GMT_ASHGO
ID GMT_ASHGO Reviewed; 329 AA.
AC Q753T9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=GDP-mannose transporter;
DE Short=GMT;
GN Name=VRG4; OrderedLocusNames=AFR236C;
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, AND SEQUENCE REVISION TO 155 AND 161.
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: Involved in the import of GDP-mannose from the cytoplasm into
CC the Golgi lumen. {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic
CC reticulum membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TPT transporter family. SLC35D subfamily.
CC {ECO:0000305}.
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DR EMBL; AE016819; AAS53607.2; -; Genomic_DNA.
DR RefSeq; NP_985783.2; NM_211137.2.
DR AlphaFoldDB; Q753T9; -.
DR SMR; Q753T9; -.
DR STRING; 33169.AAS53607; -.
DR EnsemblFungi; AAS53607; AAS53607; AGOS_AFR236C.
DR GeneID; 4622046; -.
DR KEGG; ago:AGOS_AFR236C; -.
DR eggNOG; KOG1444; Eukaryota.
DR HOGENOM; CLU_025360_1_2_1; -.
DR InParanoid; Q753T9; -.
DR OMA; IQSTVCV; -.
DR Proteomes; UP000000591; Chromosome VI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015297; F:antiporter activity; IBA:GO_Central.
DR GO; GO:0005458; F:GDP-mannose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR InterPro; IPR013657; UAA.
DR InterPro; IPR038736; Vrg4-like.
DR PANTHER; PTHR11132:SF251; PTHR11132:SF251; 1.
DR Pfam; PF08449; UAA; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Membrane; Reference proteome; Sugar transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..329
FT /note="GDP-mannose transporter"
FT /id="PRO_0000333507"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..44
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..109
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..174
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..245
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..298
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 329 AA; 36191 MW; A5CD642E8A3ECD68 CRC64;
MSELKVDTGR LSHIANSGPM SILAYCASSI LMTVTNKCVV GSDKFNMLFV MLFAQSLVCV
TALVLLKALG YVQYRPLNKV DVKNWLLISV LLVLMTYTSS RALKYLAVPI YTIFKNLTII
LIAYGEVLFF GGRVTAMELS SFLLIVLSSV VATLGDQQAL AKKPLAAAVE SILGLNVGYF
WMFTNCICSA LFVLIMRKRI ALTKFKDFDT MFYNNILSLP LLMLASFMFE DWGAANIARN
LTKDYIIIMI ISGLASVGIS YCSGWCVRVT SSTTYSMVGA LNKLPIALSG LLFFDAPKNF
LSIFSIFLGF LSGIVYAVAK QKKQSQPAN
