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P21283

- VATC1_HUMAN

UniProt

P21283 - VATC1_HUMAN

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Protein

V-type proton ATPase subunit C 1

Gene
ATP6V1C1, ATP6C, ATP6D, VATC
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. hydrogen-exporting ATPase activity, phosphorylative mechanism Source: Ensembl
  2. protein binding Source: IntAct
  3. proton-transporting ATPase activity, rotational mechanism Source: ProtInc
  4. transporter activity Source: ProtInc

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: InterPro
  2. cellular iron ion homeostasis Source: Reactome
  3. insulin receptor signaling pathway Source: Reactome
  4. interaction with host Source: Reactome
  5. phagosome maturation Source: Reactome
  6. proton transport Source: ProtInc
  7. transferrin transport Source: Reactome
  8. transmembrane transport Source: Reactome
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.

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
Synonyms:ATP6C, ATP6D, VATC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:856. ATP6V1C1.

Subcellular locationi

GO - Cellular componenti

  1. apical part of cell Source: Ensembl
  2. cytoplasmic vesicle Source: Ensembl
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
  5. lysosomal membrane Source: UniProtKB
  6. plasma membrane Source: UniProtKB
  7. proton-transporting two-sector ATPase complex Source: ProtInc
  8. proton-transporting V-type ATPase, V1 domain Source: InterPro
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25156.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
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

ArrayExpressiP21283.
BgeeiP21283.
CleanExiHS_ATP6V1C1.
GenevestigatoriP21283.

Organism-specific databases

HPAiHPA023943.
HPA024243.

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. 44 interactions.
IntActiP21283. 4 interactions.
STRINGi9606.ENSP00000379203.

Structurei

3D structure databases

ProteinModelPortaliP21283.
SMRiP21283. Positions 7-346.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5127.
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

MTEFWLISAP GEKTCQQTWE KLHAATSKNN NLAVTSKFNI PDLKVGTLDV    50
LVGLSDELAK LDAFVEGVVK KVAQYMADVL EDSKDKVQEN LLANGVDLVT 100
YITRFQWDMA KYPIKQSLKN ISEIIAKGVT QIDNDLKSRA SAYNNLKGNL 150
QNLERKNAGS LLTRSLAEIV KKDDFVLDSE YLVTLLVVVP KLNHNDWIKQ 200
YETLAEMVVP RSSNVLSEDQ DSYLCNVTLF RKAVDDFRHK ARENKFIVRD 250
FQYNEEEMKA DKEEMNRLST DKKKQFGPLV RWLKVNFSEA FIAWIHVKAL 300
RVFVESVLRY GLPVNFQAML LQPNKKTLKK LREVLHELYK HLDSSAAAII 350
DAPMDIPGLN LSQQEYYPYV YYKIDCNLLE FK 382
Length:382
Mass (Da):43,942
Last modified:January 23, 2007 - v4
Checksum:i5626E2AB2BD66BA7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi401329.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X69151 mRNA. Translation: CAA48903.1 .
AF363578 Genomic DNA. Translation: AAL50383.1 .
BC010960 mRNA. Translation: AAH10960.1 .
J05682 mRNA. Translation: AAA36803.1 .
CCDSi CCDS6296.1.
PIRi JN0907.
RefSeqi NP_001686.1. NM_001695.4.
UniGenei Hs.86905.

3D structure databases

ProteinModelPortali P21283.
SMRi P21283. Positions 7-346.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107011. 44 interactions.
IntActi P21283. 4 interactions.
STRINGi 9606.ENSP00000379203.

Protein family/group databases

TCDBi 3.A.2.2.4. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

PhosphoSitei P21283.

Polymorphism databases

DMDMi 401329.

Proteomic databases

MaxQBi P21283.
PaxDbi P21283.
PRIDEi P21283.

Protocols and materials databases

DNASUi 528.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000395862 ; ENSP00000379203 ; ENSG00000155097 .
ENST00000518738 ; ENSP00000430282 ; ENSG00000155097 .
GeneIDi 528.
KEGGi hsa:528.
UCSCi uc003ykz.4. human.

Organism-specific databases

CTDi 528.
GeneCardsi GC08P104033.
HGNCi HGNC:856. ATP6V1C1.
HPAi HPA023943.
HPA024243.
MIMi 603097. gene.
neXtProti NX_P21283.
PharmGKBi PA25156.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5127.
HOGENOMi HOG000207528.
HOVERGENi HBG002470.
InParanoidi P21283.
KOi K02148.
OMAi QRQYAPL.
OrthoDBi EOG7QNVKX.
PhylomeDBi P21283.
TreeFami TF314912.

Enzyme and pathway databases

BioCyci MetaCyc:HS08030-MONOMER.
Reactomei REACT_1109. Insulin receptor recycling.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_25283. Transferrin endocytosis and recycling.

Miscellaneous databases

ChiTaRSi ATP6V1C1. human.
GeneWikii ATP6V1C1.
GenomeRNAii 528.
NextBioi 2193.
PROi P21283.
SOURCEi Search...

Gene expression databases

ArrayExpressi P21283.
Bgeei P21283.
CleanExi HS_ATP6V1C1.
Genevestigatori P21283.

Family and domain databases

InterProi IPR004907. ATPase_V1-cplx_csu.
[Graphical view ]
PANTHERi PTHR10137. PTHR10137. 1 hit.
Pfami PF03223. V-ATPase_C. 1 hit.
[Graphical view ]
ProtoNeti Search...

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].

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: September 3, 2014
This is version 140 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

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