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BC10_ORYSJ
ID   BC10_ORYSJ              Reviewed;         399 AA.
AC   Q65XS5;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Glycosyltransferase BC10 {ECO:0000305};
DE            EC=2.4.-.- {ECO:0000269|PubMed:18939965};
DE   AltName: Full=Protein BRITTLE CULM 10 {ECO:0000303|PubMed:18939965};
DE   AltName: Full=Protein FRAGILE CULM 116 {ECO:0000303|PubMed:27708650};
GN   Name=BC10 {ECO:0000303|PubMed:18939965};
GN   Synonyms=FC116 {ECO:0000303|PubMed:27708650};
GN   OrderedLocusNames=Os05g0170000 {ECO:0000312|EMBL:BAF16680.1},
GN   LOC_Os05g07790 {ECO:0000305};
GN   ORFNames=OsJ_17281 {ECO:0000312|EMBL:EEE62484.1},
GN   P0685E10.4 {ECO:0000312|EMBL:AAU44326.1};
OS   Oryza sativa subsp. japonica (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=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, SUBCELLULAR
RP   LOCATION, TOPOLOGY, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=18939965; DOI=10.1111/j.1365-313x.2008.03703.x;
RA   Zhou Y., Li S., Qian Q., Zeng D., Zhang M., Guo L., Liu X., Zhang B.,
RA   Deng L., Liu X., Luo G., Wang X., Li J.;
RT   "BC10, a DUF266-containing and Golgi-located type II membrane protein, is
RT   required for cell-wall biosynthesis in rice (Oryza sativa L.).";
RL   Plant J. 57:446-462(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA   Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA   Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA   Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT   "A fine physical map of the rice chromosome 5.";
RL   Mol. Genet. Genomics 274:337-345(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
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).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [8]
RP   FUNCTION, AND MUTAGENESIS OF TRP-232.
RX   PubMed=27708650; DOI=10.3389/fpls.2016.01366;
RA   Zhang M., Wei F., Guo K., Hu Z., Li Y., Xie G., Wang Y., Cai X., Peng L.,
RA   Wang L.;
RT   "A novel FC116/BC10 mutation distinctively causes alteration in the
RT   expression of the genes for cell wall polymer synthesis in rice.";
RL   Front. Plant Sci. 7:1366-1366(2016).
CC   -!- FUNCTION: Glycosyltransferase required for the regulation of cellulose
CC       biosynthesis in the cell wall (PubMed:18939965, PubMed:27708650).
CC       Required for the biosynthesis of hexoses (glucose, mannose and
CC       galactose) in both cellulosic and non-cellulosic (pectins and
CC       hemicelluloses) components of cell walls (PubMed:27708650). Required
CC       for the formation of arabinogalactan proteins which contribute to the
CC       strengthening of cell walls (PubMed:18939965). Possesses low
CC       glycosyltransferase activity (PubMed:18939965).
CC       {ECO:0000269|PubMed:18939965, ECO:0000269|PubMed:27708650}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18939965}; Single-
CC       pass type II membrane protein {ECO:0000269|PubMed:18939965}.
CC       Note=Localizes in punctuate patterns. {ECO:0000269|PubMed:18939965}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, culms, leaves and panicles
CC       (PubMed:18939965). Expressed in vascular bundles of leaf sheaths and
CC       stems where sclerenchyma cells are developing (PubMed:18939965).
CC       Expressed in mechanical tissues of young organs, such as young leaf
CC       sheaths, stems and tiller buds (PubMed:18939965).
CC       {ECO:0000269|PubMed:18939965}.
CC   -!- DISRUPTION PHENOTYPE: Retarded growth and reduced mechanical strength
CC       (brittleness) due to reduced cell wall thickness in sclerenchyma and
CC       bundle sheath fiber cells. {ECO:0000269|PubMed:18939965}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 14 family.
CC       {ECO:0000305}.
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DR   EMBL; EF140884; ABN72585.1; -; Genomic_DNA.
DR   EMBL; AC087553; AAU44326.1; -; Genomic_DNA.
DR   EMBL; AP008211; BAF16680.1; -; Genomic_DNA.
DR   EMBL; AP014961; BAS92477.1; -; Genomic_DNA.
DR   EMBL; CM000142; EEE62484.1; -; Genomic_DNA.
DR   EMBL; AK100216; BAG94494.1; -; mRNA.
DR   EMBL; AK103412; BAG96067.1; -; mRNA.
DR   RefSeq; XP_015637963.1; XM_015782477.1.
DR   AlphaFoldDB; Q65XS5; -.
DR   STRING; 4530.OS05T0170000-02; -.
DR   PaxDb; Q65XS5; -.
DR   PRIDE; Q65XS5; -.
DR   EnsemblPlants; Os05t0170000-01; Os05t0170000-01; Os05g0170000.
DR   EnsemblPlants; Os05t0170000-02; Os05t0170000-02; Os05g0170000.
DR   GeneID; 4337935; -.
DR   Gramene; Os05t0170000-01; Os05t0170000-01; Os05g0170000.
DR   Gramene; Os05t0170000-02; Os05t0170000-02; Os05g0170000.
DR   KEGG; osa:4337935; -.
DR   eggNOG; ENOG502QS7F; Eukaryota.
DR   HOGENOM; CLU_035559_3_0_1; -.
DR   InParanoid; Q65XS5; -.
DR   OMA; HERRGWH; -.
DR   OrthoDB; 1055945at2759; -.
DR   Proteomes; UP000000763; Chromosome 5.
DR   Proteomes; UP000007752; Chromosome 5.
DR   Proteomes; UP000059680; Chromosome 5.
DR   GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:glycosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009664; P:plant-type cell wall organization; IMP:UniProtKB.
DR   InterPro; IPR044174; BC10-like.
DR   InterPro; IPR003406; Glyco_trans_14.
DR   PANTHER; PTHR31042; PTHR31042; 1.
DR   Pfam; PF02485; Branch; 1.
PE   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Cellulose biosynthesis; Glycoprotein;
KW   Glycosyltransferase; Membrane; Reference proteome; Signal-anchor;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..399
FT                   /note="Glycosyltransferase BC10"
FT                   /id="PRO_0000445726"
FT   TOPO_DOM        1..17
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:18939965"
FT   TRANSMEM        18..38
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        39..399
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:18939965"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   MUTAGEN         232
FT                   /note="Missing: In fc116; reduced mechanical strength
FT                   caused by decreased cellulose content and altered cell wall
FT                   structure and composition."
FT                   /evidence="ECO:0000269|PubMed:27708650"
SQ   SEQUENCE   399 AA;  45170 MW;  11A9DD3EFC46CA29 CRC64;
     MKPPRRWMYG RGGGKGKPAG LLLLGVFLCL SVVLLLLLHG SSPSLEGEGR KPEAVEAAGG
     GGEEEEVAVA RAEVEEAPLP PGNARLAFLF IARNRLPLDL VWDAFFRGDK EGRFSIFVHS
     RPGFVLTRAT TRSGFFYNRQ VNNSVQVDWG EASMIEAERV LLAHALKDPL NERFVFVSDS
     CVPLYNFNYT YDYIMSSSTS FVDSFADTKA GRYNPRMDPI IPVENWRKGS QWAVLTRKHA
     EVVVEDEEVL PEFQKHCRRR PLPEFWRDWD RPIPAEAWKA HNCIPDEHYV QTLLAQHGLE
     EELTRRSVTH SAWDLSSSKD RERRGWHPVT YKISDATPAL VKSIKDIDNI YYETENRKEW
     CTSNGKPAPC FLFARKFTRA AGLKLLDLSL IAANGASTM
 
 
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