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FUCTB_DROME
ID   FUCTB_DROME             Reviewed;         444 AA.
AC   Q9VLC1; Q4QQB0; Q8I928;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Alpha-(1,3)-fucosyltransferase B;
DE            EC=2.4.1.-;
DE   AltName: Full=Galactoside 3-L-fucosyltransferase;
GN   Name=FucTB; ORFNames=CG4435;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Canton-S;
RX   PubMed=11382750; DOI=10.1074/jbc.m100573200;
RA   Fabini G., Freilinger A., Altmann F., Wilson I.B.H.;
RT   "Identification of core alpha1,3-fucosylated glycans and cloning of the
RT   requisite fucosyltransferase cDNA from Drosophila melanogaster: Potential
RT   basis of the neural anti-horseradish peroxidase epitope.";
RL   J. Biol. Chem. 276:28058-28067(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Petit D., Picaud F., Dupuy F., Germot A., Julien R., Maftah A.;
RT   "Core a3- and a6-fucosyltransferases in Drosophila: characterization and
RT   origin of diversity.";
RL   Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC       {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC       Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ302046; CAC41642.1; -; mRNA.
DR   EMBL; AY061932; AAL31643.1; -; mRNA.
DR   EMBL; AE014134; AAF52773.4; -; Genomic_DNA.
DR   EMBL; BT023506; AAY84906.1; -; mRNA.
DR   RefSeq; NP_001285779.1; NM_001298850.1.
DR   RefSeq; NP_609288.4; NM_135444.5.
DR   AlphaFoldDB; Q9VLC1; -.
DR   BioGRID; 60364; 1.
DR   IntAct; Q9VLC1; 1.
DR   STRING; 7227.FBpp0079411; -.
DR   CAZy; GT10; Glycosyltransferase Family 10.
DR   GlyGen; Q9VLC1; 3 sites.
DR   PaxDb; Q9VLC1; -.
DR   PRIDE; Q9VLC1; -.
DR   DNASU; 34260; -.
DR   EnsemblMetazoa; FBtr0079811; FBpp0079411; FBgn0032117.
DR   EnsemblMetazoa; FBtr0346623; FBpp0312203; FBgn0032117.
DR   GeneID; 34260; -.
DR   KEGG; dme:Dmel_CG4435; -.
DR   UCSC; CG4435-RA; d. melanogaster.
DR   CTD; 34260; -.
DR   FlyBase; FBgn0032117; FucTB.
DR   VEuPathDB; VectorBase:FBgn0032117; -.
DR   eggNOG; KOG2619; Eukaryota.
DR   HOGENOM; CLU_032075_0_2_1; -.
DR   InParanoid; Q9VLC1; -.
DR   OMA; FTAQEFW; -.
DR   OrthoDB; 551308at2759; -.
DR   PhylomeDB; Q9VLC1; -.
DR   Reactome; R-DME-9037629; Lewis blood group biosynthesis.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 34260; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 34260; -.
DR   PRO; PR:Q9VLC1; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0032117; Expressed in testis and 26 other tissues.
DR   ExpressionAtlas; Q9VLC1; baseline and differential.
DR   Genevisible; Q9VLC1; DM.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:InterPro.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046920; F:alpha-(1->3)-fucosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0036065; P:fucosylation; IBA:GO_Central.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.11660; -; 1.
DR   InterPro; IPR017176; Alpha-1_3-FUT_met.
DR   InterPro; IPR031481; Glyco_tran_10_N.
DR   InterPro; IPR001503; Glyco_trans_10.
DR   InterPro; IPR038577; GT10-like_C_sf.
DR   PANTHER; PTHR11929; PTHR11929; 1.
DR   Pfam; PF17039; Glyco_tran_10_N; 1.
DR   Pfam; PF00852; Glyco_transf_10; 1.
DR   PIRSF; PIRSF037332; Alpha1_3FUT_met; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..444
FT                   /note="Alpha-(1,3)-fucosyltransferase B"
FT                   /id="PRO_0000221127"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..27
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..444
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        279
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        437
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        440
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        409
FT                   /note="V -> I (in Ref. 1; CAC41642)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        417
FT                   /note="D -> N (in Ref. 1; CAC41642)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   444 AA;  51801 MW;  6D95748CA5EF2A76 CRC64;
     MRLAQRYGIA LVALLMVGAT VLFFWSENII NYENIKFNSP VELVWWSRDM SWNYDVQRQC
     GIHTCRITNK RSRRPWARGV LFYGSNIKTG DFPLPRNEHQ IWALLHEESP RNTPFVSNKE
     FLRHFHFTST FSRYSNLPLT TMYLPSGEAL TSKDYYVTFD GKSKYGYRPS TSVVFLQSDC
     DTMSGREDYV KELMKHLPID SYGSCLRNRD LPESLQKDYL NNLYSPELLR FLSEYKFMIA
     IENAACPDYI TEKFWRPLIM GVIPIYFGSP TIKDWEPNNK SAIFVNDFQN PQALVEYLNK
     LADNKKLYNS YRQHKLNRRN PISNKKLLHN LVTRQYHIGD SSPGASLFEK FECAVCYHVI
     NTARNVKADL RHYNCPLEPV YAKMEGQKIP QNVADWRAAM EVGQCQAKVL DEFFRRDIGF
     NDAEFDAELN RRIEGNNCSN SSNT
 
 
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