GMT_BOTFB
ID GMT_BOTFB Reviewed; 392 AA.
AC A6RJQ8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=GDP-mannose transporter;
DE Short=GMT;
GN Name=gmt1; Synonyms=vrg4; ORFNames=BC1G_00679;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH476843; EDN23206.1; -; Genomic_DNA.
DR RefSeq; XP_001560651.1; XM_001560601.1.
DR AlphaFoldDB; A6RJQ8; -.
DR SMR; A6RJQ8; -.
DR GeneID; 5441191; -.
DR KEGG; bfu:BCIN_03g04240; -.
DR VEuPathDB; FungiDB:Bcin03g04240; -.
DR OMA; IQSTVCV; -.
DR OrthoDB; 1093260at2759; -.
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; 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; Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..392
FT /note="GDP-mannose transporter"
FT /id="PRO_0000333514"
FT TOPO_DOM 1..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..76
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..116
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 117..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..142
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 143..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 172..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..210
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..285
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 315..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..340
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 341..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 392 AA; 42610 MW; 1DD8388D7CD63B55 CRC64;
MDDKKNEDLE MRNFNGRSSP SQRDPFLAKP GAAAKRGNSA FDLSNVTNSP GISILAYCLA
SISMTVTNKY CVSGSNWNLN FFYLAIQSVV CIIAIIICKQ AGLITNLAPF DTKKAKTWFP
ISLLLVGMIY TSTKALQFLS VPVYTIFKNL TIIVIAYGEV LWFGGSVTPS ALFSFGLMVL
SSVVAAWADI QHALYGGGAA QSAEAAAALS TLNAGYAWMG MNVFCTAAYV LSMRKVIKKM
NFKDWDTMFY NNLLTIPVLF VCSFIFENWS SENLTKNFPL ETRNNLILGM IYSGLATIFI
SYCSAWCIRV TSSTTYSMVG ALNKLPIAVS GLVFFAAPVT FGSVSAIFIG FVSGIVYAWA
KVRQNQSKGN ILPTTQPVMS ASSQSNRDAA KA
