochondrial inner membrane
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0043209 myelin sheath
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0045259 proton-transporting ATP synthase complex
Cellular Component GO:0097229 sperm end piece
Molecular Function GO:0043531 ADP binding
Molecular Function GO:0043532 angiostatin binding
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0046872 metal ion binding
Molecular Function GO:0042288 MHC class I protein binding
Molecular Function GO:0002020 protease binding
Molecular Function GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
Biological Process GO:0006754 ATP biosynthetic process
Biological Process GO:0071549 cellular response to dexamethasone stimulus
Biological Process GO:0071732 cellular response to nitric oxide

Reference

[1] Chang J, Wu W, Qian P, Lu Z, He X et al.. Multi-omics study on the effect of moderate-intensity exercise on protein lactylation in mouse muscle tissue.. Front Cell Dev Biol 12:1472338. 2024. PMID: 39935788.

[2] Zhuo W, Zhang M, Tan J, Gao Y, Wang Y et al.. Lysine lactylation analysis of proteins in the heart of the Kawasaki disease mouse model.. Front Cell Dev Biol 13:1550220. 2025. PMID: 40114965.

[3] Wu D, Tang Y, Li X, Xiong S, Zhang Z et al.. Characterization of protein lactylation in healthy and ischemic mouse hearts.. Front Cardiovasc Med 12:1644886. 2025. PMID: 41089239.