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P15920 (VPP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
V-type proton ATPase 116 kDa subunit a isoform 2

Short name=V-ATPase 116 kDa isoform a2
Alternative name(s):
Immune suppressor factor J6B7
Short name=ISF
Lysosomal H(+)-transporting ATPase V0 subunit a2
ShIF
Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2
Gene names
Name:Atp6v0a2
Synonyms:Atp6n1b, Tj6
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length856 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part of the proton channel of V-ATPases By similarity. Essential component of the endosomal pH-sensing machinery. May play a role in maintaining the Golgi functions, such as glycosylation maturation, by controlling the Golgi pH. Ref.7

Subunit structure

The V-ATPase is a heteromultimeric enzyme composed of at least thirteen different subunits. It has a membrane peripheral V1 sector for ATP hydrolysis and an integral V0 for proton translocation. The V1 sector comprises subunits A-H, whereas V0 includes subunits a, d, c, c', and c''. Directly interacts with PSCD2 through its N-terminal cytosolic tail in an intra-endosomal acidification-dependent manner. Disruption of this interaction results in the inhibition of endocytosis. Ref.7

Subcellular location

Cell membrane; Multi-pass membrane protein. Endosome membrane. Note: In kidney proximal tubules, detected in subapical early endosomes. Ref.7

Tissue specificity

Relatively high expression in kidney and liver. Lower levels in the spleen, testis, and skeletal muscle. Also expressed in the thymus. Ref.6

Sequence similarities

Belongs to the V-ATPase 116 kDa subunit family.

Sequence caution

The sequence AAL57303.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Cyth2P630345EBI-988456,EBI-988425

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P15920-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P15920-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-593: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 856856V-type proton ATPase 116 kDa subunit a isoform 2
PRO_0000119217

Regions

Topological domain1 – 393393Cytoplasmic Potential
Transmembrane394 – 41219Helical; Potential
Topological domain413 – 4142Vacuolar Potential
Transmembrane415 – 43117Helical; Potential
Topological domain432 – 44514Cytoplasmic Potential
Transmembrane446 – 47530Helical; Potential
Topological domain476 – 54974Vacuolar Potential
Transmembrane550 – 56920Helical; Potential
Topological domain570 – 58718Cytoplasmic Potential
Transmembrane588 – 60821Helical; Potential
Topological domain609 – 65143Vacuolar Potential
Transmembrane652 – 67120Helical; Potential
Topological domain672 – 73968Cytoplasmic Potential
Transmembrane740 – 76425Helical; Potential
Topological domain765 – 78521Vacuolar Potential
Transmembrane786 – 82439Helical; Potential
Topological domain825 – 85632Cytoplasmic Potential

Amino acid modifications

Modified residue6951Phosphoserine Ref.8
Modified residue7001Phosphoserine Ref.8

Natural variations

Alternative sequence1 – 593593Missing in isoform 2.
VSP_032088

Experimental info

Sequence conflict4861S → C in AAA39336. Ref.1
Sequence conflict4861S → C in CAA38968. Ref.1
Sequence conflict7911Missing in AAA39336. Ref.1
Sequence conflict7911Missing in CAA38968. Ref.1

Secondary structure

... 856
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: 6A0D593F6F401E22

FASTA85698,145
        10         20         30         40         50         60 
MGSLFRSESM CLAQLFLQSG TAYECLSALG EKGLVQFRDL NQNVSSFQRK FVGEVKRCEE 

        70         80         90        100        110        120 
LERILVYLVQ EITRADIPLP EGEASPPAPP LKHVLEMQEQ LQKLEVELRE VTKNKEKLRK 

       130        140        150        160        170        180 
NLLELVEYTH MLRVTKTFLK RNVEFEPTYE EFPALENDSL LDYSCMQRLG AKLGFVSGLI 

       190        200        210        220        230        240 
QQGRVEAFER MLWRACKGYT IVTYAELDEC LEDPETGEVI KWYVFLISFW GEQIGHKVKK 

       250        260        270        280        290        300 
ICDCYHCHIY PYPNTAEERR EIQEGLNTRI QDLYTVLHKT EDYLRQVLCK AAESVCSRVV 

       310        320        330        340        350        360 
QVRKMKAIYH MLNMCSFDVT NKCLIAEVWC PEVDLPGLRR ALEEGSRESG ATIPSFMNTI 

       370        380        390        400        410        420 
PTKETPPTLI RTNKFTEGFQ NIVDAYGVGS YREVNPALFT IITFPFLFAV MFGDFGHGFV 

       430        440        450        460        470        480 
MFLFALLLVL NENHPRLSQS QEILRMFFDG RYILLLMGLF SVYTGLIYND CFSKSVNLFG 

       490        500        510        520        530        540 
SGWNVSAMYS SSHSPEEQRK MVLWNDSTIR HSRTLQLDPN IPGVFRGPYP FGIDPIWNLA 

       550        560        570        580        590        600 
TNRLTFLNSF KMKMSVILGI FHMTFGVVLG IFNHLHFRKK FNVYLVSVPE ILFMLCIFGY 

       610        620        630        640        650        660 
LIFMIIYKWL AYSAETSREA PSILIEFINM FLFPTSKTHG LYPGQAHVQR VLVALTVLAV 

       670        680        690        700        710        720 
PVLFLGKPLF LLWLHNGRNC FGMSRSGYTL VRKDSEEEVS LLGNQDIEEG NSRMEEGCRE 

       730        740        750        760        770        780 
VTCEEFNFGE ILMTQAIHSI EYCLGCISNT ASYLRLWALS LAHAQLSDVL WAMLMRVGLR 

       790        800        810        820        830        840 
VDTTYGVLLL LPVMAFFAVL TIFILLVMEG LSAFLHAIRL HWVEFQNKFY VGAGTKFVPF 

       850 
SFSLLSSKFS NDDSIA 

« Hide

Isoform 2 [UniParc].

Checksum: 0A1BDE2F82C0C02C
Show »

FASTA26329,740

References

« Hide 'large scale' references
[1]"Cloning of a cDNA for a T cell produced molecule with a putative immune regulatory role."
Lee C.-K., Ghoshal K., Beaman K.D.
Mol. Immunol. 27:1137-1144(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Three subunit a isoforms of mouse vacuolar H+-ATPase. Preferential expression of the a3 isoform during osteoclast differentiation."
Toyomura T., Oka T., Yamaguchi C., Wada Y., Futai M.
J. Biol. Chem. 275:8760-8765(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Molecular cloning and expression of three isoforms of the 100-kDa a subunit of the mouse vacuolar proton-translocating ATPase."
Nishi T., Forgac M.
J. Biol. Chem. 275:6824-6830(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain and Heart.
[4]"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. expand/collapse author list , 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] (ISOFORMS 1 AND 2).
Strain: NOD.
Tissue: Dendritic cell and Wolffian duct.
[5]"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] (ISOFORM 1).
Tissue: Mammary tumor.
[6]"A novel secreted form of immune suppressor factor with high homology to vacuolar ATPases identified by a forward genetic approach of functional screening based on cell proliferation."
Tulin E.E., Onoda N., Maeda M., Hasegawa M., Nosaka T., Nomura H., Asano S., Kitamura T.
J. Biol. Chem. 276:27519-27526(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 569-856, TISSUE SPECIFICITY.
[7]"V-ATPase interacts with ARNO and Arf6 in early endosomes and regulates the protein degradative pathway."
Hurtado-Lorenzo A., Skinner M., El Annan J., Futai M., Sun-Wada G.-H., Bourgoin S., Casanova J., Wildeman A., Bechoua S., Ausiello D.A., Brown D., Marshansky V.
Nat. Cell Biol. 8:124-136(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PSCD2.
[8]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695 AND SER-700, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31226 mRNA. Translation: AAA39336.1.
X55184 mRNA. Translation: CAA38968.1.
AB022323 mRNA. Translation: BAA93007.1.
AF218252 mRNA. Translation: AAF59921.1.
AK032909 mRNA. Translation: BAC28081.1.
AK155055 mRNA. Translation: BAE33017.1.
BC108991 mRNA. Translation: AAI08992.1.
BC108992 mRNA. Translation: AAI08993.1.
BC112905 mRNA. Translation: AAI12906.1.
AF388674 mRNA. Translation: AAL57303.1. Different initiation.
PIRJH0287.
RefSeqNP_035726.2. NM_011596.5.
UniGeneMm.1158.
Mm.392098.
Mm.490281.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LX4NMR-A1-17[»]
ProteinModelPortalP15920.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP15920. 1 interaction.

Protein family/group databases

TCDB3.A.2.2.6. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

PhosphoSiteP15920.

Proteomic databases

PaxDbP15920.
PRIDEP15920.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000037865; ENSMUSP00000039737; ENSMUSG00000038023. [P15920-1]
GeneID21871.
KEGGmmu:21871.
UCSCuc008zqn.1. mouse. [P15920-2]
uc029voo.1. mouse. [P15920-1]

Organism-specific databases

CTD23545.
MGIMGI:104855. Atp6v0a2.

Phylogenomic databases

eggNOGCOG1269.
GeneTreeENSGT00390000004941.
HOGENOMHOG000037059.
HOVERGENHBG014606.
InParanoidP15920.
KOK02154.
OMAEIMRMFF.
OrthoDBEOG74FF04.
PhylomeDBP15920.
TreeFamTF300346.

Gene expression databases

BgeeP15920.
CleanExMM_ATP6V0A2.
GenevestigatorP15920.

Family and domain databases

InterProIPR002490. V-ATPase_116kDa_su.
IPR026028. V-type_ATPase_116kDa_su_euka.
[Graphical view]
PANTHERPTHR11629. PTHR11629. 1 hit.
PfamPF01496. V_ATPase_I. 1 hit.
[Graphical view]
PIRSFPIRSF001293. ATP6V0A1. 1 hit.
ProtoNetSearch...

Other

NextBio301372.
PROP15920.
SOURCESearch...

Entry information

Entry nameVPP2_MOUSE
AccessionPrimary (citable) accession number: P15920
Secondary accession number(s): A4FU82 expand/collapse secondary AC list , Q3U2X3, Q8VHU0, Q9JHJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 11, 2001
Last modified: April 16, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot