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FUT2_ARATH
ID   FUT2_ARATH              Reviewed;         539 AA.
AC   O81053; Q1PFA3;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=Fucosyltransferase 2;
DE            Short=AtFUT2;
DE            EC=2.4.1.-;
GN   Name=FUT2; OrderedLocusNames=At2g03210; ORFNames=T18E12.12;
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=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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
RN   [4]
RP   IDENTIFICATION AS A PUTATIVE FUCOSYLTRANSFERASE, AND TISSUE SPECIFICITY.
RX   PubMed=11743104; DOI=10.1104/pp.010596;
RA   Sarria R., Wagner T.A., O'Neill M.A., Faik A., Wilkerson C.G., Keegstra K.,
RA   Raikhel N.V.;
RT   "Characterization of a family of Arabidopsis genes related to xyloglucan
RT   fucosyltransferase1.";
RL   Plant Physiol. 127:1595-1606(2001).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA   Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT   thaliana.";
RL   J. Proteomics 72:439-451(2009).
CC   -!- FUNCTION: May be involved in cell wall biosynthesis. May act as a
CC       fucosyltransferase.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC       {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC       Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers,
CC       siliques and seedlings. {ECO:0000269|PubMed:11743104}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 37 family.
CC       {ECO:0000305}.
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DR   EMBL; AC005313; AAC34481.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05675.1; -; Genomic_DNA.
DR   EMBL; DQ446460; ABE65797.1; -; mRNA.
DR   PIR; T02705; T02705.
DR   RefSeq; NP_178420.1; NM_126372.1.
DR   AlphaFoldDB; O81053; -.
DR   SMR; O81053; -.
DR   STRING; 3702.AT2G03210.1; -.
DR   CAZy; GT37; Glycosyltransferase Family 37.
DR   PaxDb; O81053; -.
DR   PRIDE; O81053; -.
DR   ProteomicsDB; 230479; -.
DR   EnsemblPlants; AT2G03210.1; AT2G03210.1; AT2G03210.
DR   GeneID; 814850; -.
DR   Gramene; AT2G03210.1; AT2G03210.1; AT2G03210.
DR   KEGG; ath:AT2G03210; -.
DR   Araport; AT2G03210; -.
DR   TAIR; locus:2056901; AT2G03210.
DR   eggNOG; ENOG502QTTA; Eukaryota.
DR   HOGENOM; CLU_001992_2_1_1; -.
DR   InParanoid; O81053; -.
DR   OMA; EPDGCKY; -.
DR   PhylomeDB; O81053; -.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:O81053; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O81053; baseline and differential.
DR   Genevisible; O81053; AT.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008417; F:fucosyltransferase activity; ISS:TAIR.
DR   GO; GO:0008107; F:galactoside 2-alpha-L-fucosyltransferase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009969; P:xyloglucan biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR004938; XG_FTase.
DR   PANTHER; PTHR31889; PTHR31889; 1.
DR   Pfam; PF03254; XG_FTase; 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..539
FT                   /note="Fucosyltransferase 2"
FT                   /id="PRO_0000193911"
FT   TOPO_DOM        1..5
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        6..26
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        27..539
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        482
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   539 AA;  61571 MW;  5AEA7F45847DC67C CRC64;
     MRITEILALF MVLVPVSLVI VAMFGYDQGN GFVQASRFIT MEPNVTSSSD DSSLVQRDQE
     QKDSVDMSLL GGLLVSGFKK ESCLSRYQSY LYRKASPYKP SLHLLSKLRA YEELHKRCGP
     GTRQYTNAER LLKQKQTGEM ESQGCKYVVW MSFSGLGNRI ISIASVFLYA MLTDRVLLVE
     GGEQFADLFC EPFLDTTWLL PKDFTLASQF SGFGQNSAHC HGDMLKRKLI NESSVSSLSH
     LYLHLAHDYN EHDKMFFCEE DQNLLKNVPW LIMRTNNFFA PSLFLISSFE EELGMMFPEK
     GTVFHHLGRY LFHPSNQVWG LITRYYQAYL AKADERIGLQ IRVFDEKSGV SPRVTKQIIS
     CVQNENLLPR LSKGEEQYKQ PSEEELKLKS VLVTSLTTGY FEILKTMYWE NPTVTRDVIG
     IHQPSHEGHQ QTEKLMHNRK AWAEMYLLSL TDKLVISAWS TFGYVAQGLG GLRAWILYKQ
     ENQTNPNPPC GRAMSPDPCF HAPPYYDCKA KKGTDTGNVV PHVRHCEDIS WGLKLVDNF
 
 
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