VMA21_COCIM
ID VMA21_COCIM Reviewed; 127 AA.
AC Q1DPX9; A0A0D6K9N0; J3K4G2;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 53.
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=CIMG_07634;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; GG704913; EAS28888.1; -; Genomic_DNA.
DR RefSeq; XP_001240471.1; XM_001240470.1.
DR AlphaFoldDB; Q1DPX9; -.
DR EnsemblFungi; EAS28888; EAS28888; CIMG_07634.
DR GeneID; 4560234; -.
DR KEGG; cim:CIMG_07634; -.
DR VEuPathDB; FungiDB:CIMG_07634; -.
DR InParanoid; Q1DPX9; -.
DR OrthoDB; 1623513at2759; -.
DR Proteomes; UP000001261; 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..127
FT /note="Vacuolar ATPase assembly integral membrane protein
FT VMA21"
FT /id="PRO_0000377585"
FT TOPO_DOM 1..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT TOPO_DOM 67..79
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT TOPO_DOM 101..127
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03058"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 124..127
FT /note="Prevents secretion from ER"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 127 AA; 14500 MW; 247798E8C7F2B80D CRC64;
MATRRNPTKE SITTSPPPDQ QPRQPGELEH REAIQLRDLP GYPQQVLWKL IIYSIAVLVL
PLSAYFYSVN YVFDGNTTYA GATAAITANL ILFSYIVVAM REDKGDQEQL REQQQLRGNK
EETKKMK