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OFT36_ARATH
ID   OFT36_ARATH             Reviewed;         566 AA.
AC   Q9FK30; Q8L9A2;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=O-fucosyltransferase 36 {ECO:0000305};
DE            Short=O-FucT-36 {ECO:0000305};
DE            EC=2.4.1.- {ECO:0000305};
DE   AltName: Full=O-fucosyltransferase family protein {ECO:0000305};
GN   Name=OFUT36 {ECO:0000305};
GN   Synonyms=GT68 {ECO:0000303|PubMed:23272088, ECO:0000312|EMBL:AHL38584.1};
GN   OrderedLocusNames=At5g50420 {ECO:0000312|Araport:AT5G50420};
GN   ORFNames=MXI22.14 {ECO:0000312|EMBL:BAB09461.1};
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND WEB RESOURCE.
RC   STRAIN=cv. Columbia;
RX   PubMed=24905498; DOI=10.1111/tpj.12577;
RA   Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA   Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA   Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA   Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA   Loque D., Scheller H.V., Heazlewood J.L.;
RT   "The plant glycosyltransferase clone collection for functional genomics.";
RL   Plant J. 79:517-529(2014).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   REVIEW.
RX   PubMed=22629278; DOI=10.3389/fpls.2012.00059;
RA   Hansen S.F., Harholt J., Oikawa A., Scheller H.V.;
RT   "Plant glycosyltransferases beyond CAZy: a perspective on DUF families.";
RL   Front. Plant Sci. 3:59-59(2012).
RN   [7]
RP   GENE FAMILY.
RX   PubMed=23272088; DOI=10.1371/journal.pone.0051129;
RA   Voxeur A., Andre A., Breton C., Lerouge P.;
RT   "Identification of putative rhamnogalacturonan-II specific
RT   glycosyltransferases in Arabidopsis using a combination of bioinformatics
RT   approaches.";
RL   PLoS ONE 7:E51129-E51129(2012).
RN   [8]
RP   GENE FAMILY.
RX   PubMed=22966747; DOI=10.1111/tpj.12019;
RA   Wang Y., Mortimer J.C., Davis J., Dupree P., Keegstra K.;
RT   "Identification of an additional protein involved in mannan biosynthesis.";
RL   Plant J. 73:105-117(2013).
CC   -!- PATHWAY: Glycan metabolism. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase GT106 family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=The Arabidopsis GT Collection;
CC       URL="http://gt.jbei.org/arabidopsis.html";
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DR   EMBL; KJ138644; AHL38584.1; -; mRNA.
DR   EMBL; AB012248; BAB09461.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95941.1; -; Genomic_DNA.
DR   EMBL; BT030356; ABO38769.1; -; mRNA.
DR   EMBL; AY088561; AAM66093.1; -; mRNA.
DR   RefSeq; NP_199853.1; NM_124424.4.
DR   AlphaFoldDB; Q9FK30; -.
DR   SMR; Q9FK30; -.
DR   STRING; 3702.AT5G50420.1; -.
DR   iPTMnet; Q9FK30; -.
DR   PaxDb; Q9FK30; -.
DR   PRIDE; Q9FK30; -.
DR   ProteomicsDB; 250799; -.
DR   EnsemblPlants; AT5G50420.1; AT5G50420.1; AT5G50420.
DR   GeneID; 835110; -.
DR   Gramene; AT5G50420.1; AT5G50420.1; AT5G50420.
DR   KEGG; ath:AT5G50420; -.
DR   Araport; AT5G50420; -.
DR   TAIR; locus:2177492; AT5G50420.
DR   eggNOG; ENOG502QS4M; Eukaryota.
DR   HOGENOM; CLU_039118_0_0_1; -.
DR   InParanoid; Q9FK30; -.
DR   OMA; ANLYERC; -.
DR   OrthoDB; 459621at2759; -.
DR   PRO; PR:Q9FK30; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FK30; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046922; F:peptide-O-fucosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR019378; GDP-Fuc_O-FucTrfase.
DR   InterPro; IPR045130; OFUT2-like.
DR   PANTHER; PTHR13398; PTHR13398; 1.
DR   Pfam; PF10250; O-FucT; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Fucose metabolism; Glycoprotein;
KW   Glycosyltransferase; Membrane; Reference proteome; Signal-anchor;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..566
FT                   /note="O-fucosyltransferase 36"
FT                   /id="PRO_0000442098"
FT   TRANSMEM        66..86
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000305"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         415..417
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT   BINDING         531..532
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        129
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CONFLICT        233
FT                   /note="I -> L (in Ref. 5; AAM66093)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   566 AA;  64411 MW;  96523115A0F72411 CRC64;
     MERNSSDDEE DHQHLIPQND TRIRHREDSV SSNATTIGGN QRSAFQIDDI LHRVQHRGKI
     SLNKRYVIVF VSLIISIGLL FLLTDPRELF AANFSSFKLD PLSNRVKESE LRALYLLRQQ
     QLALLSLWNG TLVNPSLNQS ENALGSSVLF EDVKSAVSKQ ISLNKEIQEV LLSPHRSSNY
     SGGTDVDSVN FSYNRCRKVD QKLSDRKTVE WKPRSDKFLF AICLSGQMSN HLICLEKHMF
     FAALLDRVLV IPSSKFDYQY DRVIDIERIN TCLGRNVVVA FDQFKEKAKK NHFRIDRFIC
     YFSSPQLCYV DEEHIKKLKG LGISIDGKLE APWSEDIKKP SKRTVQDVQM KFKSDDDVIA
     IGDVFYADME QDWVMQPGGP INHKCKTLIE PSKLILLTAQ RFIQTFLGKN FIALHFRRHG
     FLKFCNAKSP SCFYPIPQAA ECIARIVERS NGAVIYLSTD AAESETSLLQ SLVVVDGKIV
     PLVKRPPRNS AEKWDALLYR HGIEDDSQVD AMLDKTICAM SSVFIGASGS TFTEDILRLR
     KDWGTSSTCD EYLCRGEEPN FIAEDE
 
 
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