GMT_COCIM
ID GMT_COCIM Reviewed; 387 AA.
AC Q1DTI4; J3K8K7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=GDP-mannose transporter;
DE Short=GMT;
GN Name=VRG4; ORFNames=CIMG_06379;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; GG704912; EAS30900.3; -; Genomic_DNA.
DR RefSeq; XP_001242483.2; XM_001242482.2.
DR AlphaFoldDB; Q1DTI4; -.
DR SMR; Q1DTI4; -.
DR STRING; 246410.Q1DTI4; -.
DR EnsemblFungi; EAS30900; EAS30900; CIMG_06379.
DR GeneID; 4562445; -.
DR KEGG; cim:CIMG_06379; -.
DR VEuPathDB; FungiDB:CIMG_06379; -.
DR InParanoid; Q1DTI4; -.
DR OMA; IQSTVCV; -.
DR OrthoDB; 1093260at2759; -.
DR Proteomes; UP000001261; 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; Golgi apparatus; Membrane;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..387
FT /note="GDP-mannose transporter"
FT /id="PRO_0000333518"
FT TOPO_DOM 1..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..71
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 113..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..136
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 137..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 163..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..206
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..280
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 310..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..332
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 333..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 387 AA; 42489 MW; 4F8E02DF796968E7 CRC64;
MADTKKNDNY AIDMDKLDAE SDRFRPPPQP QPRHSSSSHS QSISNSPVLP ILSYCASSIL
MTVTNKYVLS GVQFNLNFFL LCVQSVVCII AIQTCKSMGL INYRDFNSDE AKKWFPISLL
LIGMIYTGTK ALKFLSIPVY TIFKNLTIIL IAYGEVLWFG GSVTGMALFS FGLMVLSSVI
AAWADIKHAL DTSGFSGAEA TSKISTLNAG YIWMLINCLC TSTYILGMRK RIKLTNFKDF
DTMFYNNLLS IPILMIGSFI VEDWSSENIN KNFPIETRNS LIFAMIFSGL SSVFISYTSA
WCVRVTSSTT YSMVGALNKL PIALSGLIFF GDPVTVPSVS AIVVGFISGI VYSLAKVKQN
AKPRTGVLPT TNPVSASTQS MRDGLKS
