GMT_ASPTN
ID GMT_ASPTN Reviewed; 384 AA.
AC Q0CA27;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=GDP-mannose transporter;
DE Short=GMT;
GN Name=gmt1; Synonyms=vrg4; ORFNames=ATEG_09457;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476607; EAU30594.1; -; Genomic_DNA.
DR RefSeq; XP_001218079.1; XM_001218078.1.
DR AlphaFoldDB; Q0CA27; -.
DR SMR; Q0CA27; -.
DR STRING; 341663.Q0CA27; -.
DR EnsemblFungi; EAU30594; EAU30594; ATEG_09457.
DR GeneID; 4353765; -.
DR VEuPathDB; FungiDB:ATEG_09457; -.
DR eggNOG; KOG1444; Eukaryota.
DR HOGENOM; CLU_025360_1_2_1; -.
DR OMA; IQSTVCV; -.
DR OrthoDB; 1093260at2759; -.
DR Proteomes; UP000007963; 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; 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..384
FT /note="GDP-mannose transporter"
FT /id="PRO_0000333513"
FT TOPO_DOM 1..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..69
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 111..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..134
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 135..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 161..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..200
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..276
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..329
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 364..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 384 AA; 41848 MW; 4870EC85B85A9423 CRC64;
MVEDKKTDDY TIEMDKMDQG SKNFEAAAPP PQPRTPPAGS ISNNPILPVL AYCGSSILMT
VMNKYVLSGL DFNLNFFLLC VQSIVCIVAI QTCKSCGLIT YRDFSADEAR KWFPITLLLI
GMIYTGSKAL QFLSIPVYTI FKNLTIILIA YGEVLWFGGS VTGLTLFSFG LMVLSSIIAA
WADIKHAVES TGDATAKVST LNAGYIWMLV NCLCTSSYVL GMRKRIKLTN FKDFDTLAMF
YNNLLSIPVL IVLTGLMEDW SSANITRNFP PADRNNIIFA MILSGLSSVF ISYTSAWCVR
VTSSTTYSMV GALNKLPIAL SGLIFFDAPV TFPSVSAIVV GFVSGIVYAV AKIKQNAKPK
TGVLPMSNPP VSASSQSMRD SLRS
