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RCN11_ORYSJ
ID   RCN11_ORYSJ             Reviewed;         533 AA.
AC   Q6ZFH6; Q703H0; Q703H1;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Beta-1,2-xylosyltransferase RCN11 {ECO:0000305};
DE            Short=OsXylT {ECO:0000303|PubMed:26025522};
DE            EC=2.4.2.- {ECO:0000269|PubMed:26025522};
DE   AltName: Full=Protein REDUCED CULM NUMBER 11 {ECO:0000303|PubMed:26025522};
GN   Name=RCN11 {ECO:0000303|PubMed:26025522};
GN   OrderedLocusNames=Os08g0503800 {ECO:0000312|EMBL:BAF24091.1},
GN   LOC_Os08g39380 {ECO:0000305};
GN   ORFNames=OJ1506_F01.30 {ECO:0000312|EMBL:BAD09279.1};
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 [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   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 52-244 AND 245-533.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15604706; DOI=10.1007/s11103-004-1558-3;
RA   Leonard R., Kolarich D., Paschinger K., Altmann F., Wilson I.;
RT   "A genetic and structural analysis of the N-glycosylation capabilities.";
RL   Plant Mol. Biol. 55:631-644(2004).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26025522; DOI=10.1016/j.plantsci.2015.03.022;
RA   Takano S., Matsuda S., Funabiki A., Furukawa J., Yamauchi T., Tokuji Y.,
RA   Nakazono M., Shinohara Y., Takamure I., Kato K.;
RT   "The rice RCN11 gene encodes beta1,2-xylosyltransferase and is required for
RT   plant responses to abiotic stresses and phytohormones.";
RL   Plant Sci. 236:75-88(2015).
CC   -!- FUNCTION: Glycosyltransferase involved in the xylosylation of N-glycans
CC       (PubMed:26025522). Possesses beta-1,2-xylosyltransferase activity,
CC       transferring xylose from UDP-xylose to the core beta-linked mannose of
CC       N-glycans (PubMed:26025522). Beta-1,2-linked xylose residues on N-
CC       glycans are critical for seed germination and plant development and
CC       growth under conditions of abiotic stress (PubMed:26025522).
CC       {ECO:0000269|PubMed:26025522}.
CC   -!- PATHWAY: Glycan metabolism. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:26025522}; Single-pass type II membrane protein
CC       {ECO:0000305|PubMed:26025522}.
CC   -!- TISSUE SPECIFICITY: Expressed at the base of the crown roots and in the
CC       basal region of the shoot, which contains the shoot and axillary
CC       meristems. {ECO:0000269|PubMed:26025522}.
CC   -!- INDUCTION: Induced by osmotic stress (mannitol), abscisic acid (ABA),
CC       jasmonate (JA), cytokinin (BPA) and brassinosteroid.
CC       {ECO:0000269|PubMed:26025522}.
CC   -!- DISRUPTION PHENOTYPE: Reduced number of tillers and reduced biomass.
CC       {ECO:0000269|PubMed:26025522}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 61 family.
CC       {ECO:0000305}.
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DR   EMBL; AP004190; BAD09279.1; -; Genomic_DNA.
DR   EMBL; AP008214; BAF24091.1; -; Genomic_DNA.
DR   EMBL; AP014964; BAT06140.1; -; Genomic_DNA.
DR   EMBL; AJ621917; CAF21940.1; -; Genomic_DNA.
DR   EMBL; AJ621918; CAF21941.1; -; mRNA.
DR   AlphaFoldDB; Q6ZFH6; -.
DR   STRING; 4530.OS08T0503800-01; -.
DR   CAZy; GT61; Glycosyltransferase Family 61.
DR   PaxDb; Q6ZFH6; -.
DR   PRIDE; Q6ZFH6; -.
DR   EnsemblPlants; Os08t0503800-01; Os08t0503800-01; Os08g0503800.
DR   Gramene; Os08t0503800-01; Os08t0503800-01; Os08g0503800.
DR   eggNOG; KOG4698; Eukaryota.
DR   HOGENOM; CLU_026674_0_0_1; -.
DR   InParanoid; Q6ZFH6; -.
DR   OMA; WRSCEGY; -.
DR   BRENDA; 2.4.2.38; 4460.
DR   Proteomes; UP000000763; Chromosome 8.
DR   Proteomes; UP000059680; Chromosome 8.
DR   GO; GO:0005797; C:Golgi medial cisterna; IEA:EnsemblPlants.
DR   GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050513; F:glycoprotein 2-beta-D-xylosyltransferase activity; IEA:EnsemblPlants.
DR   GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0035252; F:UDP-xylosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IBA:GO_Central.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR   GO; GO:0048367; P:shoot system development; IMP:UniProtKB.
DR   InterPro; IPR007657; Glycosyltransferase_61.
DR   PANTHER; PTHR20961; PTHR20961; 1.
DR   Pfam; PF04577; Glyco_transf_61; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW   Reference proteome; Signal-anchor; Stress response; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..533
FT                   /note="Beta-1,2-xylosyltransferase RCN11"
FT                   /id="PRO_0000445788"
FT   TOPO_DOM        1..23
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        24..44
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        45..533
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   REGION          51..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        307
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        313
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CONFLICT        145
FT                   /note="E -> D (in Ref. 4; CAF21940)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   533 AA;  58896 MW;  9ADCDB02F71DA72A CRC64;
     MMPVRTYHHH HHHNNSNNHR LRRIIPRVLL AVFAIYAVSF AAYLLRHQSP HPHPHPAADP
     ERDAVDAAGG GGGGGAVDRV RVEAPSSQKP WPRLPSFLPW TSASVRPPPK HSCEGYFGNG
     FSRLVDVLPA RGGGGGGWFR CHHSETLRSS ICEGGRVRLD PGLIAMSRGG EPLDQVMGRA
     EEEELPKYEP GALQVEAAAK RTGPLVEAGF LDAYVPTGGI GMHTMRSLLD SGRVVPPGEL
     HCSQWVEEPT LLVTRFEYAN LFHTITDWYS AYVSSRVTDL PNRPNVVFVD GHCKAQLEQT
     WEALFSNVTY VKNFSGPVCF RHAILSPLGY ETALFKGLSE SFSCEGASAE SLREKPDHQK
     TARLSEFGEM ILASFDLLRD DILSSKTSNG LNVLFVRRED YLAHPRHSGK VESRLSNEKE
     VYDAIEGWAK GQKCKINVIN GLFAHMNMKE QLRAIQEASV VIGAHGAGLT HLVSATPDTK
     VLEIISSMYR RPHFALISHW KSLEYHAINL PGSYARVTDV INELSNILKG FGC
 
 
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