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VMA21_ASHGO
ID   VMA21_ASHGO             Reviewed;          77 AA.
AC   Q75EI3;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 85.
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}; OrderedLocusNames=AAR096W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016814; AAS50461.1; -; Genomic_DNA.
DR   RefSeq; NP_982637.1; NM_207990.1.
DR   AlphaFoldDB; Q75EI3; -.
DR   STRING; 33169.AAS50461; -.
DR   EnsemblFungi; AAS50461; AAS50461; AGOS_AAR096W.
DR   GeneID; 4618561; -.
DR   KEGG; ago:AGOS_AAR096W; -.
DR   eggNOG; ENOG502SBNA; Eukaryota.
DR   HOGENOM; CLU_154717_1_0_1; -.
DR   InParanoid; Q75EI3; -.
DR   OMA; MAVDIPR; -.
DR   Proteomes; UP000000591; Chromosome I.
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:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IBA:GO_Central.
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..77
FT                   /note="Vacuolar ATPase assembly integral membrane protein
FT                   VMA21"
FT                   /id="PRO_0000377578"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT   TOPO_DOM        30..41
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT   TOPO_DOM        63..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;  8353 MW;  42B6E952501B2F71 CRC64;
     MAVDVPTSVI VKLMFFTLAM VSFPVLTFFV SQQYTSNTLV NGGLAALAAN VVLFAYVIMA
     FSEDVPQSDG KESKKQQ
 
 
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