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MSR_TRIFG
ID   MSR_TRIFG               Reviewed;         413 AA.
AC   K7R4D4;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2013, sequence version 1.
DT   03-AUG-2022, entry version 16.
DE   RecName: Full=Protein MANNAN SYNTHESIS-RELATED {ECO:0000303|PubMed:22966747, ECO:0000312|EMBL:AFV79649.1};
DE            Short=TfMSR {ECO:0000303|PubMed:22966747};
DE            EC=2.4.1.- {ECO:0000305};
DE   AltName: Full=O-fucosyltransferase {ECO:0000305};
DE            Short=O-FucT {ECO:0000305};
DE   AltName: Full=O-fucosyltransferase family protein {ECO:0000305};
DE   AltName: Full=TfDUF246 {ECO:0000303|PubMed:22527750};
GN   Name=MSR {ECO:0000303|PubMed:22966747, ECO:0000312|EMBL:AFV79649.1};
OS   Trigonella foenum-graecum (Fenugreek).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trigonella.
OX   NCBI_TaxID=78534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=22527750; DOI=10.1007/s11103-012-9909-y;
RA   Wang Y., Alonso A.P., Wilkerson C.G., Keegstra K.;
RT   "Deep EST profiling of developing fenugreek endosperm to investigate
RT   galactomannan biosynthesis and its regulation.";
RL   Plant Mol. Biol. 79:243-258(2012).
RN   [2]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=22966747; DOI=10.1111/tpj.12019;
RA   Wang Y., Mortimer J.C., Davis J., Dupree P., Keegstra K.;
RT   "Identification of an additional protein involved in mannan biosynthesis.";
RL   Plant J. 73:105-117(2013).
CC   -!- FUNCTION: Glycosyltransferase involved in mannan biosynthesis.
CC       {ECO:0000269|PubMed:22966747}.
CC   -!- PATHWAY: Glycan biosynthesis. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:22966747}; Single-pass type II membrane protein
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Highly and specifically expressed in the endosperm.
CC       {ECO:0000269|PubMed:22966747}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase GT106 family.
CC       {ECO:0000305}.
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DR   EMBL; JX237834; AFV79649.1; -; mRNA.
DR   AlphaFoldDB; K7R4D4; -.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
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:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR024709; FucosylTrfase_pln.
DR   InterPro; IPR019378; GDP-Fuc_O-FucTrfase.
DR   PANTHER; PTHR31288; PTHR31288; 1.
DR   Pfam; PF10250; O-FucT; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW   Fucose metabolism; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW   Membrane; Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..413
FT                   /note="Protein MANNAN SYNTHESIS-RELATED"
FT                   /id="PRO_0000442102"
FT   TOPO_DOM        1..5
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        6..26
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        27..413
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   BINDING         255..257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H488"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   413 AA;  46439 MW;  057F07D10B0330BA CRC64;
     MNSMEIRQAF AGLLTLSMFI MLGNMIKKDH FDYPAEEVEI QTTEVSQHDL ATVSHISQKS
     KQNDKALKPC WNPPTLKEVE QSKGFIIFSL TNGPEYHIAQ VADAVVVAKY LGATLVLPDI
     KNSKSGNSMN LGDIYDVENV LNKLNGLVKV TKTLPPHVST RNTPIVRVPN KVSQDYIMKK
     LKPIYQAKGI IKIESYFPSK NTISRNNNSL ESLLCQTMFG GTLELKKEIQ EEAESIVQKL
     ETWSQESNGP FVAVDLRIEG LKNECNGKDG KGRKQCYQGH EIGEFLKRIG FGQETVIYVT
     QTKWSPDLNS LRYMFPKTYT KENIMSSTKK EKFINSESIE FEKAIDFYIC SESDVFVPSI
     LGPFYENVAG MRIVSGKNEI IVPSEVVSPS ASASEHMSPY VTKKNHLAYK CFC
 
 
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