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GT5_ORYSI
ID   GT5_ORYSI               Reviewed;         449 AA.
AC   A2XFT6;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2015, sequence version 2.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Probable glycosyltransferase 5 {ECO:0000305};
DE            EC=2.4.-.- {ECO:0000305};
GN   Name=GT5 {ECO:0000305}; ORFNames=OsI_11232 {ECO:0000312|EMBL:EAY89696.1};
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
CC   -!- FUNCTION: Probable glycosyltransferase that may be involved in the
CC       biosynthesis of xyloglucan. {ECO:0000250|UniProtKB:Q10MQ0}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC       pass type II membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 34 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAY89696.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CM000128; EAY89696.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A2XFT6; -.
DR   SMR; A2XFT6; -.
DR   STRING; 39946.A2XFT6; -.
DR   HOGENOM; CLU_034328_1_1_1; -.
DR   Proteomes; UP000007015; Chromosome 3.
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   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR008630; Glyco_trans_34.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR31311; PTHR31311; 1.
DR   Pfam; PF05637; Glyco_transf_34; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..449
FT                   /note="Probable glycosyltransferase 5"
FT                   /id="PRO_0000434332"
FT   TOPO_DOM        1..28
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        29..49
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        50..449
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          74..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        413
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        422
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   449 AA;  50430 MW;  2BCE9BD17A808ED7 CRC64;
     MMEKHGGKVT SDRRAGRRQH GQRCSASDAA PLVVVVILIV GALFLILGPT GSSSFTVPRI
     RVVFNEPVHV AVAAPPPPPP PAQMQAGANA SSEEDSGLPP PRQLTDPPYS LGRTILGYDA
     RRSAWLAAHP EFPARVAPAG RPRVLVVTGS APARCPDPDG DHLLLRAFKN KVDYCRIHGL
     DVFYNTAFLD AEMSGFWAKL PLLRMLMVAH PEAELIWWVD SDAVFTDMLF EIPWERYAVH
     NLVLHGWEAK VFDEKSWIGV NTGSFLIRNC QWSLDLLDAW APMGPRGPVR DRYGELFAEE
     LSGRPPFEAD DQSALIYLLV TQRQRWGDKV FIESSYDLNG FWEGIVDRYE ELRRAGRDDG
     RWPFVTHFVG CKPCRRYADS YPAERCRRGM ERAFNFADDQ ILKLYGFAHE SLNTTAVRRV
     RNETGEPLDA GDEELGRLLH PTFRAARPT
 
 
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