Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for P22068

Entry ID Method Resolution Chain Position Source
AF-P22068-F1 Predicted AlphaFoldDB

2 variants for P22068

Variant ID(s) Position Change Description Diseaes Association Provenance
I_970338_C_T 8 S>N No Jeffares_SNPs
I_969863_A_T 166 D>E No Jeffares_SNPs

No associated diseases with P22068

4 regional properties for P22068

Type Name Position InterPro Accession
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain 183 - 401 IPR000194
domain AAA+ ATPase domain 195 - 378 IPR003593
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain 57 - 126 IPR004100
active_site ATPase, alpha/beta subunit, nucleotide-binding domain, active site 392 - 401 IPR020003

Functions

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

4 GO annotations of cellular component

Name Definition
mitochondrial proton-transporting ATP synthase complex A proton-transporting ATP synthase complex found in the mitochondrial membrane.
mitochondrial proton-transporting ATP synthase, catalytic core The hexamer, comprising three alpha and three beta subunits, that possesses the catalytic activity of the mitochondrial hydrogen-transporting ATP synthase.
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.

4 GO annotations of molecular function

Name Definition
ADP binding Binding to ADP, adenosine 5'-diphosphate.
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.

1 GO annotations of biological process

Name Definition
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLKKQALSGI RRFSLATKQS FVKTSYKLPR KSWLNTAKFN TIRYASTEAA KHNKGSIKQV
70 80 90 100 110 120
IGAVVDCQFE DADSLPSILN ALEVKLPDNK RLVLEVAQHV GENTVRTIAM DGTEGLVRGT
130 140 150 160 170 180
AVIDTGSPIS IPVGPGTLGR IMNVIGEPVD ERGPIKAVKY SPIHADAPSF EEQSTTPEIL
190 200 210 220 230 240
ETGIKVVDLL APYARGGKIG LFGGAGVGKT VFIQELINNI AKAHGGYSVF TGVGERTREG
250 260 270 280 290 300
NDLYREMQET GVIKLEGESK AALVFGQMNE PPGARARVAL TGLTVAEYFR DIEGQDVLLF
310 320 330 340 350 360
IDNIFRFTQA GSEVSALLGR IPSAVGYQPT LATDMGAMQE RITTTKKGSI TSVQAVYVPA
370 380 390 400 410 420
DDLTDPAPAT TFAHLDATTV LSRSISELGI YPAVDPLDSK SRMMDPRILG EEHYNLAGSV
430 440 450 460 470 480
QQMLQEYKSL QDIIAILGMD ELSEADKLTV ERARKVQRFL SQPFAVAEVF TGIEGRLVSL
490 500 510 520
KDTIRSFKEI LEGKHDSLPE SAFYMVGSID DAVKKAEKIA QELAA