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VMA21_YEAST
ID   VMA21_YEAST             Reviewed;          77 AA.
AC   P41806; D6VUN7; Q6Q5Q3;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 147.
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=YGR105W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF 74-LYS-LYS-75.
RC   STRAIN=SF838-1D;
RX   PubMed=7841520; DOI=10.1091/mbc.5.9.1039;
RA   Hill K.J., Stevens T.H.;
RT   "Vma21p is a yeast membrane protein retained in the endoplasmic reticulum
RT   by a di-lysine motif and is required for the assembly of the vacuolar H(+)-
RT   ATPase complex.";
RL   Mol. Biol. Cell 5:1039-1050(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   FUNCTION.
RX   PubMed=8416931; DOI=10.1016/s0021-9258(18)54138-7;
RA   Ho M.N., Hill K.J., Lindorfer M.A., Stevens T.H.;
RT   "Isolation of vacuolar membrane H(+)-ATPase-deficient yeast mutants; the
RT   VMA5 and VMA4 genes are essential for assembly and activity of the vacuolar
RT   H(+)-ATPase.";
RL   J. Biol. Chem. 268:221-227(1993).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   FUNCTION, INTERACTION WITH VMA3; VMA6; VMA11; VMA16 AND VPH1, AND
RP   MUTAGENESIS OF 74-LYS-LYS-75.
RX   PubMed=15356264; DOI=10.1091/mbc.e04-06-0514;
RA   Malkus P., Graham L.A., Stevens T.H., Schekman R.;
RT   "Role of Vma21p in assembly and transport of the yeast vacuolar ATPase.";
RL   Mol. Biol. Cell 15:5075-5091(2004).
RN   [8]
RP   INTERACTION WITH VMA3; VMA6; VMA11 AND VPH1.
RX   PubMed=16569636; DOI=10.1074/jbc.m600890200;
RA   Compton M.A., Graham L.A., Stevens T.H.;
RT   "Vma9p (subunit e) is an integral membrane V0 subunit of the yeast V-
RT   ATPase.";
RL   J. Biol. Chem. 281:15312-15319(2006).
RN   [9]
RP   FUNCTION.
RX   PubMed=16926153; DOI=10.1074/jbc.m606451200;
RA   Davis-Kaplan S.R., Compton M.A., Flannery A.R., Ward D.M., Kaplan J.,
RA   Stevens T.H., Graham L.A.;
RT   "PKR1 encodes an assembly factor for the yeast V-type ATPase.";
RL   J. Biol. Chem. 281:32025-32035(2006).
RN   [10]
RP   FUNCTION.
RX   PubMed=17077122; DOI=10.1242/jcs.03250;
RA   Welsh L.M., Tong A.H.Y., Boone C., Jensen O.N., Otte S.;
RT   "Genetic and molecular interactions of the Erv41p-Erv46p complex involved
RT   in transport between the endoplasmic reticulum and Golgi complex.";
RL   J. Cell Sci. 119:4730-4740(2006).
RN   [11]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [12]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VMA3; VMA6; VMA11;
RP   VMA16 AND VOA1.
RX   PubMed=18799613; DOI=10.1091/mbc.e08-06-0629;
RA   Ryan M., Graham L.A., Stevens T.H.;
RT   "Voa1p functions in V-ATPase assembly in the yeast endoplasmic reticulum.";
RL   Mol. Biol. Cell 19:5131-5142(2008).
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       ECO:0000269|PubMed:15356264, ECO:0000269|PubMed:16926153,
CC       ECO:0000269|PubMed:17077122, ECO:0000269|PubMed:18799613,
CC       ECO:0000269|PubMed:7841520, ECO:0000269|PubMed:8416931}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein. Endoplasmic reticulum-Golgi intermediate compartment
CC       membrane {ECO:0000255|HAMAP-Rule:MF_03058}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03058}. Cytoplasmic vesicle, COPII-coated
CC       vesicle membrane; Multi-pass membrane protein.
CC   -!- MISCELLANEOUS: Present with 1480 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the VMA21 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03058}.
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DR   EMBL; U09329; AAA74455.1; -; Genomic_DNA.
DR   EMBL; Z72890; CAA97109.1; -; Genomic_DNA.
DR   EMBL; AY557816; AAS56142.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08198.1; -; Genomic_DNA.
DR   PIR; S47941; S47941.
DR   RefSeq; NP_011619.3; NM_001181234.3.
DR   AlphaFoldDB; P41806; -.
DR   BioGRID; 33348; 916.
DR   DIP; DIP-5526N; -.
DR   IntAct; P41806; 10.
DR   MINT; P41806; -.
DR   STRING; 4932.YGR105W; -.
DR   MaxQB; P41806; -.
DR   PaxDb; P41806; -.
DR   PRIDE; P41806; -.
DR   TopDownProteomics; P41806; -.
DR   EnsemblFungi; YGR105W_mRNA; YGR105W; YGR105W.
DR   GeneID; 852997; -.
DR   KEGG; sce:YGR105W; -.
DR   SGD; S000003337; VMA21.
DR   VEuPathDB; FungiDB:YGR105W; -.
DR   eggNOG; ENOG502SBNA; Eukaryota.
DR   HOGENOM; CLU_154717_1_0_1; -.
DR   InParanoid; P41806; -.
DR   OMA; MAVDIPR; -.
DR   BioCyc; YEAST:G3O-30815-MON; -.
DR   PRO; PR:P41806; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P41806; protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
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; IMP:SGD.
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   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_0000065875"
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"
FT   MUTAGEN         74..75
FT                   /note="KK->QQ: Mislocalizes to the vacuole membrane and
FT                   stay associated with the V0 sector after transport out of
FT                   the ER."
FT                   /evidence="ECO:0000269|PubMed:15356264,
FT                   ECO:0000269|PubMed:7841520"
FT   MUTAGEN         74
FT                   /note="K->Q: Secretion from ER."
FT   MUTAGEN         75
FT                   /note="K->Q: Secretion from ER."
FT   CONFLICT        70
FT                   /note="V -> G (in Ref. 4; AAS56142)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   77 AA;  8435 MW;  D09719B2A2839A4B CRC64;
     MAVDVPRAVI NKLMLFTAAM VVLPVLTFFI IQQFTPNTLI SGGLAAAMAN VVLIVYIVVA
     FREDTEDHKV DGNKKED
 
 
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