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RAG1_KLULA
ID   RAG1_KLULA              Reviewed;         567 AA.
AC   P18631;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 130.
DE   RecName: Full=Low-affinity glucose transporter;
DE   AltName: Full=Hexose transporter 1;
GN   Name=RAG1; Synonyms=KHT1; OrderedLocusNames=KLLA0D13310g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
RX   PubMed=2402460; DOI=10.1093/nar/18.17.5294;
RA   Goffrini P., Wesolowski-Louvel M., Ferrero I., Fukuhara H.;
RT   "RAG1 gene of the yeast Kluyveromyces lactis codes for a sugar
RT   transporter.";
RL   Nucleic Acids Res. 18:5294-5294(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=1603078; DOI=10.1007/bf00587565;
RA   Wesolowski-Louvel M., Goffrini P., Ferrero I., Fukuhara H.;
RT   "Glucose transport in the yeast Kluyveromyces lactis. I. Properties of an
RT   inducible low-affinity glucose transporter gene.";
RL   Mol. Gen. Genet. 233:89-96(1992).
CC   -!- FUNCTION: Low-affinity glucose transporter.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC       transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR   EMBL; X53752; CAA37781.1; -; Genomic_DNA.
DR   EMBL; CR382124; CAH00752.1; -; Genomic_DNA.
DR   PIR; S11295; S11295.
DR   RefSeq; XP_453656.1; XM_453656.1.
DR   AlphaFoldDB; P18631; -.
DR   SMR; P18631; -.
DR   STRING; 28985.XP_453656.1; -.
DR   EnsemblFungi; CAH00752; CAH00752; KLLA0_D13310g.
DR   GeneID; 2892737; -.
DR   KEGG; kla:KLLA0_D13310g; -.
DR   eggNOG; KOG0254; Eukaryota.
DR   HOGENOM; CLU_001265_30_1_1; -.
DR   InParanoid; P18631; -.
DR   OMA; FWNIIFC; -.
DR   Proteomes; UP000000598; Chromosome D.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005353; F:fructose transmembrane transporter activity; IEA:EnsemblFungi.
DR   GO; GO:0005355; F:glucose transmembrane transporter activity; IEA:EnsemblFungi.
DR   GO; GO:0015578; F:mannose transmembrane transporter activity; IEA:EnsemblFungi.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR005828; MFS_sugar_transport-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR003663; Sugar/inositol_transpt.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   PRINTS; PR00171; SUGRTRNSPORT.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   TIGRFAMs; TIGR00879; SP; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR   PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Reference proteome; Sugar transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..567
FT                   /note="Low-affinity glucose transporter"
FT                   /id="PRO_0000050419"
FT   TOPO_DOM        18..62
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        63..83
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        84..113
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        135..141
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..167
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        189..199
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..220
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        221..234
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..255
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        256..334
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        335..354
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        355..358
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        359..379
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        380..386
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        387..407
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        408..429
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        430..450
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        451..466
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        467..487
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        488..493
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        494..514
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        515..567
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   567 AA;  63124 MW;  89CB737202B117C2 CRC64;
     MSNQMTDSTS AGSGTEHSVD TNTALKAGSP NDLKVSHEED LNDLEKTAEE TLQQKPAKEY
     IFVSLCCVMV AFGGFVFGWD TGTISGFVNQ TDFLRRFGQE KADGSHYLSN VRTGLIVSIF
     NIGCAVGGIV LSNIGDRWGR RIGLITVIII YVIGIIIQIA SVDKWYQYFI GRIISGLGVG
     GITVLSPMLI SETAPKHLRG TLVSCYQLMI TFGIFLGYCT NYGTKNYSNS VQWRVPLGLC
     FAWAIFMVLG MMFVPESARF LVETDQIEEA RKSLAKTNKV SIDDPVVKYE LLKIQSSIEL
     EKAAGNASWG ELITGKPSMF RRTLMGIMIQ SLQQLTGDNY FFYYGTTIFQ SVGMDDSFET
     SIVLGIVNFA STFFALYTVD HFGRRNCLLY GCVGMVACYV VYASVGVTRL WPDGPDHPDI
     SSKGAGNCMI VFACFYIFCF ATTWAPIAYV VISESYPLRV KGKAMAIASA SNWIWGFLIG
     FFTPFITSAI HFYYGYVFMG CMVFAFFYVY FFVPETKGLT LEEVNEMYSE GVLPWKSSSW
     VPSSRRGAEY DVDALQHDDK PWYKAML
 
 
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