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VMA21_PYRTR
ID   VMA21_PYRTR             Reviewed;         107 AA.
AC   B2WDD8;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Vacuolar ATPase assembly integral membrane protein vma21 {ECO:0000255|HAMAP-Rule:MF_03058};
GN   Name=vma21; ORFNames=PTRG_07997;
OS   Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS   (Drechslera tritici-repentis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=426418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP;
RX   PubMed=23316438; DOI=10.1534/g3.112.004044;
RA   Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA   Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA   Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA   Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA   Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT   "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT   repentis, reveals transduplication and the impact of repeat elements on
RT   pathogenicity and population divergence.";
RL   G3 (Bethesda) 3:41-63(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; DS231622; EDU50916.1; -; Genomic_DNA.
DR   RefSeq; XP_001938329.1; XM_001938294.1.
DR   AlphaFoldDB; B2WDD8; -.
DR   STRING; 45151.EDU50916; -.
DR   EnsemblFungi; EDU50916; EDU50916; PTRG_07997.
DR   GeneID; 6346274; -.
DR   eggNOG; ENOG502SBNA; Eukaryota.
DR   HOGENOM; CLU_154717_1_1_1; -.
DR   InParanoid; B2WDD8; -.
DR   OMA; AMKEDQT; -.
DR   OrthoDB; 1623513at2759; -.
DR   Proteomes; UP000001471; 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; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..107
FT                   /note="Vacuolar ATPase assembly integral membrane protein
FT                   vma21"
FT                   /id="PRO_0000377596"
FT   TOPO_DOM        1..41
FT                   /note="Cytoplasmic"
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..68
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT   TOPO_DOM        90..107
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           104..107
FT                   /note="Prevents secretion from ER"
SQ   SEQUENCE   107 AA;  11894 MW;  88A03524676A9576 CRC64;
     MTTRRIVTSE KSTLDYDGKG APEPSNTSPA VPSSVIWKLM SFTFAMITLP IGTYFFTVNW
     VFQGNATYAG GLAALMANVV LIAYVIMAFR DDQEEMREEA EKSKKKL
 
 
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