GMT_ASPNC
ID GMT_ASPNC Reviewed; 381 AA.
AC A2R9P4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=GDP-mannose transporter;
DE Short=GMT;
GN Name=gmt1; Synonyms=vrg4; ORFNames=An17g02140;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM270393; CAL00557.1; -; Genomic_DNA.
DR RefSeq; XP_001398443.1; XM_001398406.2.
DR AlphaFoldDB; A2R9P4; -.
DR SMR; A2R9P4; -.
DR PaxDb; A2R9P4; -.
DR EnsemblFungi; CAL00557; CAL00557; An17g02140.
DR GeneID; 4989537; -.
DR KEGG; ang:ANI_1_302154; -.
DR VEuPathDB; FungiDB:An17g02140; -.
DR HOGENOM; CLU_025360_1_2_1; -.
DR Proteomes; UP000006706; Chromosome 5L.
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:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005458; F:GDP-mannose transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR InterPro; IPR000620; EamA_dom.
DR InterPro; IPR038736; Vrg4-like.
DR PANTHER; PTHR11132:SF251; PTHR11132:SF251; 1.
DR Pfam; PF00892; EamA; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Golgi apparatus; Membrane;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..381
FT /note="GDP-mannose transporter"
FT /id="PRO_0000333511"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..70
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 110..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..133
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 134..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 160..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..199
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..273
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..326
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 19..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 381 AA; 41550 MW; 8983725273E05DB2 CRC64;
MAEGKKTDDY TIQMDSIDQG NKSFEAPPPP QPRSPPSGSL SNNPILPVLA YCGSSILMTV
MNKYVLSGTD FNLNFFLLCI QSLVCIIAIQ TCKSCGLITY RDFSADEARK WFPITLLLIG
MIYTGSKALQ FLSIPVYTIF KNLTIILIAY GEVLWFGGSV TGLTLFSFGL MVLSSIIAAW
ADIKHAVESN GDATAKVSTL NAGYIWMLVN CLCTSSYVLG MRKRIKLTNF KDFDTMFYNN
LLSIPVLIVL SAFLEDWSST NVNRNFPPMD RNSIVFAMIL SGLSSVFISY TSAWCVRVTS
STTYSMVGAL NKLPIAISGL IFFDAPVTFP SVSAIVVGFV SGIVYAVAKI KQNAKPRTGV
LPTANPPVSA SSQSMRDSLR S
