GMT_SCLS1
ID GMT_SCLS1 Reviewed; 391 AA.
AC A7E558;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=GDP-mannose transporter;
DE Short=GMT;
GN Name=vrg4; ORFNames=SS1G_00430;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476621; EDN91030.1; -; Genomic_DNA.
DR RefSeq; XP_001598344.1; XM_001598294.1.
DR AlphaFoldDB; A7E558; -.
DR SMR; A7E558; -.
DR STRING; 665079.A7E558; -.
DR EnsemblFungi; EDN91030; EDN91030; SS1G_00430.
DR GeneID; 5494635; -.
DR KEGG; ssl:SS1G_00430; -.
DR VEuPathDB; FungiDB:sscle_03g027180; -.
DR eggNOG; KOG1444; Eukaryota.
DR HOGENOM; CLU_025360_1_2_1; -.
DR InParanoid; A7E558; -.
DR OMA; IQSTVCV; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
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; IPR038736; Vrg4-like.
DR PANTHER; PTHR11132:SF251; PTHR11132:SF251; 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..391
FT /note="GDP-mannose transporter"
FT /id="PRO_0000333536"
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..75
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 116..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..141
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 142..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 171..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..209
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..284
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 314..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..339
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 340..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 391 AA; 42590 MW; A9C869AEBF5D25A1 CRC64;
MDDKKNEDVE MRNFNGRSSP SQRDPFISKP GAAKRGGSSF DLSNVTNSPG ISILAYCLAS
ISMTVTNKYC VSGSNWNLNF FYLAIQSVVC IIAIIICKQA GLITNLAPFD TKKAKTWFPI
SLLLVGMIYT STKALQFLSV PVYTIFKNLT IIVIAYGEVL WFGGSVTPSA LFSFGLMVLS
SVVAAWADIQ HALYGGGATQ TKEAADALST LNAGYAWMGM NVFCTAAYVL SMRKVIKKMN
FKDWDTMFYN NLLTIPVLFV CSFVFENWSS ENLTKNFPLE TRNNLILGMI YSGLATIFIS
YCSAWCIRVT SSTTYSMVGA LNKLPIAVSG LVFFAAPVTF GSVSAIFIGF VSGIVYAWAK
VRQNQSKGSV LPTTQPVMSA SSQSNRDAAK A