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Protein

Vacuolar ATPase assembly integral membrane protein VMA21

Gene

VMA21

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.1 PublicationUniRule annotation

GO - Biological processi

  1. vacuolar proton-transporting V-type ATPase complex assembly Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar ATPase assembly integral membrane protein VMA21UniRule annotation
Alternative name(s):
Myopathy with excessive autophagy protein
Gene namesi
Name:VMA21UniRule annotation
Synonyms:MEAX, XMEA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:22082. VMA21.

Subcellular locationi

Endoplasmic reticulum membrane 1 PublicationUniRule annotation; Multi-pass membrane protein 1 PublicationUniRule annotation. Endoplasmic reticulum-Golgi intermediate compartment membrane 1 PublicationUniRule annotation; Multi-pass membrane protein 1 PublicationUniRule annotation. Cytoplasmic vesicleCOPII-coated vesicle membrane 1 PublicationUniRule annotation; Multi-pass membrane protein 1 PublicationUniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2525CytoplasmicUniRule annotationAdd
BLAST
Transmembranei26 – 4621HelicalUniRule annotationAdd
BLAST
Topological domaini47 – 6519LumenalUniRule annotationAdd
BLAST
Transmembranei66 – 8621HelicalUniRule annotationAdd
BLAST
Topological domaini87 – 10115CytoplasmicUniRule annotationAdd
BLAST

GO - Cellular componenti

  1. COPII vesicle coat Source: UniProtKB
  2. endoplasmic reticulum-Golgi intermediate compartment membrane Source: UniProtKB-SubCell
  3. endoplasmic reticulum membrane Source: UniProtKB
  4. integral component of membrane Source: UniProtKB-KW
  5. lysosome Source: LIFEdb
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Myopathy, X-linked, with excessive autophagy1 Publication

The gene represented in this entry may be involved in disease pathogenesis. VMA21 deficiency results in an increase of lysosomal pH from 4.7 to 5.2, which reduces lysosomal degradative ability and blocks autophagy. This reduces cellular free amino acids, which upregulates the mTOR pathway and mTOR-dependent macroautophagy, resulting in proliferation of large and ineffective autolysosomes that engulf sections of cytoplasm, merge together, and vacuolate the cell (PubMed:19379691).

Disease descriptionA muscle disorder characterized by childhood early onset of a slowly progressive proximal limb muscle weakness (especially in legs) and elevation of serum creatine kinase, without evidence of cardiac, respiratory or central nervous system involvement. Histopathological analysis reveals diseased muscle fibers that are not necrotic, but show abnormal autophagic vacuolation as a manifestation of excessive autophagic activity in skeletal muscle cells.

See also OMIM:310440

Organism-specific databases

MIMi310440. phenotype.
Orphaneti25980. X-linked myopathy with excessive autophagy.
PharmGKBiPA164727498.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 101101Vacuolar ATPase assembly integral membrane protein VMA21PRO_0000331499Add
BLAST

Proteomic databases

MaxQBiQ3ZAQ7.
PaxDbiQ3ZAQ7.
PRIDEiQ3ZAQ7.

Expressioni

Gene expression databases

BgeeiQ3ZAQ7.
GenevestigatoriQ3ZAQ7.

Organism-specific databases

HPAiHPA010972.

Interactioni

Subunit structurei

Associates with the V0 complex of the vacuolar ATPase (V-ATPase).

Protein-protein interaction databases

BioGridi128477. 15 interactions.
IntActiQ3ZAQ7. 1 interaction.
STRINGi9606.ENSP00000333255.

Structurei

3D structure databases

ProteinModelPortaliQ3ZAQ7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the VMA21 family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG287271.
GeneTreeiENSGT00390000017980.
HOGENOMiHOG000154822.
InParanoidiQ3ZAQ7.
OMAiSKAYIFE.
OrthoDBiEOG7XWPR8.
PhylomeDBiQ3ZAQ7.
TreeFamiTF314021.

Family and domain databases

HAMAPiMF_03058. VMA21.
InterProiIPR019013. VMA21-like_domain.
[Graphical view]
PfamiPF09446. VMA21. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q3ZAQ7-1) [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
MERPDKAALN ALQPPEFRNE SSLASTLKTL LFFTALMITV PIGLYFTTKS
60 70 80 90 100
YIFEGALGMS NRDSYFYAAI VAVVAVHVVL ALFVYVAWNE GSRQWREGKQ

D
Length:101
Mass (Da):11,354
Last modified:September 27, 2005 - v1
Checksum:i9DE436A7FF533443
GO
Isoform 2 (identifier: Q3ZAQ7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: MERPDKAALNALQPPEF → MLGSPCGPQL...LAGRTPRSHR

Note: No experimental confirmation available.

Show »
Length:156
Mass (Da):17,766
Checksum:i8A3F475CD071D5BC
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1717MERPD…QPPEF → MLGSPCGPQLSDRDADEDQC SREFRGRRSRRPPRRTMLRG KSRLNVEWLGYSPGLLLEHR PLLAGRTPRSHR in isoform 2. CuratedVSP_041257Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK096835 mRNA. Translation: BAG53371.1.
AF003627 Genomic DNA. No translation available.
BC103701 mRNA. Translation: AAI03702.1.
BC103702 mRNA. Translation: AAI03703.1.
BC105693 mRNA. Translation: AAI05694.1.
BC105694 mRNA. Translation: AAI05695.1.
BC110800 mRNA. Translation: AAI10801.1.
CCDSiCCDS35430.1. [Q3ZAQ7-1]
RefSeqiNP_001017980.1. NM_001017980.3. [Q3ZAQ7-1]
UniGeneiHs.58633.

Genome annotation databases

EnsembliENST00000330374; ENSP00000333255; ENSG00000160131. [Q3ZAQ7-1]
ENST00000370361; ENSP00000359386; ENSG00000160131. [Q3ZAQ7-2]
GeneIDi203547.
KEGGihsa:203547.
UCSCiuc004feu.3. human. [Q3ZAQ7-1]

Polymorphism databases

DMDMi121943063.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK096835 mRNA. Translation: BAG53371.1.
AF003627 Genomic DNA. No translation available.
BC103701 mRNA. Translation: AAI03702.1.
BC103702 mRNA. Translation: AAI03703.1.
BC105693 mRNA. Translation: AAI05694.1.
BC105694 mRNA. Translation: AAI05695.1.
BC110800 mRNA. Translation: AAI10801.1.
CCDSiCCDS35430.1. [Q3ZAQ7-1]
RefSeqiNP_001017980.1. NM_001017980.3. [Q3ZAQ7-1]
UniGeneiHs.58633.

3D structure databases

ProteinModelPortaliQ3ZAQ7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128477. 15 interactions.
IntActiQ3ZAQ7. 1 interaction.
STRINGi9606.ENSP00000333255.

Polymorphism databases

DMDMi121943063.

Proteomic databases

MaxQBiQ3ZAQ7.
PaxDbiQ3ZAQ7.
PRIDEiQ3ZAQ7.

Protocols and materials databases

DNASUi203547.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000330374; ENSP00000333255; ENSG00000160131. [Q3ZAQ7-1]
ENST00000370361; ENSP00000359386; ENSG00000160131. [Q3ZAQ7-2]
GeneIDi203547.
KEGGihsa:203547.
UCSCiuc004feu.3. human. [Q3ZAQ7-1]

Organism-specific databases

CTDi203547.
GeneCardsiGC0XP150564.
HGNCiHGNC:22082. VMA21.
HPAiHPA010972.
MIMi300913. gene.
310440. phenotype.
neXtProtiNX_Q3ZAQ7.
Orphaneti25980. X-linked myopathy with excessive autophagy.
PharmGKBiPA164727498.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG287271.
GeneTreeiENSGT00390000017980.
HOGENOMiHOG000154822.
InParanoidiQ3ZAQ7.
OMAiSKAYIFE.
OrthoDBiEOG7XWPR8.
PhylomeDBiQ3ZAQ7.
TreeFamiTF314021.

Miscellaneous databases

ChiTaRSiVMA21. human.
GenomeRNAii203547.
NextBioi90447.
PROiQ3ZAQ7.
SOURCEiSearch...

Gene expression databases

BgeeiQ3ZAQ7.
GenevestigatoriQ3ZAQ7.

Family and domain databases

HAMAPiMF_03058. VMA21.
InterProiIPR019013. VMA21-like_domain.
[Graphical view]
PfamiPF09446. VMA21. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  2. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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: Testis carcinoma.
  4. Cited for: FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN MEAX.
  5. Cited for: RETRACTION.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiVMA21_HUMAN
AccessioniPrimary (citable) accession number: Q3ZAQ7
Secondary accession number(s): A6NKV7, B3KUA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: September 27, 2005
Last modified: January 7, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.