Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P15920

- VPP2_MOUSE

UniProt

P15920 - VPP2_MOUSE

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (11 Jan 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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
    2. protein binding Source: IntAct

    GO - Biological processi

    1. ATP hydrolysis coupled proton transport Source: InterPro

    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 membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. lysosomal membrane Source: Ensembl
    5. plasma membrane Source: UniProtKB-SubCell
    6. vacuolar proton-transporting V-type ATPase, V0 domain Source: InterPro

    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

    MGSLFRSESM CLAQLFLQSG TAYECLSALG EKGLVQFRDL NQNVSSFQRK    50
    FVGEVKRCEE LERILVYLVQ EITRADIPLP EGEASPPAPP LKHVLEMQEQ 100
    LQKLEVELRE VTKNKEKLRK NLLELVEYTH MLRVTKTFLK RNVEFEPTYE 150
    EFPALENDSL LDYSCMQRLG AKLGFVSGLI QQGRVEAFER MLWRACKGYT 200
    IVTYAELDEC LEDPETGEVI KWYVFLISFW GEQIGHKVKK ICDCYHCHIY 250
    PYPNTAEERR EIQEGLNTRI QDLYTVLHKT EDYLRQVLCK AAESVCSRVV 300
    QVRKMKAIYH MLNMCSFDVT NKCLIAEVWC PEVDLPGLRR ALEEGSRESG 350
    ATIPSFMNTI PTKETPPTLI RTNKFTEGFQ NIVDAYGVGS YREVNPALFT 400
    IITFPFLFAV MFGDFGHGFV MFLFALLLVL NENHPRLSQS QEILRMFFDG 450
    RYILLLMGLF SVYTGLIYND CFSKSVNLFG SGWNVSAMYS SSHSPEEQRK 500
    MVLWNDSTIR HSRTLQLDPN IPGVFRGPYP FGIDPIWNLA TNRLTFLNSF 550
    KMKMSVILGI FHMTFGVVLG IFNHLHFRKK FNVYLVSVPE ILFMLCIFGY 600
    LIFMIIYKWL AYSAETSREA PSILIEFINM FLFPTSKTHG LYPGQAHVQR 650
    VLVALTVLAV PVLFLGKPLF LLWLHNGRNC FGMSRSGYTL VRKDSEEEVS 700
    LLGNQDIEEG NSRMEEGCRE VTCEEFNFGE ILMTQAIHSI EYCLGCISNT 750
    ASYLRLWALS LAHAQLSDVL WAMLMRVGLR VDTTYGVLLL LPVMAFFAVL 800
    TIFILLVMEG LSAFLHAIRL HWVEFQNKFY VGAGTKFVPF SFSLLSSKFS 850
    NDDSIA 856
    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

    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 1, 2014
    This is version 139 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