GMT_MALGO
ID GMT_MALGO Reviewed; 484 AA.
AC A8PTV6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=GDP-mannose transporter;
DE Short=GMT;
GN Name=VRG4; ORFNames=MGL_0485;
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966;
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., DeAngelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L. Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(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; AAYY01000001; EDP45496.1; -; Genomic_DNA.
DR RefSeq; XP_001732710.1; XM_001732658.1.
DR AlphaFoldDB; A8PTV6; -.
DR SMR; A8PTV6; -.
DR STRING; 425265.A8PTV6; -.
DR EnsemblFungi; EDP45496; EDP45496; MGL_0485.
DR GeneID; 5857016; -.
DR KEGG; mgl:MGL_0485; -.
DR VEuPathDB; FungiDB:MGL_0485; -.
DR InParanoid; A8PTV6; -.
DR OMA; IRVWIPV; -.
DR OrthoDB; 1093260at2759; -.
DR Proteomes; UP000008837; 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: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; Glycoprotein; Golgi apparatus;
KW Membrane; Reference proteome; Sugar transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..484
FT /note="GDP-mannose transporter"
FT /id="PRO_0000333528"
FT TOPO_DOM 1..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..90
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..155
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..287
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..360
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..413
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..484
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 484 AA; 52613 MW; 8BD92F1A2506B766 CRC64;
MSMTTSRERN VPPDDNEIEL GRSRHSDVAP ESESPQAHLL NSDVASVTKN FMRNASHATA
NSGAIAAVLS YCIASISMTV INKFTVSGEK FTMNLLVLLC QCSVGVAMVY AAKCMGWIQI
RTLNMRDVKT WFPISTMLVF VIYTGSKALQ HMDIPIYTIF KNLTIILIAY GELLWFNGRI
TPMVFLSFIL MVLSSIIAAW PDLAPSTAKT LYSRAFESLN LYTGVPHATE GWGEGVRTEA
ASAMHPHTAL SPLSVKPYVG AATPLAAAVA QQNSEAAASS STLSSWSTNG YVWMLANCMI
SATYVLVMRK RIKLTGFKDW DTMFYNNLLS IPVLLFMSLL VENWSVETFE HNFPREKRST
LVFAILLSGT GGVFISYTTA WCIRVTSSTT YSMVGALNKL PLALSGMLFF GNPVTPYNSI
GVAVGFIAGI VYAVGKYKQV VAARIANSDA TGASTSLSSS SSAAPSGEYV FDLKGEIPTH
TRQQ
