GMT_NEUCR
ID GMT_NEUCR Reviewed; 392 AA.
AC Q7SBC5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=GDP-mannose transporter;
DE Short=GMT;
GN Name=vrg-4; ORFNames=NCU06198;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; CM002238; EAA33678.1; -; Genomic_DNA.
DR RefSeq; XP_962914.1; XM_957821.2.
DR AlphaFoldDB; Q7SBC5; -.
DR SMR; Q7SBC5; -.
DR STRING; 5141.EFNCRP00000006017; -.
DR EnsemblFungi; EAA33678; EAA33678; NCU06198.
DR GeneID; 3879062; -.
DR KEGG; ncr:NCU06198; -.
DR VEuPathDB; FungiDB:NCU06198; -.
DR HOGENOM; CLU_025360_1_2_1; -.
DR InParanoid; Q7SBC5; -.
DR OMA; IQSTVCV; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
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; Golgi apparatus; Membrane;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..392
FT /note="GDP-mannose transporter"
FT /id="PRO_0000333531"
FT TOPO_DOM 1..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..80
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 122..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..149
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 150..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 175..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..213
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..287
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..342
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 343..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 392 AA; 42749 MW; 43872E5025770FF4 CRC64;
MANKRNEDIE LGPAEGRGST DKDPFLARRS SSQPNRPQQA GPFGGYFDKI DHSPGASIIA
YCLSSISMTV VNKYVVSGSE WNLNFFYLAV QSLVCTAAIL ICKQLGMFQN LAAFDSTKAK
KWFPISLLLV GMIYTSTKAL QFLSVPVYTI FKNLTIIVVA YGEVLWFGGS VTPMALLSFG
LMVLSSVIAA WADIQAAVEG VGHTAEATDA ISTLNAGYAW MGMNVFCTAA YLLGMRKVIK
KMNFKDYDTM FYNNLLTIPV LIVFSLLFED WSNDNLIKNF PVETRNSLFI GMIYSGLAAI
FISYCSAWCI RVTSSTTYSM VGALNKLPLA ISGLIFFDAP VTFGSVTAIF VGFVSGLVYT
WSKTRQKVSQ ILPTTQPTMS ASAASNRDAA NA