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OFUT5_ARATH
ID   OFUT5_ARATH             Reviewed;         564 AA.
AC   Q84WU0; Q9SHI5;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=O-fucosyltransferase 5 {ECO:0000305};
DE            Short=O-FucT-5 {ECO:0000305};
DE            EC=2.4.1.- {ECO:0000305};
DE   AltName: Full=O-fucosyltransferase family protein {ECO:0000305};
GN   Name=OFUT5 {ECO:0000305};
GN   Synonyms=GT68 {ECO:0000303|PubMed:23272088, ECO:0000312|EMBL:AHL38942.1};
GN   OrderedLocusNames=At1g17270 {ECO:0000312|Araport:AT1G17270};
GN   ORFNames=F20D23.3 {ECO:0000312|EMBL:AAD50008.1};
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=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   [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;
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   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   [6]
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   [7]
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAD50008.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=The Arabidopsis GT Collection;
CC       URL="http://gt.jbei.org/arabidopsis.html";
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DR   EMBL; KJ139002; AHL38942.1; -; mRNA.
DR   EMBL; AC007651; AAD50008.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE29566.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM60393.1; -; Genomic_DNA.
DR   EMBL; BT002770; AAO22598.1; -; mRNA.
DR   PIR; A86309; A86309.
DR   RefSeq; NP_001322684.1; NM_001332286.1.
DR   RefSeq; NP_173170.2; NM_101588.4.
DR   AlphaFoldDB; Q84WU0; -.
DR   SMR; Q84WU0; -.
DR   STRING; 3702.AT1G17270.1; -.
DR   iPTMnet; Q84WU0; -.
DR   PaxDb; Q84WU0; -.
DR   PRIDE; Q84WU0; -.
DR   ProteomicsDB; 250801; -.
DR   EnsemblPlants; AT1G17270.1; AT1G17270.1; AT1G17270.
DR   EnsemblPlants; AT1G17270.2; AT1G17270.2; AT1G17270.
DR   GeneID; 838298; -.
DR   Gramene; AT1G17270.1; AT1G17270.1; AT1G17270.
DR   Gramene; AT1G17270.2; AT1G17270.2; AT1G17270.
DR   KEGG; ath:AT1G17270; -.
DR   Araport; AT1G17270; -.
DR   TAIR; locus:2020432; AT1G17270.
DR   eggNOG; ENOG502QS4M; Eukaryota.
DR   HOGENOM; CLU_039118_0_0_1; -.
DR   InParanoid; Q84WU0; -.
DR   OMA; VEKKWVM; -.
DR   OrthoDB; 459621at2759; -.
DR   PhylomeDB; Q84WU0; -.
DR   PRO; PR:Q84WU0; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q84WU0; 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..564
FT                   /note="O-fucosyltransferase 5"
FT                   /id="PRO_0000442068"
FT   TRANSMEM        70..90
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000305"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         413..415
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT   BINDING         529..530
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT   CARBOHYD        129
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   564 AA;  63622 MW;  3B59E16A878B2AE1 CRC64;
     MVRNSSDEEE DHRNLIPQND TRDNDLNLRP DARTVNMANG GGRSPRSALQ IDEILSRARN
     RWKISVNKRY VVAAVSLTLF VGLLFLFTDT RTFFSSFKLD PMSSRVKESE LQALNLLRQQ
     QLALVSLLNR TNFNSSNAIS SSVVIDNVKA ALLKQISVNK EIEEVLLSPH RTGNYSITAS
     GSDSFTGSYN ADICRKVDQK LLDRKTIEWK PRPDKFLFAI CLSGQMSNHL ICLEKHMFFA
     ALLDRVLVIP SSKFDYQYDK VIDIERINTC LGRTVVISFD QFKEIDKKNN AHIDRFICYV
     SSPQPCYVDE DHIKKLKGLG VSIGGKLEAP WSEDIKKPTK RTSQEVVEKF KSDDGVIAIG
     DVFYADMEQD LVMQPGGPIN HKCKTLIEPS RLILVTAQRF IQTFLGKNFI SLHLRRHGFL
     KFCNAKSPSC FYPIPQAADC ISRMVERANA PVIYLSTDAA ESETGLLQSL VVVDGKVVPL
     VKRPPQNSAE KWDSLLYRHG IEDDSQVYAM LDKTICAMSS VFIGASGSTF TEDILRLRKD
     WGTSSMCDEY LCRGEEPNFI AENE
 
 
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