VMA21_YEAS1
ID VMA21_YEAS1 Reviewed; 77 AA.
AC B3LIC1;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Vacuolar ATPase assembly integral membrane protein VMA21 {ECO:0000255|HAMAP-Rule:MF_03058};
GN Name=VMA21 {ECO:0000255|HAMAP-Rule:MF_03058}; ORFNames=SCRG_00912;
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions with VOA1 in assembly of the integral membrane
CC sector (also called V0 sector) of the V-ATPase in the endoplasmic
CC reticulum. Escorts the assembled V0 sector in COPII vesicles. Also
CC required for normal packaging of the SNARE BOS1 and possibly the ER to
CC Golgi transport receptor ERV29. {ECO:0000255|HAMAP-Rule:MF_03058}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03058}; 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 Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03058}.
CC Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000255|HAMAP-
CC Rule:MF_03058}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03058}.
CC -!- SIMILARITY: Belongs to the VMA21 family. {ECO:0000255|HAMAP-
CC Rule:MF_03058}.
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DR EMBL; CH408044; EDV10142.1; -; Genomic_DNA.
DR AlphaFoldDB; B3LIC1; -.
DR EnsemblFungi; EDV10142; EDV10142; SCRG_00912.
DR HOGENOM; CLU_154717_1_0_1; -.
DR Proteomes; UP000008335; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03058; VMA21; 1.
DR InterPro; IPR019013; Vma21.
DR PANTHER; PTHR31792; PTHR31792; 1.
DR Pfam; PF09446; VMA21; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Membrane; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..77
FT /note="Vacuolar ATPase assembly integral membrane protein
FT VMA21"
FT /id="PRO_0000377600"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT TOPO_DOM 35..38
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT TOPO_DOM 60..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT MOTIF 74..77
FT /note="Prevents secretion from ER"
SQ SEQUENCE 77 AA; 8435 MW; D09719B2A2839A4B CRC64;
MAVDVPRAVI NKLMLFTAAM VVLPVLTFFI IQQFTPNTLI SGGLAAAMAN VVLIVYIVVA
FREDTEDHKV DGNKKED