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RGXT3_ARATH
ID   RGXT3_ARATH             Reviewed;         383 AA.
AC   Q9FXA7;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferase 3 {ECO:0000305};
DE            EC=2.4.2.- {ECO:0000305};
DE   AltName: Full=Rhamnogalacturonan xylosyltransferase 3 {ECO:0000305};
GN   Name=RGXT3 {ECO:0000303|PubMed:18755189}; OrderedLocusNames=At1g56550;
GN   ORFNames=F25P12.100;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND
RP   GLYCOSYLATION.
RX   PubMed=18755189; DOI=10.1016/j.febslet.2008.08.015;
RA   Egelund J., Damager I., Faber K., Olsen C.E., Ulvskov P., Petersen B.L.;
RT   "Functional characterisation of a putative rhamnogalacturonan II specific
RT   xylosyltransferase.";
RL   FEBS Lett. 582:3217-3222(2008).
CC   -!- FUNCTION: Catalyzes the transfer of D-xylose from UDP-alpha-D-xylose
CC       onto L-fucose. Probably involved in the biosynthesis of
CC       rhamnogalacturonan II (RG-II) through xylosylation of the internal
CC       fucose moiety of the A-chain of RG-II, a structurally complex pectic
CC       polysaccharide of the primary cell wall. RG-II is essential for the
CC       cell wall integrity of rapidly growing tissues such as roots and pollen
CC       tube growth and elongation. {ECO:0000269|PubMed:18755189}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=110 uM for UDP-xylose {ECO:0000269|PubMed:18755189};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed around trichome support cells in the
CC       adaxial epidermis of rosette leaves, in cauline leaves, petals and both
CC       the proximal and distal ends of siliques.
CC       {ECO:0000269|PubMed:18755189}.
CC   -!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
CC       {ECO:0000250|UniProtKB:Q9JI93}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:18755189}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 77 family.
CC       {ECO:0000305}.
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DR   EMBL; AC009323; AAG09108.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33406.1; -; Genomic_DNA.
DR   EMBL; AK117396; BAC42064.1; -; mRNA.
DR   EMBL; BT005111; AAO50644.1; -; mRNA.
DR   PIR; B96607; B96607.
DR   RefSeq; NP_176048.1; NM_104532.4.
DR   AlphaFoldDB; Q9FXA7; -.
DR   STRING; 3702.AT1G56550.1; -.
DR   CAZy; GT77; Glycosyltransferase Family 77.
DR   PaxDb; Q9FXA7; -.
DR   ProteomicsDB; 236902; -.
DR   EnsemblPlants; AT1G56550.1; AT1G56550.1; AT1G56550.
DR   GeneID; 842108; -.
DR   Gramene; AT1G56550.1; AT1G56550.1; AT1G56550.
DR   KEGG; ath:AT1G56550; -.
DR   Araport; AT1G56550; -.
DR   TAIR; locus:2027605; AT1G56550.
DR   eggNOG; ENOG502QT5X; Eukaryota.
DR   HOGENOM; CLU_051257_0_0_1; -.
DR   InParanoid; Q9FXA7; -.
DR   OrthoDB; 819015at2759; -.
DR   PhylomeDB; Q9FXA7; -.
DR   PRO; PR:Q9FXA7; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9FXA7; baseline and differential.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0035252; F:UDP-xylosyltransferase activity; IDA:TAIR.
DR   GO; GO:0010306; P:rhamnogalacturonan II biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR005069; Nucl-diP-sugar_transferase.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF03407; Nucleotid_trans; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW   Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..383
FT                   /note="UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferase
FT                   3"
FT                   /id="PRO_0000423715"
FT   TOPO_DOM        1..20
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        21..41
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        42..383
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           180..182
FT                   /note="DXD motif"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        157
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        301
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        306
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        357
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        364
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   383 AA;  43910 MW;  EC207CC6EE3E7DD2 CRC64;
     MAQQSQRPIS NRHISLLNRN GLILLLLLAL FVILGVFLPL TKSSLFMFPN TTSSSLSPSS
     SLSVSDWRDY SLAQAVKFVA KNETVIVCAV SYPFLPFLNN WLISISRQKH QEKVLVIAED
     YATLYKVNEK WPGHAVLIPP ALDPQSAHKF GSQGFFNLTS RRPQHLLNIL ELGYNVMYND
     VDMVWLQDPF DYLQGSYDAY FMDDMIAIKP LNHSHDLPPL SRSGVTYVCS CMIFLRSTDG
     GKLLMKTWVE EIQAQPWNNT QAKKPHDQPA FNRALHKTAN QVKVYLLPQS AFPSGGLYFR
     NETWVNETRG KHVIVHNNYI IGYDKKMKRF QDFSLWLVDD HALESPLGKL EIYQEQNTTT
     EGKNLTKIVR KQRKNRGKKH KLP
 
 
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