Overview
| Uniprot ID | H0VZD9 |
| Protein Name | ATP synthase subunit beta |
| Gene Name | ATP5F1B |
| Organism | Cavia porcellus |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 124 |
EGLVRGQKVLDSGAP |
| 133 |
LDSGAPIKIPVGPET |
| 443 |
MGKLVPLKETIKGFQ |
| 480 |
EAVAKADKLAEEHAS |
Function
Catalytic subunit beta, 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. In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro. With the subunit alpha (ATP5F1A), forms the catalytic core in the F(1) domain
Protein Sequence
10
MLSLVGRVAA
20
ASACGALRGL
30
SPSASLPQPQ
40
LLLRASPAAV
50
QPARDYAAQT
60
SPSPKPGAAT
70
GRIVAVIGAV
80
VDVQFDEGLP
90
PILNALEVQG
100
RDTRLVLEVA
110
QHLGESTVRT
120
IAMDGTEGLV
130
RGQKVLDSGA
140
PIKIPVGPET
150
LGRIMNVIGE
160
PIDERGPIKT
170
KLFGGAGVGK
180
TVLIMELINN
190
VAKAHGGYSV
200
FAGVGERTRE
210
GNDLYHEMIE
220
SGVINLKDAT
230
SKVALVYGQM
240
NEPPGARARV
250
ALTGLTVAEY
260
FRDQEGQDVL
270
LFIDNIFRFT
280
QAGSEVSALL
290
GRIPSAVGYQ
300
PTLATDMGTM
310
QERITTTKKG
320
SITSVQAIYV
330
PADDLTDPAP
340
ATTFAHLDAT
350
TVLSRAIAEL
360
GIYPAVDPLD
370
STSRIMDPNI
380
VGSEHYDVAR
390
GVQKILQDYK
400
SLQDIIAILG
410
MDELSEEDKL
420
TVSRARKIQR
430
FLSQPFQVAE
440
VFTGHMGKLV
450
PLKETIKGFQ
460
QILAGDYDHL
470
PEQAFYMVGP
480
IEEAVAKADK
LAEEHAS
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0009986 |
cell surface |
| Cellular Component |
GO:0031966 |
mitochondrial membrane |
| Cellular Component |
GO:0042645 |
mitochondrial nucleoid |
| Cellular Component |
GO:0005886 |
plasma membrane |
| Cellular Component |
GO:0045259 |
proton-transporting ATP synthase complex |
| Molecular Function |
GO:0043532 |
angiostatin binding |
| Molecular Function |
GO:0005524 |
ATP binding |
| Molecular Function |
GO:0042288 |
MHC class I protein binding |
| Molecular Function |
GO:0046933 |
proton-transporting ATP synthase activity, rotational mechanism |
| Molecular Function |
GO:0046961 |
proton-transporting ATPase activity, rotational mechanism |
| Biological Process |
GO:0001525 |
angiogenesis |
| Biological Process |
GO:0043536 |
positive regulation of blood vessel endothelial cell migration |
| Biological Process |
GO:0042776 |
proton motive force-driven mitochondrial ATP synthesis |
| Biological Process |
GO:0051453 |
regulation of intracellular pH |
Reference
[1] Feng J, Chen X, Li R, Xie Y, Zhang X et al.. Lactylome analysis reveals potential target modified proteins in the retina of form-deprivation myopia.. iScience 27(9):110606. 2024 Sep 20. PMID: 39246443.