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FUT11_CHICK
ID   FUT11_CHICK             Reviewed;         505 AA.
AC   Q8AWC7;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
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   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Candelier J.-J., Martinez-Duncker I., Oriol R., Mollicone R.;
RT   "Cloning expression and genomic organization of a new human alpha3-
RT   fucosyltransferase (FUT11).";
RL   Submitted (DEC-2002) 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; AJ535752; CAD59736.1; -; mRNA.
DR   RefSeq; NP_989759.1; NM_204428.1.
DR   AlphaFoldDB; Q8AWC7; -.
DR   SMR; Q8AWC7; -.
DR   STRING; 9031.ENSGALP00000008285; -.
DR   CAZy; GT10; Glycosyltransferase Family 10.
DR   PaxDb; Q8AWC7; -.
DR   GeneID; 395071; -.
DR   KEGG; gga:395071; -.
DR   CTD; 170384; -.
DR   VEuPathDB; HostDB:geneid_395071; -.
DR   eggNOG; KOG2619; Eukaryota.
DR   InParanoid; Q8AWC7; -.
DR   OrthoDB; 551308at2759; -.
DR   PhylomeDB; Q8AWC7; -.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q8AWC7; -.
DR   Proteomes; UP000000539; 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; 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   Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW   Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..505
FT                   /note="Alpha-(1,3)-fucosyltransferase 11"
FT                   /id="PRO_0000299012"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        13..29
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..505
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          30..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        483
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        110..115
FT                   /evidence="ECO:0000250"
FT   DISULFID        401..404
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   505 AA;  57516 MW;  CA5102A0537B37F6 CRC64;
     MGGGGPGRAA RRGPTCLWVT LALAWGAGSR AAAGDGDGDG EPGPGDAGTP CGAEGWARAA
     VPPGPAFVAA ASYRGPGNND TRSNKALPIL LWWSGSLFPH FPGDTERIDC PRGSCLVTRS
     RRAARHRRTK ALIFYGTDFR AYEAPLPRLP HQTWALFHEE SPMNNYLLSH PPGIRLFNYT
     ATFRRESDYP LTLQWLPGAG YLRGPALPLA EKDAWRRRGY GPVLYMQSHC DVPSDRDRYV
     RELMKYIQVD SYGKCLHNRE LPSERLRDTS TATTEDPEFM AFIARYKFHL ALENAICNDY
     MTEKLWRPMH LGAVPVYRGS PAVRDWMPNN LSIILIDDFD SPQELAKYLD FLDKNGEEYM
     KYLEYKNLDG IKNQFLLESL ERREWGVNDM TLPNYLNGFE CFICDRENAR VRAEQEHKKS
     RGKTPAPSPH IAHFQHMGCP MPTPGFGSVE DLPGEDSWKE MWLQDYWQSL DQGEALTAMI
     RHNESHQGRF WDYMHEIFLK RTRQH
 
 
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