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P15920

- VPP2_MOUSE

UniProt

P15920 - VPP2_MOUSE

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Protein

V-type proton ATPase 116 kDa subunit a isoform 2

Gene

Atp6v0a2

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

Functioni

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.By similarity1 Publication

GO - Molecular functioni

  1. hydrogen ion transmembrane transporter activity Source: InterPro

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_198345. Phagosomal maturation (early endosomal stage).
REACT_198515. Transferrin endocytosis and recycling.

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 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 namesi
Name:Atp6v0a2
Synonyms:Atp6n1b, Tj6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:104855. Atp6v0a2.

Subcellular locationi

Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication. Endosome membrane 1 Publication
Note: In kidney proximal tubules, detected in subapical early endosomes.

GO - Cellular componenti

  1. acrosomal vesicle Source: MGI
  2. endosome Source: UniProtKB-KW
  3. integral component of membrane Source: UniProtKB-KW
  4. lysosomal membrane Source: Ensembl
  5. plasma membrane Source: UniProtKB-KW
  6. vacuolar proton-transporting V-type ATPase, V0 domain Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 856856V-type proton ATPase 116 kDa subunit a isoform 2PRO_0000119217Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei695 – 6951Phosphoserine1 Publication
Modified residuei700 – 7001Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP15920.
PaxDbiP15920.
PRIDEiP15920.

PTM databases

PhosphoSiteiP15920.

Expressioni

Tissue specificityi

Relatively high expression in kidney and liver. Lower levels in the spleen, testis, and skeletal muscle. Also expressed in the thymus.1 Publication

Gene expression databases

BgeeiP15920.
CleanExiMM_ATP6V0A2.
GenevestigatoriP15920.

Interactioni

Subunit structurei

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Cyth2P630345EBI-988456,EBI-988425

Protein-protein interaction databases

IntActiP15920. 1 interaction.

Structurei

Secondary structure

1
856
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1613

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LX4NMR-A1-17[»]
ProteinModelPortaliP15920.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 393393CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini413 – 4142VacuolarSequence Analysis
Topological domaini432 – 44514CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini476 – 54974VacuolarSequence AnalysisAdd
BLAST
Topological domaini570 – 58718CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini609 – 65143VacuolarSequence AnalysisAdd
BLAST
Topological domaini672 – 73968CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini765 – 78521VacuolarSequence AnalysisAdd
BLAST
Topological domaini825 – 85632CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei394 – 41219HelicalSequence AnalysisAdd
BLAST
Transmembranei415 – 43117HelicalSequence AnalysisAdd
BLAST
Transmembranei446 – 47530HelicalSequence AnalysisAdd
BLAST
Transmembranei550 – 56920HelicalSequence AnalysisAdd
BLAST
Transmembranei588 – 60821HelicalSequence AnalysisAdd
BLAST
Transmembranei652 – 67120HelicalSequence AnalysisAdd
BLAST
Transmembranei740 – 76425HelicalSequence AnalysisAdd
BLAST
Transmembranei786 – 82439HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase 116 kDa subunit family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1269.
GeneTreeiENSGT00390000004941.
HOGENOMiHOG000037059.
HOVERGENiHBG014606.
InParanoidiP15920.
KOiK02154.
OMAiEIMRMFF.
OrthoDBiEOG74FF04.
PhylomeDBiP15920.
TreeFamiTF300346.

Family and domain databases

InterProiIPR002490. V-ATPase_116kDa_su.
IPR026028. V-type_ATPase_116kDa_su_euka.
[Graphical view]
PANTHERiPTHR11629. PTHR11629. 1 hit.
PfamiPF01496. V_ATPase_I. 1 hit.
[Graphical view]
PIRSFiPIRSF001293. ATP6V0A1. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P15920-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGSLFRSESM CLAQLFLQSG TAYECLSALG EKGLVQFRDL NQNVSSFQRK
60 70 80 90 100
FVGEVKRCEE LERILVYLVQ EITRADIPLP EGEASPPAPP LKHVLEMQEQ
110 120 130 140 150
LQKLEVELRE VTKNKEKLRK NLLELVEYTH MLRVTKTFLK RNVEFEPTYE
160 170 180 190 200
EFPALENDSL LDYSCMQRLG AKLGFVSGLI QQGRVEAFER MLWRACKGYT
210 220 230 240 250
IVTYAELDEC LEDPETGEVI KWYVFLISFW GEQIGHKVKK ICDCYHCHIY
260 270 280 290 300
PYPNTAEERR EIQEGLNTRI QDLYTVLHKT EDYLRQVLCK AAESVCSRVV
310 320 330 340 350
QVRKMKAIYH MLNMCSFDVT NKCLIAEVWC PEVDLPGLRR ALEEGSRESG
360 370 380 390 400
ATIPSFMNTI PTKETPPTLI RTNKFTEGFQ NIVDAYGVGS YREVNPALFT
410 420 430 440 450
IITFPFLFAV MFGDFGHGFV MFLFALLLVL NENHPRLSQS QEILRMFFDG
460 470 480 490 500
RYILLLMGLF SVYTGLIYND CFSKSVNLFG SGWNVSAMYS SSHSPEEQRK
510 520 530 540 550
MVLWNDSTIR HSRTLQLDPN IPGVFRGPYP FGIDPIWNLA TNRLTFLNSF
560 570 580 590 600
KMKMSVILGI FHMTFGVVLG IFNHLHFRKK FNVYLVSVPE ILFMLCIFGY
610 620 630 640 650
LIFMIIYKWL AYSAETSREA PSILIEFINM FLFPTSKTHG LYPGQAHVQR
660 670 680 690 700
VLVALTVLAV PVLFLGKPLF LLWLHNGRNC FGMSRSGYTL VRKDSEEEVS
710 720 730 740 750
LLGNQDIEEG NSRMEEGCRE VTCEEFNFGE ILMTQAIHSI EYCLGCISNT
760 770 780 790 800
ASYLRLWALS LAHAQLSDVL WAMLMRVGLR VDTTYGVLLL LPVMAFFAVL
810 820 830 840 850
TIFILLVMEG LSAFLHAIRL HWVEFQNKFY VGAGTKFVPF SFSLLSSKFS

NDDSIA
Length:856
Mass (Da):98,145
Last modified:January 11, 2001 - v2
Checksum:i6A0D593F6F401E22
GO
Isoform 2 (identifier: P15920-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-593: Missing.

Note: No experimental confirmation available.

Show »
Length:263
Mass (Da):29,740
Checksum:i0A1BDE2F82C0C02C
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti486 – 4861S → C in AAA39336. (PubMed:2247090)Curated
Sequence conflicti486 – 4861S → C in CAA38968. (PubMed:2247090)Curated
Sequence conflicti791 – 7911Missing in AAA39336. (PubMed:2247090)Curated
Sequence conflicti791 – 7911Missing in CAA38968. (PubMed:2247090)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 593593Missing in isoform 2. 1 PublicationVSP_032088Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiJH0287.
RefSeqiNP_035726.2. NM_011596.5. [P15920-1]
UniGeneiMm.1158.
Mm.392098.
Mm.490281.

Genome annotation databases

EnsembliENSMUST00000037865; ENSMUSP00000039737; ENSMUSG00000038023. [P15920-1]
GeneIDi21871.
KEGGimmu:21871.
UCSCiuc008zqn.1. mouse. [P15920-2]
uc029voo.1. mouse. [P15920-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRi JH0287.
RefSeqi NP_035726.2. NM_011596.5. [P15920-1 ]
UniGenei Mm.1158.
Mm.392098.
Mm.490281.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LX4 NMR - A 1-17 [» ]
ProteinModelPortali P15920.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P15920. 1 interaction.

Protein family/group databases

TCDBi 3.A.2.2.6. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

PhosphoSitei P15920.

Proteomic databases

MaxQBi P15920.
PaxDbi P15920.
PRIDEi P15920.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000037865 ; ENSMUSP00000039737 ; ENSMUSG00000038023 . [P15920-1 ]
GeneIDi 21871.
KEGGi mmu:21871.
UCSCi uc008zqn.1. mouse. [P15920-2 ]
uc029voo.1. mouse. [P15920-1 ]

Organism-specific databases

CTDi 23545.
MGIi MGI:104855. Atp6v0a2.

Phylogenomic databases

eggNOGi COG1269.
GeneTreei ENSGT00390000004941.
HOGENOMi HOG000037059.
HOVERGENi HBG014606.
InParanoidi P15920.
KOi K02154.
OMAi EIMRMFF.
OrthoDBi EOG74FF04.
PhylomeDBi P15920.
TreeFami TF300346.

Enzyme and pathway databases

Reactomei REACT_198345. Phagosomal maturation (early endosomal stage).
REACT_198515. Transferrin endocytosis and recycling.

Miscellaneous databases

NextBioi 301372.
PROi P15920.
SOURCEi Search...

Gene expression databases

Bgeei P15920.
CleanExi MM_ATP6V0A2.
Genevestigatori P15920.

Family and domain databases

InterProi IPR002490. V-ATPase_116kDa_su.
IPR026028. V-type_ATPase_116kDa_su_euka.
[Graphical view ]
PANTHERi PTHR11629. PTHR11629. 1 hit.
Pfami PF01496. V_ATPase_I. 1 hit.
[Graphical view ]
PIRSFi PIRSF001293. ATP6V0A1. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695 AND SER-700, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiVPP2_MOUSE
AccessioniPrimary (citable) accession number: P15920
Secondary accession number(s): A4FU82
, Q3U2X3, Q8VHU0, Q9JHJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 11, 2001
Last modified: October 29, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3