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OFT15_ARATH
ID   OFT15_ARATH             Reviewed;         652 AA.
AC   F4HYR4; O48796; Q67XL6;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=O-fucosyltransferase 15 {ECO:0000305};
DE            Short=O-FucT-15 {ECO:0000305};
DE            EC=2.4.1.- {ECO:0000305};
DE   AltName: Full=O-fucosyltransferase family protein {ECO:0000312|EMBL:ARJ31416.1};
GN   Name=OFUT15 {ECO:0000305};
GN   OrderedLocusNames=At1g62330 {ECO:0000312|Araport:AT1G62330};
GN   ORFNames=F24O1.5 {ECO:0000312|EMBL:AAF70834.1};
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].
RC   STRAIN=cv. Columbia;
RA   Zeng W., Gluza P., Heazlewood J.;
RT   "Arabidopsis glycosyltransferases: an update.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   GENE FAMILY, AND 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=22916179; DOI=10.1371/journal.pone.0042914;
RA   Neumetzler L., Humphrey T., Lumba S., Snyder S., Yeats T.H., Usadel B.,
RA   Vasilevski A., Patel J., Rose J.K., Persson S., Bonetta D.;
RT   "The FRIABLE1 gene product affects cell adhesion in Arabidopsis.";
RL   PLoS ONE 7:E42914-E42914(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).
RN   [9]
RP   WEB RESOURCE.
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).
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=AAF70834.1; 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; KY906052; ARJ31416.1; -; mRNA.
DR   EMBL; AC003113; AAF70834.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE33954.1; -; Genomic_DNA.
DR   EMBL; AK176802; BAD44565.1; -; mRNA.
DR   PIR; T01442; T01442.
DR   RefSeq; NP_176423.3; NM_104913.4.
DR   AlphaFoldDB; F4HYR4; -.
DR   IntAct; F4HYR4; 5.
DR   STRING; 3702.AT1G62330.1; -.
DR   iPTMnet; F4HYR4; -.
DR   PaxDb; F4HYR4; -.
DR   PRIDE; F4HYR4; -.
DR   ProteomicsDB; 250892; -.
DR   EnsemblPlants; AT1G62330.1; AT1G62330.1; AT1G62330.
DR   GeneID; 842531; -.
DR   Gramene; AT1G62330.1; AT1G62330.1; AT1G62330.
DR   KEGG; ath:AT1G62330; -.
DR   Araport; AT1G62330; -.
DR   TAIR; locus:2027129; AT1G62330.
DR   eggNOG; ENOG502QU78; Eukaryota.
DR   HOGENOM; CLU_018420_8_0_1; -.
DR   InParanoid; F4HYR4; -.
DR   OMA; RHLVGPF; -.
DR   OrthoDB; 526720at2759; -.
DR   PRO; PR:F4HYR4; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; F4HYR4; baseline and differential.
DR   GO; GO:0005768; C:endosome; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0000137; C:Golgi cis cisterna; HDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11299; O-FucT_plant; 1.
DR   InterPro; IPR024709; FucosylTrfase_pln.
DR   InterPro; IPR019378; GDP-Fuc_O-FucTrfase.
DR   Pfam; PF10250; O-FucT; 1.
DR   PIRSF; PIRSF009360; UCP009360; 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..652
FT                   /note="O-fucosyltransferase 15"
FT                   /id="PRO_0000442077"
FT   TRANSMEM        91..111
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000305"
FT   BINDING         426..428
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H488"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        464
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        546
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        607
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CONFLICT        105
FT                   /note="V -> I (in Ref. 4; BAD44565)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   652 AA;  73296 MW;  D47CADF1C299909D CRC64;
     MSSERPDEEK PETRDVLRVQ DLIHGGGGAS PVQSPTRLGP TRFSEVAGDK ILNTGSNCIG
     SVLSWINGDP NRNLKNPVKR AKRKRIRTAK TAAFVIVLVG FFIFVNWFML SQLHEGRAWL
     RRGFSKKTNL KPKLNPDPNS SVKRVSVKVS ANVQHKEKKK MGKPKKTYNG TYGRLLAYAA
     HALAEGQNKL EPKELWREPK DQALAWKPCA DQRSWKPSDG KNGYIMVTAN GGINQQRVAV
     CNIVVVARML NATLVIPKFM FSDVWTDASQ FGDIYQVEHF IKYLSPDIRI VKKLPKELQS
     LDLEAIGSVV TDIDVMKEAK PGFYMKHILP LLLKNRVVHF LGFGNRLAFD PIPFELQRLR
     CRCNFHALNF VPKIQETGAI LVRRLRDSGS HLAPVDPYLV GPKFASFILD KKAGPLHKAS
     KYLAVHLRFE IDMVAHSLCY FGGGDAEKAE LDAYREKHFP TLANLTKTQK MPSPDDLRTE
     GLCPLSPEEA VLMLAGLGFS RKTRVFVAGA NIYGGNKRLA ALTSLYPNLV TKENVLSQTE
     LEPFKNFSSQ LAVLDFIACA ASDAFAMTDS GSQLSSLVSG YRIYYGAGKM PTIRPNKRRF
     SDILLKNNTI EWKVFEQRVR KTVRQTKHVL VRPTGRSVYR YPRCKECMCN ED
 
 
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