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FUT11_TAKRU
ID   FUT11_TAKRU             Reviewed;         501 AA.
AC   Q70AG8;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Alpha-(1,3)-fucosyltransferase 11;
DE            EC=2.4.1.-;
DE   AltName: Full=Fucosyltransferase XI;
DE            Short=Fuc-TXI;
DE            Short=FucT-XI;
DE   AltName: Full=Galactoside 3-L-fucosyltransferase 11;
DE            Short=Fucosyltransferase 11;
GN   Name=fut11;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Martinez-Duncker I., Mollicone R., Candelier J.-J., Oriol R.;
RT   "Phylogeny of fucosyltransferases.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable fucosyltransferase. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ606069; CAE54304.1; -; mRNA.
DR   RefSeq; NP_001027930.1; NM_001032758.1.
DR   AlphaFoldDB; Q70AG8; -.
DR   STRING; 31033.ENSTRUP00000023062; -.
DR   CAZy; GT10; Glycosyltransferase Family 10.
DR   GeneID; 445970; -.
DR   KEGG; tru:445970; -.
DR   CTD; 170384; -.
DR   eggNOG; KOG2619; Eukaryota.
DR   InParanoid; Q70AG8; -.
DR   OrthoDB; 551308at2759; -.
DR   BRENDA; 2.4.1.152; 6209.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000005226; Unplaced.
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; IEA:InterPro.
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   Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW   Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..501
FT                   /note="Alpha-(1,3)-fucosyltransferase 11"
FT                   /id="PRO_0000299014"
FT   TOPO_DOM        1..10
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        11..31
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        32..501
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        428
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        478
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        105..110
FT                   /evidence="ECO:0000250"
FT   DISULFID        396..399
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   501 AA;  57567 MW;  FBBCBF6AC373E0B7 CRC64;
     MLLQMAGRGK MVPCVCLGLL GVLCWVWVSF ASFPDEQLSL GAMDAVERAA FQPQSALSEM
     EFASIGSYRG PGNLDHRSNK ELPILLWWSA GLFPHFPGDT ERIDCARSSC LATSNRKVQL
     YKRTASIIFY GTDFRAYEAP LPRLRHQTWA LFHEESPMNN YLLSHGPGIR LFNYTATFRR
     ESDYPLTLQW LPSLEYLLTP VPVPLEEKNR LRREGLAPVL YMQSHCDVPS DRDRYVQELM
     KYIQVDSYGK CLNNKPLAGN LEDTSTATGE EQTFMSFVAR YKFHLALENG LCPDYMTEKL
     WRPLHQGCVP VYRGSSVVAD WMPNERSAII IDEFPSPQAL AEYLLHLDEN DDEYRKYLEF
     KSPKRITNAR LLEALERREW GVNDMSKPNY LNGFECYVCD QENARLAAER AHRKAPKTNK
     PPEWKMANNS HMGCPLPSPG YGQVHHLPAD DGWLQTWPQD YWQSLDQAEG LESLIRHNES
     DPSLLWKHIQ NMAVRRARGK N
 
 
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