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Protein

V-type proton ATPase subunit S1

Gene

Atp6ap1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.By similarity

GO - Molecular functioni

GO - Biological processi

  • ATP hydrolysis coupled proton transport Source: InterPro
  • establishment of organelle localization Source: UniProtKB
  • pH reduction Source: UniProtKB
  • positive regulation of bone resorption Source: UniProtKB
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of exocytosis Source: UniProtKB
  • positive regulation of osteoblast differentiation Source: UniProtKB
  • positive regulation of osteoclast development Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase subunit S1
Short name:
V-ATPase subunit S1
Alternative name(s):
Protein C7-1
V-ATPase Ac45 subunit
V-ATPase S1 accessory protein
Vacuolar proton pump subunit S1
Gene namesi
Name:Atp6ap1
Synonyms:Atp6ip1, Atp6s1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:109629. Atp6ap1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini33 – 412380VacuolarSequence analysisAdd
BLAST
Transmembranei413 – 43321HelicalSequence analysisAdd
BLAST
Topological domaini434 – 46330CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Sequence analysisAdd
BLAST
Chaini33 – 463431V-type proton ATPase subunit S1PRO_0000002544Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi164 – 1641N-linked (GlcNAc...)Sequence analysis
Glycosylationi255 – 2551N-linked (GlcNAc...)1 Publication
Glycosylationi267 – 2671N-linked (GlcNAc...)Sequence analysis
Glycosylationi290 – 2901N-linked (GlcNAc...)Sequence analysis
Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence analysis
Glycosylationi344 – 3441N-linked (GlcNAc...)Sequence analysis
Glycosylationi351 – 3511N-linked (GlcNAc...)Sequence analysis
Glycosylationi399 – 3991N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ9R1Q9.
MaxQBiQ9R1Q9.
PaxDbiQ9R1Q9.
PeptideAtlasiQ9R1Q9.
PRIDEiQ9R1Q9.

PTM databases

iPTMnetiQ9R1Q9.
PhosphoSiteiQ9R1Q9.

Expressioni

Gene expression databases

BgeeiQ9R1Q9.
ExpressionAtlasiQ9R1Q9. baseline and differential.
GenevisibleiQ9R1Q9. MM.

Interactioni

Subunit structurei

Composed of at least 10 subunits.

GO - Molecular functioni

  • Rab GTPase binding Source: UniProtKB

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000019231.

Structurei

3D structure databases

ProteinModelPortaliQ9R1Q9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the vacuolar ATPase subunit S1 family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3868. Eukaryota.
ENOG410XTHY. LUCA.
GeneTreeiENSGT00530000063584.
HOVERGENiHBG001090.
InParanoidiQ9R1Q9.
KOiK03662.
OMAiGHITSDM.
OrthoDBiEOG75TMBV.
TreeFamiTF325819.

Family and domain databases

InterProiIPR008388. ATPase_V1-cplx_s1su.
IPR024722. ATPase_V1_suS1_fam.
[Graphical view]
PANTHERiPTHR12471. PTHR12471. 1 hit.
PfamiPF05827. ATP-synt_S1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9R1Q9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMAATVVSRI RTGTGRAPVM WLSLSLVAVA AAVATEQQVP LVLWSSDRNL
60 70 80 90 100
WAPVADTHEG HITSDMQLST YLDPALELGP RNVLLFLQDK LSIEDFTAYG
110 120 130 140 150
GVFGNKQDSA FSNLENALDL APSSLVLPAV DWYAISTLTT YLQEKLGASP
160 170 180 190 200
LHVDLATLKE LKLNASLPAL LLIRLPYTAS SGLMAPREVL TGNDEVIGQV
210 220 230 240 250
LSTLKSEDVP YTAALTAVRP SRVARDITMV AGGLGRQLLQ TQVASPAIHP
260 270 280 290 300
PVSYNDTAPR ILFWAQNFSV AYKDEWKDLT SLTFGVENLN LTGSFWNDSF
310 320 330 340 350
AMLSLTYEPL FGATVTFKFI LASRFYPVSA RYWFAMERLE IHSNGSVAHF
360 370 380 390 400
NVSQVTGPSI YSFHCEYVSS VSKKGNLLVT NVPSVWQMTL HNFQIQAFNV
410 420 430 440 450
TGEQFSYASD CAGFFSPGIW MGLLTTLFML FIFTYGLHMI LSLKTMDRFD
460
DHKGPTITLT QIV
Length:463
Mass (Da):51,008
Last modified:May 1, 2000 - v1
Checksum:iAE28D99718BA0AC0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB031290 mRNA. Translation: BAA83498.1.
BC048241 mRNA. Translation: AAH48241.1.
CCDSiCCDS30226.1.
RefSeqiNP_061264.1. NM_018794.4.
UniGeneiMm.21961.

Genome annotation databases

EnsembliENSMUST00000019231; ENSMUSP00000019231; ENSMUSG00000019087.
GeneIDi54411.
KEGGimmu:54411.
UCSCiuc009tol.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB031290 mRNA. Translation: BAA83498.1.
BC048241 mRNA. Translation: AAH48241.1.
CCDSiCCDS30226.1.
RefSeqiNP_061264.1. NM_018794.4.
UniGeneiMm.21961.

3D structure databases

ProteinModelPortaliQ9R1Q9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000019231.

PTM databases

iPTMnetiQ9R1Q9.
PhosphoSiteiQ9R1Q9.

Proteomic databases

EPDiQ9R1Q9.
MaxQBiQ9R1Q9.
PaxDbiQ9R1Q9.
PeptideAtlasiQ9R1Q9.
PRIDEiQ9R1Q9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019231; ENSMUSP00000019231; ENSMUSG00000019087.
GeneIDi54411.
KEGGimmu:54411.
UCSCiuc009tol.2. mouse.

Organism-specific databases

CTDi537.
MGIiMGI:109629. Atp6ap1.

Phylogenomic databases

eggNOGiKOG3868. Eukaryota.
ENOG410XTHY. LUCA.
GeneTreeiENSGT00530000063584.
HOVERGENiHBG001090.
InParanoidiQ9R1Q9.
KOiK03662.
OMAiGHITSDM.
OrthoDBiEOG75TMBV.
TreeFamiTF325819.

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

ChiTaRSiAtp6ap1. mouse.
PROiQ9R1Q9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9R1Q9.
ExpressionAtlasiQ9R1Q9. baseline and differential.
GenevisibleiQ9R1Q9. MM.

Family and domain databases

InterProiIPR008388. ATPase_V1-cplx_s1su.
IPR024722. ATPase_V1_suS1_fam.
[Graphical view]
PANTHERiPTHR12471. PTHR12471. 1 hit.
PfamiPF05827. ATP-synt_S1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Hayashi A., Hattori A., Okaze H., Kozuma S., Seki N., Saito T.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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: Retina.
  3. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 325-338 AND 454-463, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  4. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-255.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Testis.

Entry informationi

Entry nameiVAS1_MOUSE
AccessioniPrimary (citable) accession number: Q9R1Q9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 132 of the entry and version 1 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.