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GMT1_CRYNJ
ID   GMT1_CRYNJ              Reviewed;         397 AA.
AC   P0CS02; Q4JL68; Q55QM9; Q5KFI6;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=GDP-mannose transporter 1;
DE            Short=GMT 1;
GN   Name=GMT1; Synonyms=VRG4-1; OrderedLocusNames=CNF01620;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=17351078; DOI=10.1128/ec.00015-07;
RA   Cottrell T.R., Griffith C.L., Liu H., Nenninger A.A., Doering T.L.;
RT   "The pathogenic fungus Cryptococcus neoformans expresses two functional
RT   GDP-mannose transporters with distinct expression patterns and roles in
RT   capsule synthesis.";
RL   Eukaryot. Cell 6:776-785(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
CC   -!- FUNCTION: Involved in the import of GDP-mannose from the cytoplasm into
CC       the Golgi lumen. Involved in capsule synthesis.
CC       {ECO:0000269|PubMed:17351078}.
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; DQ075902; AAY85624.1; -; mRNA.
DR   EMBL; AE017346; AAW44189.1; -; Genomic_DNA.
DR   RefSeq; XP_571496.1; XM_571496.1.
DR   AlphaFoldDB; P0CS02; -.
DR   SMR; P0CS02; -.
DR   STRING; 5207.AAW44189; -.
DR   TCDB; 2.A.7.13.6; the drug/metabolite transporter (dmt) superfamily.
DR   PaxDb; P0CS02; -.
DR   EnsemblFungi; AAW44189; AAW44189; CNF01620.
DR   GeneID; 3258477; -.
DR   KEGG; cne:CNF01620; -.
DR   VEuPathDB; FungiDB:CNF01620; -.
DR   eggNOG; KOG1444; Eukaryota.
DR   HOGENOM; CLU_025360_1_2_1; -.
DR   InParanoid; P0CS02; -.
DR   OMA; DKVAEHT; -.
DR   OrthoDB; 1093260at2759; -.
DR   PHI-base; PHI:3489; -.
DR   Proteomes; UP000002149; Chromosome 6.
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; IPR013657; UAA.
DR   InterPro; IPR038736; Vrg4-like.
DR   PANTHER; PTHR11132:SF251; PTHR11132:SF251; 1.
DR   Pfam; PF08449; UAA; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasmic vesicle; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW   Membrane; Reference proteome; Sugar transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..397
FT                   /note="GDP-mannose transporter 1"
FT                   /id="PRO_0000333520"
FT   TOPO_DOM        1..61
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        83..87
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109..124
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        125..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        143..145
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        146..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        169..174
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        175..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        198..228
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        250..272
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        294..300
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        301..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        322..332
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        333..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        354..355
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        377..397
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   397 AA;  42883 MW;  2B51E2EB024C6EB5 CRC64;
     MSKPFVPTPN ISRPATPSSL DYGKDEASST LLRDMGERGD RERKDREERD KKEAMPSGQD
     QVLPILSYCA ASIMMTVVNK YVVSGANFTM TFLLLAIQSS VCVLAVTTVK KLGFISFRDF
     DKNDAKAWWP ISTLLVAVIY TGSKALQFLS IPVYTIFKNL TIILIAYGEV FMFNGAVSGL
     TLCSFALMVG SSIIAAWSDI TSVWNKEPEL DPITGLEITV GPVSTIGGLN AGYIWMALNC
     FVSAAYVLFM RKRIKVTGFK DWDSMYYNNL LSIPILVVFS LVIEDWGSES LALNFPASNR
     VLLLSAMAFS GAAAVFISYS TAWCVRITGS TTYSMVGALN KLPVAASGIL FFGDPANFGN
     ISAIAVGGVA GVVYAVAKTN QAKVEKARQA RAAGGRP
 
 
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