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OFT14_ARATH
ID   OFT14_ARATH             Reviewed;         563 AA.
AC   Q501D6; Q0WQ13; Q9C8N1;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=O-fucosyltransferase 14 {ECO:0000305};
DE            Short=O-FucT-14 {ECO:0000305};
DE            EC=2.4.1.- {ECO:0000305};
DE   AltName: Full=O-fucosyltransferase family protein {ECO:0000305};
GN   Name=OFUT14 {ECO:0000305};
GN   Synonyms=GT68 {ECO:0000303|PubMed:23272088, ECO:0000312|EMBL:AHL38903.1};
GN   OrderedLocusNames=At1g53770 {ECO:0000312|Araport:AT1G53770};
GN   ORFNames=F22G10.23 {ECO:0000312|EMBL:AAG51963.1},
GN   T18A20.22 {ECO:0000312|EMBL:AC009324};
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   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 (JUL-2006) 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=Additional isoforms seem to exist. {ECO:0000305};
CC       Name=1;
CC         IsoId=Q501D6-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the glycosyltransferase GT106 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG51963.1; 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; KJ138963; AHL38903.1; -; mRNA.
DR   EMBL; AC009324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC024260; AAG51963.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE32995.1; -; Genomic_DNA.
DR   EMBL; BT022031; AAY25443.1; -; mRNA.
DR   EMBL; AK228897; BAF00786.1; -; mRNA.
DR   RefSeq; NP_175780.1; NM_104254.4. [Q501D6-1]
DR   AlphaFoldDB; Q501D6; -.
DR   STRING; 3702.AT1G53770.2; -.
DR   EnsemblPlants; AT1G53770.1; AT1G53770.1; AT1G53770. [Q501D6-1]
DR   GeneID; 841814; -.
DR   Gramene; AT1G53770.1; AT1G53770.1; AT1G53770. [Q501D6-1]
DR   KEGG; ath:AT1G53770; -.
DR   Araport; AT1G53770; -.
DR   eggNOG; ENOG502QS4M; Eukaryota.
DR   HOGENOM; CLU_039118_0_0_1; -.
DR   PhylomeDB; Q501D6; -.
DR   PRO; PR:Q501D6; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q501D6; 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   Alternative splicing; Carbohydrate metabolism; Fucose metabolism;
KW   Glycoprotein; Glycosyltransferase; Membrane; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..563
FT                   /note="O-fucosyltransferase 14"
FT                   /id="PRO_0000442076"
FT   TRANSMEM        73..93
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000305"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         412..414
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT   BINDING         528..529
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2G5"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        339
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CONFLICT        265
FT                   /note="C -> Y (in Ref. 5; BAF00786)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   563 AA;  63943 MW;  3BE60071AA2A872E CRC64;
     MVKVSSSTTS SSSSSSPDEE SDLQNLLEES DSQIDQFRIS DEAAEQRPTF DVESLRSRLR
     RSFKLNLTKK QSIFIFLPIV IILIYLSTDF SNYFSVKVPN SAFRSNTLTG RVHESDLQAL
     YLLRKQESDL FSIWNHTVSN LSTIDDVKSA VFRQISLNRQ IQNALLSPHK TGNVDIGGSS
     DGYFAGGSCR KVDQKLNGRK TIQWKPRPDK FLFAICLSGQ MSNHLICLEK HMFFAALLKR
     VLVIPSHRFD YHYSRIIDID RINTCLGRTV VVSFEEFWKK DKNRKKHHHV HINRFICYFS
     KPEPCYVDKE HITKLKALGI TVGGKLDTPW EEDIARPSNK TAEEVEANFR SDDDVIAIGD
     VFYANVEREW VMQPGGPVAH KCRTLIEPNR LILLTAQRFI QTFLGKNYIA LHFRRHGFLK
     FCNAKNPSCF FPIPQAASCI TRLIEKVEAP VLYLSTDAAE SETGLLQSLL ILNGKTVPLV
     KRPARDSAEK WDALLYRHGL EGDSQVEAML DKTICALSSV FIGASGSTFT EDILRLRKDW
     GTASECDEYL CANEQPNFIA DHE
 
 
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