VMA21_ASPTN
ID VMA21_ASPTN Reviewed; 107 AA.
AC Q0CXF5;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Vacuolar ATPase assembly integral membrane protein vma21 {ECO:0000255|HAMAP-Rule:MF_03058};
GN Name=vma21; ORFNames=ATEG_01629;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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; CH476595; EAU38386.1; -; Genomic_DNA.
DR RefSeq; XP_001208994.1; XM_001208994.1.
DR AlphaFoldDB; Q0CXF5; -.
DR STRING; 33178.CADATEAP00002692; -.
DR EnsemblFungi; EAU38386; EAU38386; ATEG_01629.
DR GeneID; 4315583; -.
DR VEuPathDB; FungiDB:ATEG_01629; -.
DR eggNOG; ENOG502SBNA; Eukaryota.
DR HOGENOM; CLU_154717_1_1_1; -.
DR OMA; AMKEDQT; -.
DR OrthoDB; 1623513at2759; -.
DR Proteomes; UP000007963; 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 Pfam; PF09446; VMA21; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..107
FT /note="Vacuolar ATPase assembly integral membrane protein
FT vma21"
FT /id="PRO_0000377582"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT TOPO_DOM 57..66
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT TOPO_DOM 88..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 104..107
FT /note="Prevents secretion from ER"
SQ SEQUENCE 107 AA; 11509 MW; EC9481EFF3400D07 CRC64;
MASRRTRETP ADAAAHSTAE KPPVDSDVTP AVPTHVILKL LGFSVAMVST PLGMYFAMSA
FGMSSTFSGI SAAIMANVIL FLYIYVAWQE DQEEREALAA KKAKKAQ