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Protein

V-type proton ATPase subunit C 1

Gene

ATP6V1C1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Subunit of the peripheral V1 complex of vacuolar ATPase. 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. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-BTA-77387. Insulin receptor recycling.
R-BTA-917977. Transferrin endocytosis and recycling.
R-BTA-983712. Ion channel transport.

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase subunit C 1
Short name:
V-ATPase subunit C 1
Alternative name(s):
Vacuolar proton pump subunit C 1
Gene namesi
Name:ATP6V1C1
Synonyms:ATP6C, VATC
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 14

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 382381V-type proton ATPase subunit C 1PRO_0000209347Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP21282.
PRIDEiP21282.

Interactioni

Subunit structurei

V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d).

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000017968.

Structurei

3D structure databases

ProteinModelPortaliP21282.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase C subunit family.Curated

Phylogenomic databases

eggNOGiKOG2909. Eukaryota.
COG5127. LUCA.
GeneTreeiENSGT00390000004263.
HOGENOMiHOG000207528.
HOVERGENiHBG002470.
InParanoidiP21282.
KOiK02148.
OMAiFKINIDF.
OrthoDBiEOG7QNVKX.
TreeFamiTF314912.

Family and domain databases

InterProiIPR004907. ATPase_V1-cplx_csu.
[Graphical view]
PANTHERiPTHR10137. PTHR10137. 1 hit.
PfamiPF03223. V-ATPase_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21282-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEFWLISAP GEKTCQQTWE KLHAATTKNN NLAVSSKFNI PDLKVGTLDV
60 70 80 90 100
LVGLSDELAK LDAFVEGVVK KVAQYMADVL EDSKDKVQEN LLANGVDLVT
110 120 130 140 150
YITRFQWDMA KYPIKQSLKN ISEIIAKGVT QIDNDLKSRA SAYNNLKGNL
160 170 180 190 200
QNLERKNAGS LLTRSLAEIV KKDDFVLDSE YLVTLLVVVP KLNHNDWIKQ
210 220 230 240 250
YETLAEMVVP RSSNVLSEDQ DSYLCNVTLF RKAVDDFRHK ARENKFIVRD
260 270 280 290 300
FQYNEEEMKA DKEEMNRLST DKKKQFGPLV RWLKVNFSEA FIAWIHVKAL
310 320 330 340 350
RVFVESVLRY GLPVNFQAML LQPNKKTMKK LREVLYELYK HLDSSAAAII
360 370 380
DAPMDIPGLN LSQQEYYPYV YYKIDCNLLE FK
Length:382
Mass (Da):43,986
Last modified:January 23, 2007 - v3
Checksum:i122FECB9F8A8AC9C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05681 mRNA. Translation: AAA30803.1.
BC119957 mRNA. Translation: AAI19958.1.
PIRiA23671.
RefSeqiNP_788849.1. NM_176676.1.
UniGeneiBt.52307.

Genome annotation databases

EnsembliENSBTAT00000017968; ENSBTAP00000017968; ENSBTAG00000013513.
GeneIDi338089.
KEGGibta:338089.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05681 mRNA. Translation: AAA30803.1.
BC119957 mRNA. Translation: AAI19958.1.
PIRiA23671.
RefSeqiNP_788849.1. NM_176676.1.
UniGeneiBt.52307.

3D structure databases

ProteinModelPortaliP21282.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000017968.

Proteomic databases

PaxDbiP21282.
PRIDEiP21282.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000017968; ENSBTAP00000017968; ENSBTAG00000013513.
GeneIDi338089.
KEGGibta:338089.

Organism-specific databases

CTDi528.

Phylogenomic databases

eggNOGiKOG2909. Eukaryota.
COG5127. LUCA.
GeneTreeiENSGT00390000004263.
HOGENOMiHOG000207528.
HOVERGENiHBG002470.
InParanoidiP21282.
KOiK02148.
OMAiFKINIDF.
OrthoDBiEOG7QNVKX.
TreeFamiTF314912.

Enzyme and pathway databases

ReactomeiR-BTA-77387. Insulin receptor recycling.
R-BTA-917977. Transferrin endocytosis and recycling.
R-BTA-983712. Ion channel transport.

Miscellaneous databases

NextBioi20812536.

Family and domain databases

InterProiIPR004907. ATPase_V1-cplx_csu.
[Graphical view]
PANTHERiPTHR10137. PTHR10137. 1 hit.
PfamiPF03223. V-ATPase_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of cDNA encoding the C subunit of H(+)-ATPase from bovine chromaffin granules."
    Nelson H., Mandiyan S., Noumi T., Moriyama Y., Miedel M.C., Nelson N.
    J. Biol. Chem. 265:20390-20393(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Chromaffin cell.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal muscle.

Entry informationi

Entry nameiVATC1_BOVIN
AccessioniPrimary (citable) accession number: P21282
Secondary accession number(s): Q0VCX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: December 9, 2015
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.