GMT1_CRYNB
ID GMT1_CRYNB Reviewed; 397 AA.
AC P0CS03; 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 42.
DE RecName: Full=GDP-mannose transporter 1;
DE Short=GMT 1;
GN Name=GMT1; Synonyms=VRG4-1; OrderedLocusNames=CNBF3090;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
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 -!- 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; AAEY01000032; EAL19982.1; -; Genomic_DNA.
DR RefSeq; XP_774629.1; XM_769536.1.
DR AlphaFoldDB; P0CS03; -.
DR SMR; P0CS03; -.
DR EnsemblFungi; AAW44189; AAW44189; CNF01620.
DR EnsemblFungi; EAL19982; EAL19982; CNBF3090.
DR GeneID; 4936861; -.
DR KEGG; cnb:CNBF3090; -.
DR VEuPathDB; FungiDB:CNBF3090; -.
DR HOGENOM; CLU_025360_1_2_1; -.
DR Proteomes; UP000001435; 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: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; IPR013657; UAA.
DR InterPro; IPR038736; Vrg4-like.
DR PANTHER; PTHR11132:SF251; PTHR11132:SF251; 1.
DR Pfam; PF08449; UAA; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Membrane; Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..397
FT /note="GDP-mannose transporter 1"
FT /id="PRO_0000410313"
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
