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Protein

V-type proton ATPase subunit C 1

Gene

Atp6v1c1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

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

Protein family/group databases

TCDBi3.A.2.2.6. 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, Atp6c1, Vatc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1913585. Atp6v1c1.

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_0000209349Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9Z1G3.
MaxQBiQ9Z1G3.
PaxDbiQ9Z1G3.
PRIDEiQ9Z1G3.

PTM databases

iPTMnetiQ9Z1G3.
PhosphoSiteiQ9Z1G3.

Expressioni

Tissue specificityi

Ubiquitous. Abundant in brain, liver, kidney and testis.1 Publication

Gene expression databases

BgeeiQ9Z1G3.
CleanExiMM_ATP6V1C1.
GenevisibleiQ9Z1G3. MM.

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

BioGridi211393. 1 interaction.
IntActiQ9Z1G3. 5 interactions.
STRINGi10090.ENSMUSP00000022904.

Structurei

3D structure databases

ProteinModelPortaliQ9Z1G3.
SMRiQ9Z1G3. Positions 7-346.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase C subunit family.Curated

Phylogenomic databases

eggNOGiKOG2909. Eukaryota.
COG5127. LUCA.
GeneTreeiENSGT00390000004263.
HOGENOMiHOG000207528.
HOVERGENiHBG002470.
InParanoidiQ9Z1G3.
KOiK02148.
OMAiFKINIDF.
OrthoDBiEOG7QNVKX.
PhylomeDBiQ9Z1G3.
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.

Q9Z1G3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEFWLISAP GEKTCQQTWE KLHAATTKNN NLAVSSKFNI PDLKVGTLDV
60 70 80 90 100
LVGLSDELAK LDAFVEGVVK KVAQYMADVL EDSKDKVQEN LLASGVDLVT
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 DKEEMTRLST DKKKQFGPLV RWLKVNFSEA FIAWIHIKAL
310 320 330 340 350
RVFVESVLRY GLPVNFQAML LQPNKKSVKK LREVLHELYK HLDSSAAAII
360 370 380
DAPMDIPGLN LSQQEYYPYV YYKIDCNLLE FK
Length:382
Mass (Da):43,888
Last modified:May 1, 2007 - v4
Checksum:i6D1851D8C81DF98F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti267 – 2671R → E in AAC83084 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB088407 mRNA. Translation: BAC57953.1.
U13839 mRNA. Translation: AAC83084.1.
AK075779 mRNA. Translation: BAC35953.1.
AK151237 mRNA. Translation: BAE30229.1.
BC010217 mRNA. Translation: AAH10217.1.
CCDSiCCDS27439.1.
RefSeqiNP_079770.2. NM_025494.3.
UniGeneiMm.276618.

Genome annotation databases

EnsembliENSMUST00000022904; ENSMUSP00000022904; ENSMUSG00000022295.
GeneIDi66335.
KEGGimmu:66335.
UCSCiuc007vnv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB088407 mRNA. Translation: BAC57953.1.
U13839 mRNA. Translation: AAC83084.1.
AK075779 mRNA. Translation: BAC35953.1.
AK151237 mRNA. Translation: BAE30229.1.
BC010217 mRNA. Translation: AAH10217.1.
CCDSiCCDS27439.1.
RefSeqiNP_079770.2. NM_025494.3.
UniGeneiMm.276618.

3D structure databases

ProteinModelPortaliQ9Z1G3.
SMRiQ9Z1G3. Positions 7-346.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211393. 1 interaction.
IntActiQ9Z1G3. 5 interactions.
STRINGi10090.ENSMUSP00000022904.

Protein family/group databases

TCDBi3.A.2.2.6. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

iPTMnetiQ9Z1G3.
PhosphoSiteiQ9Z1G3.

Proteomic databases

EPDiQ9Z1G3.
MaxQBiQ9Z1G3.
PaxDbiQ9Z1G3.
PRIDEiQ9Z1G3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022904; ENSMUSP00000022904; ENSMUSG00000022295.
GeneIDi66335.
KEGGimmu:66335.
UCSCiuc007vnv.2. mouse.

Organism-specific databases

CTDi528.
MGIiMGI:1913585. Atp6v1c1.

Phylogenomic databases

eggNOGiKOG2909. Eukaryota.
COG5127. LUCA.
GeneTreeiENSGT00390000004263.
HOGENOMiHOG000207528.
HOVERGENiHBG002470.
InParanoidiQ9Z1G3.
KOiK02148.
OMAiFKINIDF.
OrthoDBiEOG7QNVKX.
PhylomeDBiQ9Z1G3.
TreeFamiTF314912.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiAtp6v1c1. mouse.
NextBioi321359.
PROiQ9Z1G3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z1G3.
CleanExiMM_ATP6V1C1.
GenevisibleiQ9Z1G3. MM.

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. "Diversity of mouse proton-translocating ATPase: presence of multiple isoforms of the C, d and G subunits."
    Sun-Wada G.-H., Yoshimizu T., Imai-Senga Y., Wada Y., Futai M.
    Gene 302:147-153(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "cDNA sequences for mouse vacuolar ATPase subunits."
    Howell M.L., Dean G.E.
    Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow and Pancreas.
  4. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  5. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 38-111; 120-137; 148-155; 200-231; 275-281; 310-326 AND 374-382, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiVATC1_MOUSE
AccessioniPrimary (citable) accession number: Q9Z1G3
Secondary accession number(s): Q91Z42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 2007
Last modified: March 16, 2016
This is version 129 of the entry and version 4 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.