VMA21_HUMAN
ID VMA21_HUMAN Reviewed; 101 AA.
AC Q3ZAQ7; A6NKV7; B3KUA9;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Vacuolar ATPase assembly integral membrane protein VMA21 {ECO:0000255|HAMAP-Rule:MF_03058};
DE AltName: Full=Myopathy with excessive autophagy protein;
GN Name=VMA21 {ECO:0000255|HAMAP-Rule:MF_03058}; Synonyms=MEAX, XMEA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis carcinoma;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INVOLVEMENT IN MEAX.
RX PubMed=19379691; DOI=10.1016/j.cell.2009.01.054;
RA Ramachandran N., Munteanu I., Wang P., Aubourg P., Rilstone J.J.,
RA Israelian N., Naranian T., Paroutis P., Guo R., Ren Z.-P., Nishino I.,
RA Chabrol B., Pellissier J.-F., Minetti C., Udd B., Fardeau M., Tailor C.S.,
RA Mahuran D.J., Kissel J.T., Kalimo H., Levy N., Manolson M.F.,
RA Ackerley C.A., Minassian B.A.;
RT "VMA21 deficiency causes an autophagic myopathy by compromising V-ATPase
RT activity and lysosomal acidification.";
RL Cell 137:235-246(2009).
RN [5]
RP ERRATUM OF PUBMED:19379691, AND RETRACTION NOTICE OF PUBMED:19379691.
RX PubMed=20873370; DOI=10.1016/j.cell.2010.08.034;
RA Ramachandran N., Munteanu I., Wang P., Aubourg P., Rilstone J.J.,
RA Israelian N., Naranian T., Paroutis P., Guo R., Ren Z.-P., Nishino I.,
RA Chabrol B., Pellissier J.-F., Minetti C., Udd B., Fardeau M., Tailor C.S.,
RA Mahuran D.J., Kissel J.T., Kalimo H., Levy N., Manolson M.F.,
RA Ackerley C.A., Minassian B.A.;
RL Cell 142:984-984(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP INVOLVEMENT IN MEAX, AND SUBCELLULAR LOCATION.
RX PubMed=23315026; DOI=10.1007/s00401-012-1073-6;
RA Ramachandran N., Munteanu I., Wang P., Ruggieri A., Rilstone J.J.,
RA Israelian N., Naranian T., Paroutis P., Guo R., Ren Z.P., Nishino I.,
RA Chabrol B., Pellissier J.F., Minetti C., Udd B., Fardeau M., Tailor C.S.,
RA Mahuran D.J., Kissel J.T., Kalimo H., Levy N., Manolson M.F.,
RA Ackerley C.A., Minassian B.A.;
RT "VMA21 deficiency prevents vacuolar ATPase assembly and causes autophagic
RT vacuolar myopathy.";
RL Acta Neuropathol. 125:439-457(2013).
RN [8]
RP INVOLVEMENT IN MEAX.
RX PubMed=24488655; DOI=10.1002/mus.24197;
RA Crockett C.D., Ruggieri A., Gujrati M., Zallek C.M., Ramachandran N.,
RA Minassian B.A., Moore S.A.;
RT "Late adult-onset of X-linked myopathy with excessive autophagy.";
RL Muscle Nerve 50:138-144(2014).
RN [9]
RP INVOLVEMENT IN MEAX.
RX PubMed=25683699; DOI=10.1016/j.nmd.2014.11.014;
RA Ruggieri A., Ramachandran N., Wang P., Haan E., Kneebone C., Manavis J.,
RA Morandi L., Moroni I., Blumbergs P., Mora M., Minassian B.A.;
RT "Non-coding VMA21 deletions cause X-linked myopathy with excessive
RT autophagy.";
RL Neuromuscul. Disord. 25:207-211(2015).
RN [10]
RP INTERACTION WITH ATP6AP2.
RX PubMed=29127204; DOI=10.1084/jem.20170453;
RA Rujano M.A., Cannata Serio M., Panasyuk G., Peanne R., Reunert J.,
RA Rymen D., Hauser V., Park J.H., Freisinger P., Souche E., Guida M.C.,
RA Maier E.M., Wada Y., Jaeger S., Krogan N.J., Kretz O., Nobre S., Garcia P.,
RA Quelhas D., Bird T.D., Raskind W.H., Schwake M., Duvet S., Foulquier F.,
RA Matthijs G., Marquardt T., Simons M.;
RT "Mutations in the X-linked ATP6AP2 cause a glycosylation disorder with
RT autophagic defects.";
RL J. Exp. Med. 214:3707-3729(2017).
CC -!- FUNCTION: Required for the assembly of the V0 complex of the vacuolar
CC ATPase (V-ATPase) in the endoplasmic reticulum. {ECO:0000255|HAMAP-
CC Rule:MF_03058, ECO:0000269|PubMed:19379691}.
CC -!- SUBUNIT: Associates with the V0 complex of the vacuolar ATPase (V-
CC ATPase) (PubMed:29127204). Interacts with ATP6AP2 (PubMed:29127204).
CC {ECO:0000269|PubMed:29127204}.
CC -!- INTERACTION:
CC Q3ZAQ7; O95870: ABHD16A; NbExp=3; IntAct=EBI-1055364, EBI-348517;
CC Q3ZAQ7; Q08AM2: ADAM33; NbExp=3; IntAct=EBI-1055364, EBI-10225815;
CC Q3ZAQ7; Q13520: AQP6; NbExp=3; IntAct=EBI-1055364, EBI-13059134;
CC Q3ZAQ7; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-1055364, EBI-714543;
CC Q3ZAQ7; Q9HD20-3: ATP13A1; NbExp=3; IntAct=EBI-1055364, EBI-12069500;
CC Q3ZAQ7; Q99437: ATP6V0B; NbExp=3; IntAct=EBI-1055364, EBI-3904417;
CC Q3ZAQ7; Q12981: BNIP1; NbExp=3; IntAct=EBI-1055364, EBI-4402847;
CC Q3ZAQ7; O14735: CDIPT; NbExp=3; IntAct=EBI-1055364, EBI-358858;
CC Q3ZAQ7; Q2HXU8-2: CLEC12B; NbExp=3; IntAct=EBI-1055364, EBI-12811991;
CC Q3ZAQ7; Q9Y4D2: DAGLA; NbExp=3; IntAct=EBI-1055364, EBI-12808806;
CC Q3ZAQ7; P30519: HMOX2; NbExp=3; IntAct=EBI-1055364, EBI-712096;
CC Q3ZAQ7; Q9Y5U4: INSIG2; NbExp=3; IntAct=EBI-1055364, EBI-8503746;
CC Q3ZAQ7; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-1055364, EBI-2820517;
CC Q3ZAQ7; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-1055364, EBI-10317425;
CC Q3ZAQ7; Q6P499: NIPAL3; NbExp=3; IntAct=EBI-1055364, EBI-10252783;
CC Q3ZAQ7; Q9P0S3: ORMDL1; NbExp=3; IntAct=EBI-1055364, EBI-1054848;
CC Q3ZAQ7; Q9Y342: PLLP; NbExp=3; IntAct=EBI-1055364, EBI-3919291;
CC Q3ZAQ7; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-1055364, EBI-10244780;
CC Q3ZAQ7; O00767: SCD; NbExp=3; IntAct=EBI-1055364, EBI-2684237;
CC Q3ZAQ7; Q96AG3: SLC25A46; NbExp=3; IntAct=EBI-1055364, EBI-10281975;
CC Q3ZAQ7; Q6ICL7: SLC35E4; NbExp=3; IntAct=EBI-1055364, EBI-12867720;
CC Q3ZAQ7; Q9NZ01: TECR; NbExp=3; IntAct=EBI-1055364, EBI-2877718;
CC Q3ZAQ7; Q9UPZ6: THSD7A; NbExp=3; IntAct=EBI-1055364, EBI-310962;
CC Q3ZAQ7; Q6UX40: TMEM107; NbExp=3; IntAct=EBI-1055364, EBI-12845616;
CC Q3ZAQ7; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-1055364, EBI-2852148;
CC Q3ZAQ7; P63027: VAMP2; NbExp=3; IntAct=EBI-1055364, EBI-520113;
CC Q3ZAQ7; O95070: YIF1A; NbExp=3; IntAct=EBI-1055364, EBI-2799703;
CC Q3ZAQ7; Q9Y548: YIPF1; NbExp=3; IntAct=EBI-1055364, EBI-7850136;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03058, ECO:0000269|PubMed:19379691,
CC ECO:0000269|PubMed:23315026}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03058}. Endoplasmic reticulum-Golgi
CC intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_03058,
CC ECO:0000269|PubMed:19379691, ECO:0000269|PubMed:23315026}; Multi-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_03058}. Cytoplasmic
CC vesicle, COPII-coated vesicle membrane {ECO:0000255|HAMAP-
CC Rule:MF_03058, ECO:0000269|PubMed:19379691,
CC ECO:0000269|PubMed:23315026}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03058}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3ZAQ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3ZAQ7-2; Sequence=VSP_041257;
CC -!- DISEASE: Myopathy, X-linked, with excessive autophagy (MEAX)
CC [MIM:310440]: A muscle disorder characterized by childhood early onset
CC of a slowly progressive proximal limb muscle weakness (especially in
CC legs) and elevation of serum creatine kinase, without evidence of
CC cardiac, respiratory or central nervous system involvement.
CC Histopathological analysis reveals diseased muscle fibers that are not
CC necrotic, but show abnormal autophagic vacuolation as a manifestation
CC of excessive autophagic activity in skeletal muscle cells.
CC {ECO:0000269|PubMed:19379691, ECO:0000269|PubMed:23315026,
CC ECO:0000269|PubMed:24488655, ECO:0000269|PubMed:25683699}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry. VMA21 deficiency results in an increase of lysosomal pH from 4.7
CC to 5.2, which reduces lysosomal degradative ability and blocks
CC autophagy. This reduces cellular free amino acids, which up-regulates
CC the mTOR pathway and mTOR-dependent macroautophagy, resulting in
CC proliferation of large and ineffective autolysosomes that engulf
CC sections of cytoplasm, merge together, and vacuolate the cell.
CC {ECO:0000269|PubMed:23315026}.
CC -!- SIMILARITY: Belongs to the VMA21 family. {ECO:0000255|HAMAP-
CC Rule:MF_03058}.
CC -!- CAUTION: Protein characterization data are from PubMed:19379691. Due to
CC a number of errors in the figure panels, the article has been retracted
CC but the authors stand by the validity of the main results and
CC conclusions (PubMed:20873370). {ECO:0000305|PubMed:20873370}.
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DR EMBL; AK096835; BAG53371.1; -; mRNA.
DR EMBL; AF003627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC103701; AAI03702.1; -; mRNA.
DR EMBL; BC103702; AAI03703.1; -; mRNA.
DR EMBL; BC105693; AAI05694.1; -; mRNA.
DR EMBL; BC105694; AAI05695.1; -; mRNA.
DR EMBL; BC110800; AAI10801.1; -; mRNA.
DR CCDS; CCDS35430.1; -. [Q3ZAQ7-1]
DR CCDS; CCDS87789.1; -. [Q3ZAQ7-2]
DR RefSeq; NP_001017980.1; NM_001017980.3. [Q3ZAQ7-1]
DR RefSeq; XP_011529427.1; XM_011531125.2.
DR AlphaFoldDB; Q3ZAQ7; -.
DR SMR; Q3ZAQ7; -.
DR BioGRID; 128477; 111.
DR IntAct; Q3ZAQ7; 46.
DR STRING; 9606.ENSP00000333255; -.
DR iPTMnet; Q3ZAQ7; -.
DR PhosphoSitePlus; Q3ZAQ7; -.
DR BioMuta; VMA21; -.
DR DMDM; 121943063; -.
DR EPD; Q3ZAQ7; -.
DR jPOST; Q3ZAQ7; -.
DR MassIVE; Q3ZAQ7; -.
DR MaxQB; Q3ZAQ7; -.
DR PaxDb; Q3ZAQ7; -.
DR PeptideAtlas; Q3ZAQ7; -.
DR PRIDE; Q3ZAQ7; -.
DR ProteomicsDB; 61901; -. [Q3ZAQ7-1]
DR ProteomicsDB; 61902; -. [Q3ZAQ7-2]
DR TopDownProteomics; Q3ZAQ7-1; -. [Q3ZAQ7-1]
DR TopDownProteomics; Q3ZAQ7-2; -. [Q3ZAQ7-2]
DR Antibodypedia; 534; 79 antibodies from 23 providers.
DR DNASU; 203547; -.
DR Ensembl; ENST00000330374.7; ENSP00000333255.6; ENSG00000160131.14. [Q3ZAQ7-1]
DR Ensembl; ENST00000370361.5; ENSP00000359386.1; ENSG00000160131.14. [Q3ZAQ7-2]
DR GeneID; 203547; -.
DR KEGG; hsa:203547; -.
DR MANE-Select; ENST00000330374.7; ENSP00000333255.6; NM_001017980.4; NP_001017980.1.
DR UCSC; uc004feu.4; human. [Q3ZAQ7-1]
DR CTD; 203547; -.
DR DisGeNET; 203547; -.
DR GeneCards; VMA21; -.
DR HGNC; HGNC:22082; VMA21.
DR HPA; ENSG00000160131; Low tissue specificity.
DR MalaCards; VMA21; -.
DR MIM; 300913; gene.
DR MIM; 310440; phenotype.
DR neXtProt; NX_Q3ZAQ7; -.
DR OpenTargets; ENSG00000160131; -.
DR Orphanet; 25980; X-linked myopathy with excessive autophagy.
DR PharmGKB; PA164727498; -.
DR VEuPathDB; HostDB:ENSG00000160131; -.
DR eggNOG; KOG4783; Eukaryota.
DR GeneTree; ENSGT00390000017980; -.
DR HOGENOM; CLU_143588_0_0_1; -.
DR InParanoid; Q3ZAQ7; -.
DR OMA; PYFRGNE; -.
DR OrthoDB; 1603333at2759; -.
DR PhylomeDB; Q3ZAQ7; -.
DR TreeFam; TF314021; -.
DR PathwayCommons; Q3ZAQ7; -.
DR SignaLink; Q3ZAQ7; -.
DR BioGRID-ORCS; 203547; 121 hits in 717 CRISPR screens.
DR ChiTaRS; VMA21; human.
DR GenomeRNAi; 203547; -.
DR Pharos; Q3ZAQ7; Tdark.
DR PRO; PR:Q3ZAQ7; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q3ZAQ7; protein.
DR Bgee; ENSG00000160131; Expressed in ileal mucosa and 186 other tissues.
DR Genevisible; Q3ZAQ7; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; IDA:LIFEdb.
DR GO; GO:0043462; P:regulation of ATP-dependent activity; TAS:ParkinsonsUK-UCL.
DR GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IBA:GO_Central.
DR HAMAP; MF_03058; VMA21; 1.
DR InterPro; IPR019013; Vma21.
DR PANTHER; PTHR31792; PTHR31792; 1.
DR Pfam; PF09446; VMA21; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasmic vesicle; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..101
FT /note="Vacuolar ATPase assembly integral membrane protein
FT VMA21"
FT /id="PRO_0000331499"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT TOPO_DOM 47..65
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT TOPO_DOM 87..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT VAR_SEQ 1..17
FT /note="MERPDKAALNALQPPEF -> MLGSPCGPQLSDRDADEDQCSREFRGRRSRR
FT PPRRTMLRGKSRLNVEWLGYSPGLLLEHRPLLAGRTPRSHR (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041257"
SQ SEQUENCE 101 AA; 11354 MW; 9DE436A7FF533443 CRC64;
MERPDKAALN ALQPPEFRNE SSLASTLKTL LFFTALMITV PIGLYFTTKS YIFEGALGMS
NRDSYFYAAI VAVVAVHVVL ALFVYVAWNE GSRQWREGKQ D
