Q5ZLC5

PR
Gene name
ATP5F1B
Protein name
ATP synthase subunit beta, mitochondrial
Names
ATP synthase F1 subunit beta
Species
Gallus gallus (Chicken)
KEGG Pathway
gga:426673
EC number
7.1.2.2: Hydron translocation linked to the hydrolysis of a nucleoside triphosphate
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-91 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q5ZLC5

Entry ID Method Resolution Chain Position Source
AF-Q5ZLC5-F1 Predicted AlphaFoldDB

No variants for Q5ZLC5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5ZLC5

No associated diseases with Q5ZLC5

No regional properties for Q5ZLC5

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q5ZLC5

Functions

Description
EC Number 7.1.2.2 Hydron translocation linked to the hydrolysis of a nucleoside triphosphate
Subcellular Localization
  • Mitochondrion inner membrane ; Peripheral membrane protein ; Matrix side
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
mitochondrial proton-transporting ATP synthase complex A proton-transporting ATP synthase complex found in the mitochondrial membrane.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
proton-transporting ATP synthase complex, catalytic core F(1) The sector of a hydrogen-transporting ATP synthase complex in which the catalytic activity resides; it comprises the catalytic core and central stalk, and is peripherally associated with a membrane, such as the plasma membrane or the mitochondrial inner membrane, when the entire ATP synthase is assembled.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
proton-transporting ATP synthase activity, rotational mechanism Enables the synthesis of ATP from ADP and phosphate by the transfer of protons from one side of a membrane to the other by a rotational mechanism driven by a gradient according to the reaction: ADP + H2O + phosphate + H+(in) -> ATP + H+(out).
proton-transporting ATPase activity, rotational mechanism Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) = ADP + phosphate + H+(out), by a rotational mechanism.

2 GO annotations of biological process

Name Definition
angiogenesis Blood vessel formation when new vessels emerge from the proliferation of pre-existing blood vessels.
proton motive force-driven mitochondrial ATP synthesis The transport of protons across a mitochondrial membrane to generate an electrochemical gradient (proton-motive force) that powers ATP synthesis.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P00829 ATP5F1B ATP synthase subunit beta, mitochondrial Bos taurus (Bovine) PR
Q05825 ATPsynbeta ATP synthase subunit beta, mitochondrial Drosophila melanogaster (Fruit fly) PR
P06576 ATP5F1B ATP synthase subunit beta, mitochondrial Homo sapiens (Human) PR
P56480 Atp5f1b ATP synthase subunit beta, mitochondrial Mus musculus (Mouse) PR
P10719 Atp5f1b ATP synthase subunit beta, mitochondrial Rattus norvegicus (Rat) PR
P46561 atp-2 ATP synthase subunit beta, mitochondrial Caenorhabditis elegans PR
10 20 30 40 50 60
MLGLAGRCSA AAASAARPAL RRAAGPSHGF LPLLLSRGAG PAAAVGARRD HAAQAAPAAK
70 80 90 100 110 120
AGSATGRIVA VIGAVVDVQF DEGLPPILNA LEVQGRETRL VLEVAQHLGE NTVRTIAMDG
130 140 150 160 170 180
TEGLVRGQKV LDSGAPIRIP VGPETLGRIM NVIGEPIDER GPITTKQFAA IHAEAPEFVE
190 200 210 220 230 240
MSVEQKILVT GIKVVDLLAP YAKGGKIGLF GGAGVGKTVL IMELINNVAK AHGGYSVFAG
250 260 270 280 290 300
VGERTREGND LYHEMIESGV INLKDATSKV ALVYGQMNEP PGARARVALT GLTVAEYFRD
310 320 330 340 350 360
QEGQDVLLFI DNIFRFTQAG SEVSALLGRI PSAVGYQPTL ATDMGTMQER ITTTRKGSIT
370 380 390 400 410 420
SVQAIYVPAD DLTDPAPATT FAHLDATTVL SRAIAELGIY PAVDPLDSTS RIMDPNIVGP
430 440 450 460 470 480
EHYDVARGVQ KILQDYKSLQ DIIAILGMDE LSEEDKLTVA RARKIQRFLS QPFQVAEVFT
490 500 510 520 530
GHMGKLVPLK ETIKGFKQIL AGEYDHLPEQ AFYMVGPIEE AVAKAEKLAE EHA