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GLYT8_ARATH
ID   GLYT8_ARATH             Reviewed;         451 AA.
AC   B3H5R0; O80820;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Glycosyltransferase-like At2g41451 {ECO:0000305};
DE            EC=2.4.1.- {ECO:0000305};
DE   Flags: Precursor;
GN   OrderedLocusNames=At2g41451 {ECO:0000312|Araport:AT2G41451};
GN   ORFNames=T26J13 {ECO:0000312|EMBL:AAC23730.1};
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 {ECO:0000312|EMBL:AEC09983.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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   GENE FAMILY.
RC   STRAIN=cv. Columbia;
RX   PubMed=15010620; DOI=10.1023/b:plan.0000019067.05185.d6;
RA   Lertpiriyapong K., Sung Z.R.;
RT   "The elongation defective1 mutant of Arabidopsis is impaired in the gene
RT   encoding a serine-rich secreted protein.";
RL   Plant Mol. Biol. 53:581-595(2003).
RN   [4]
RP   GENE FAMILY.
RX   PubMed=14742875; DOI=10.1105/tpc.018077;
RA   Brocard-Gifford I., Lynch T.J., Garcia M.E., Malhotra B., Finkelstein R.R.;
RT   "The Arabidopsis thaliana ABSCISIC ACID-INSENSITIVE8 encodes a novel
RT   protein mediating abscisic acid and sugar responses essential for growth.";
RL   Plant Cell 16:406-421(2004).
CC   -!- FUNCTION: Involved in the coordination between cell elongation and
CC       cellulose synthesis by promoting the expression of genes involved in
CC       cell elongation and cellulose synthesis. Acts as a regulator of
CC       plasmodesmatal permeability. Maybe a glycosyltransferase.
CC       {ECO:0000250|UniProtKB:Q9C9Z9}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000250|UniProtKB:Q9C9Z9}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9C9Z9}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q9C9Z9}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 92 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC23730.1; Type=Erroneous gene model prediction;
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DR   EMBL; AC004625; AAC23730.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC09983.1; -; Genomic_DNA.
DR   PIR; T02440; T02440.
DR   RefSeq; NP_001118499.1; NM_001125027.2.
DR   AlphaFoldDB; B3H5R0; -.
DR   PaxDb; B3H5R0; -.
DR   PRIDE; B3H5R0; -.
DR   ProteomicsDB; 248533; -.
DR   EnsemblPlants; AT2G41451.1; AT2G41451.1; AT2G41451.
DR   GeneID; 6241352; -.
DR   Gramene; AT2G41451.1; AT2G41451.1; AT2G41451.
DR   KEGG; ath:AT2G41451; -.
DR   Araport; AT2G41451; -.
DR   TAIR; locus:4515102980; AT2G41451.
DR   eggNOG; ENOG502QPZC; Eukaryota.
DR   HOGENOM; CLU_032860_0_0_1; -.
DR   InParanoid; B3H5R0; -.
DR   OMA; CKPTRAD; -.
DR   OrthoDB; 431242at2759; -.
DR   PhylomeDB; B3H5R0; -.
DR   PRO; PR:B3H5R0; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; B3H5R0; baseline and differential.
DR   Genevisible; B3H5R0; AT.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0009505; C:plant-type cell wall; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0030244; P:cellulose biosynthetic process; IEA:InterPro.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   GO; GO:0009737; P:response to abscisic acid; IEA:InterPro.
DR   InterPro; IPR008166; Glyco_transf_92.
DR   InterPro; IPR044224; KOBITO1-like.
DR   PANTHER; PTHR46701; PTHR46701; 1.
DR   Pfam; PF01697; Glyco_transf_92; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cell membrane; Cell wall;
KW   Cell wall biogenesis/degradation; Cytoplasm; Developmental protein;
KW   Differentiation; Glycoprotein; Glycosyltransferase; Growth regulation;
KW   Membrane; Reference proteome; Secreted; Signal; Transferase.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..451
FT                   /note="Glycosyltransferase-like At2g41451"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000430757"
FT   DOMAIN          109..345
FT                   /note="GT92"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        441
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        444
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   451 AA;  52259 MW;  06AE697DD69BB064 CRC64;
     MASSDSSYSR KFLLITFLPL SLACLAFLLQ WRSGVNDSVT QWFDDNYPFP GMATVSEKRS
     LRSDSSCVSL LGQSRTQAFP YLRDLKLDHK PDLKPRICIT TSTSAGLEQT LPWIFYHKVI
     GVETFYLFVE GTAASPNVSR VLETIPGVNV IYRTRELEEE QAKSRIWNET WLEKFFYKPC
     NYELFVKQNL NMEMAITMAR DAGMDWILHL DTDELVHPSG TREYSLRNLL RDVPADVDEV
     IFTNYESSVE RDDIKEPFTE VSMFKKNFKH LPREVYYGNY KEATRGNPNY FLTYANGKSA
     ARIQDHLRPN GAHRWHNYKT YPNIKELDEA AILHYTYSKF SDLTSRRDRC GCKPTKKDVK
     RCFMLDFDRA AFIIASTSTS EEMLQWYRER VVWTDDNLIL KLLRKGILTR IYAPMVIIQE
     LREAGVFSSV VTSAHMSLSK NRSNSSTSSN Y
 
 
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