Search by BoMiProt ID - Bomi10543

Primary Information

BoMiProt ID Bomi10543
Protein Name V-type proton ATPase subunit C 1/Vacuolar proton pump subunit C 1
Organism Bos taurus
Uniprot IDP21282
Milk FractionExosomes
Ref Sequence ID NP_788849.1
Aminoacid Length 382
Molecular Weight 43986
FASTA Sequence Download
Gene Name ATP6V1C1
Gene ID 338089
Protein Existence Status Reviewed

Secondary Information

Presence in other biological fluids/tissue/cells occipital lobe
Protein Function Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons.Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity
Biochemical Properties Mammalian V-ATPase is a rotary machine made up of two domains: the ATP-hydrolytic V1 domain and the proton-translocation Vo domain. The V1 domain consists of three catalytic AB heterodimers that form a heterohexamer with threefold rotational pseudosymmetry, three peripheral stalks each consisting of the subunits EG, one central rotor including subunits D and F, and the regulatory subunits C and H.The composition of the mammalian V1 domain is similar to that of the yeast domain, which is a well-characterized model for V-ATPase studies. The c-ring of yeast’s Vo domain contains eight subunit c, one subunit c’, and one subunit c”.
PTMs N-acetylation at Thr
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
SCOP Class : Alpha and beta proteins (a+b)
Fold : Vacuolar ATP synthase subunit C
Superfamily : Vacuolar ATP synthase subunit C
Family : Vacuolar ATP synthase subunit C
Domain Name : 6XBW G:2-379

CATH Matched CATH superfamily
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Bibliography 1.Wang R, Long T, Hassan A, Wang J, Sun Y, Xie XS, Li X. Cryo-EM structures of intact V-ATPase from bovine brain. Nat Commun. 2020 Aug 6;11(1):3921. doi: 10.1038/s41467-020-17762-9. PMID: 32764564; PMCID: PMC7414150. 2.Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase.Zhao J, Benlekbir S, Rubinstein JL.Nature. 2015 May 14; 521(7551):241-5. 3.