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Protein

V-type proton ATPase subunit C 1

Gene

ATP6V1C1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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

  • hydrogen-exporting ATPase activity, phosphorylative mechanism Source: Ensembl
  • proton-transporting ATPase activity, rotational mechanism Source: ProtInc
  • transporter activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciMetaCyc:HS08030-MONOMER.
ReactomeiREACT_1109. Insulin receptor recycling.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_25283. Transferrin endocytosis and recycling.
REACT_25300. Ion channel transport.

Protein family/group databases

TCDBi3.A.2.2.4. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

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, ATP6D, VATC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:856. ATP6V1C1.

Subcellular locationi

GO - Cellular componenti

  • apical part of cell Source: Ensembl
  • cytoplasmic vesicle Source: Ensembl
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • lysosomal membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • proton-transporting two-sector ATPase complex Source: ProtInc
  • proton-transporting V-type ATPase, V1 domain Source: InterPro
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25156.

Polymorphism and mutation databases

BioMutaiATP6V1C1.
DMDMi401329.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 382381V-type proton ATPase subunit C 1PRO_0000209348Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP21283.
PaxDbiP21283.
PRIDEiP21283.

PTM databases

PhosphoSiteiP21283.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiP21283.
CleanExiHS_ATP6V1C1.
ExpressionAtlasiP21283. baseline and differential.
GenevisibleiP21283. HS.

Organism-specific databases

HPAiHPA023943.
HPA057297.

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).

Binary interactionsi

WithEntry#Exp.IntActNotes
ARF6P623304EBI-988663,EBI-638181

Protein-protein interaction databases

BioGridi107011. 51 interactions.
IntActiP21283. 4 interactions.
STRINGi9606.ENSP00000379203.

Structurei

3D structure databases

ProteinModelPortaliP21283.
SMRiP21283. Positions 7-346.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase C subunit family.Curated

Phylogenomic databases

eggNOGiCOG5127.
GeneTreeiENSGT00390000004263.
HOGENOMiHOG000207528.
HOVERGENiHBG002470.
InParanoidiP21283.
KOiK02148.
OMAiQRQYAPL.
OrthoDBiEOG7QNVKX.
PhylomeDBiP21283.
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.

P21283-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEFWLISAP GEKTCQQTWE KLHAATSKNN NLAVTSKFNI 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 LQPNKKTLKK LREVLHELYK HLDSSAAAII
360 370 380
DAPMDIPGLN LSQQEYYPYV YYKIDCNLLE FK
Length:382
Mass (Da):43,942
Last modified:January 23, 2007 - v4
Checksum:i5626E2AB2BD66BA7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69151 mRNA. Translation: CAA48903.1.
AF363578 Genomic DNA. Translation: AAL50383.1.
BC010960 mRNA. Translation: AAH10960.1.
J05682 mRNA. Translation: AAA36803.1.
CCDSiCCDS6296.1.
PIRiJN0907.
RefSeqiNP_001686.1. NM_001695.4.
UniGeneiHs.86905.

Genome annotation databases

EnsembliENST00000395862; ENSP00000379203; ENSG00000155097.
ENST00000518738; ENSP00000430282; ENSG00000155097.
GeneIDi528.
KEGGihsa:528.
UCSCiuc003ykz.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69151 mRNA. Translation: CAA48903.1.
AF363578 Genomic DNA. Translation: AAL50383.1.
BC010960 mRNA. Translation: AAH10960.1.
J05682 mRNA. Translation: AAA36803.1.
CCDSiCCDS6296.1.
PIRiJN0907.
RefSeqiNP_001686.1. NM_001695.4.
UniGeneiHs.86905.

3D structure databases

ProteinModelPortaliP21283.
SMRiP21283. Positions 7-346.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107011. 51 interactions.
IntActiP21283. 4 interactions.
STRINGi9606.ENSP00000379203.

Protein family/group databases

TCDBi3.A.2.2.4. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

PhosphoSiteiP21283.

Polymorphism and mutation databases

BioMutaiATP6V1C1.
DMDMi401329.

Proteomic databases

MaxQBiP21283.
PaxDbiP21283.
PRIDEiP21283.

Protocols and materials databases

DNASUi528.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000395862; ENSP00000379203; ENSG00000155097.
ENST00000518738; ENSP00000430282; ENSG00000155097.
GeneIDi528.
KEGGihsa:528.
UCSCiuc003ykz.4. human.

Organism-specific databases

CTDi528.
GeneCardsiGC08P104033.
HGNCiHGNC:856. ATP6V1C1.
HPAiHPA023943.
HPA057297.
MIMi603097. gene.
neXtProtiNX_P21283.
PharmGKBiPA25156.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5127.
GeneTreeiENSGT00390000004263.
HOGENOMiHOG000207528.
HOVERGENiHBG002470.
InParanoidiP21283.
KOiK02148.
OMAiQRQYAPL.
OrthoDBiEOG7QNVKX.
PhylomeDBiP21283.
TreeFamiTF314912.

Enzyme and pathway databases

BioCyciMetaCyc:HS08030-MONOMER.
ReactomeiREACT_1109. Insulin receptor recycling.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_25283. Transferrin endocytosis and recycling.
REACT_25300. Ion channel transport.

Miscellaneous databases

ChiTaRSiATP6V1C1. human.
GeneWikiiATP6V1C1.
GenomeRNAii528.
NextBioi2193.
PROiP21283.
SOURCEiSearch...

Gene expression databases

BgeeiP21283.
CleanExiHS_ATP6V1C1.
ExpressionAtlasiP21283. baseline and differential.
GenevisibleiP21283. HS.

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. "Cloning and tissue distribution of subunits C, D, and E of the human vacuolar H(+)-ATPase."
    van Hille B., Vanek M., Richener H., Green J.R., Bilbe G.
    Biochem. Biophys. Res. Commun. 197:15-21(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Osteoclastoma.
  2. "BAALC, the human member of a novel mammalian neuroectoderm gene lineage, is implicated in hematopoiesis and acute leukemia."
    Tanner S.M., Austin J.L., Leone G., Rush L.J., Plass C., Heinonen K., Mrozek K., Sill H., Knuutila S., Kolitz J.E., Archer K.J., Caligiuri M.A., Bloomfield C.D., de La Chapelle A.
    Proc. Natl. Acad. Sci. U.S.A. 98:13901-13906(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow.
  4. Kanor S., Bienvenut W.V., Quadroni M.
    Submitted (DEC-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13; 45-60 AND 200-211, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Melanoma.
  5. "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] OF 36-382.
    Tissue: Brain.
  6. "Molecular cloning and characterization of novel tissue-specific isoforms of the human vacuolar H(+)-ATPase C, G and d subunits, and their evaluation in autosomal recessive distal renal tubular acidosis."
    Smith A.N., Borthwick K.J., Karet F.E.
    Gene 297:169-177(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiVATC1_HUMAN
AccessioniPrimary (citable) accession number: P21283
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 148 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.