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OFT31_ARATH
ID   OFT31_ARATH             Reviewed;         519 AA.
AC   Q7Y030; Q9SB49;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=O-fucosyltransferase 31 {ECO:0000305};
DE            Short=O-FucT-31 {ECO:0000305};
DE            EC=2.4.1.- {ECO:0000305};
DE   AltName: Full=O-fucosyltransferase family protein {ECO:0000305};
GN   Name=OFUT31 {ECO:0000305};
GN   OrderedLocusNames=At4g24530 {ECO:0000312|Araport:AT4G24530};
GN   ORFNames=F22K18.270 {ECO:0000312|EMBL:CAA23010.1};
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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=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   [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 (JUL-2006) 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=CAA23010.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79363.1; 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; AL035356; CAA23010.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161561; CAB79363.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE84921.1; -; Genomic_DNA.
DR   EMBL; BT008775; AAP68214.1; -; mRNA.
DR   EMBL; AK227813; BAE99793.1; -; mRNA.
DR   PIR; T05581; T05581.
DR   RefSeq; NP_194184.2; NM_118586.4.
DR   AlphaFoldDB; Q7Y030; -.
DR   STRING; 3702.AT4G24530.1; -.
DR   PaxDb; Q7Y030; -.
DR   PRIDE; Q7Y030; -.
DR   ProteomicsDB; 250895; -.
DR   EnsemblPlants; AT4G24530.1; AT4G24530.1; AT4G24530.
DR   GeneID; 828555; -.
DR   Gramene; AT4G24530.1; AT4G24530.1; AT4G24530.
DR   KEGG; ath:AT4G24530; -.
DR   Araport; AT4G24530; -.
DR   TAIR; locus:2121909; AT4G24530.
DR   eggNOG; ENOG502QUG0; Eukaryota.
DR   HOGENOM; CLU_018420_8_2_1; -.
DR   InParanoid; Q7Y030; -.
DR   OMA; PTDRINT; -.
DR   OrthoDB; 459207at2759; -.
DR   PhylomeDB; Q7Y030; -.
DR   PRO; PR:Q7Y030; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q7Y030; baseline and differential.
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: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..519
FT                   /note="O-fucosyltransferase 31"
FT                   /id="PRO_0000442093"
FT   TRANSMEM        18..38
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000305"
FT   BINDING         302..304
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H488"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        373
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        474
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   519 AA;  58161 MW;  76967A236D247DC8 CRC64;
     MLQMKQPLQN LNQSQKTALA GVFVLLFPIL YPNLFSPLGR ASPSLFSEWN APRPRHLSLL
     QGALDRQISI RQQVELWSPL ADQGWKPCTE SYRGASLPEK SEGFLQVFLD GGLNQQRMGI
     CDAVAVAKIM NVTLVIPRLE VNTVWQDSSS FTDIFDLDHF ISVLKDEVRI VRELPIQYAW
     STRDYYATGI RATRIKTAPV HASAEWYLEN VLPIIQSYGI AAVAPFSHRL AFDNLPESIQ
     RLRCKVNFEA LNFVPHIREL GDALVHRLRN PPSSSQTSGT MDPTDRINTI VKAGAGKFAV
     LHLRFDKDMA AHSGCDFEGG KAEKLALAKY RQVIWQGRVL NSQFTDEELR NKGRCPLTPE
     EIGLLLSALG FSNNTRLYLA SHQVYGGEAR ISTLRKLFPG IENKKSLASA EELADVQGKA
     SLMAAVDYYV SMKSDIFISA SPGNMHNALQ AHRAYLNLKT IRPNMILLGQ VFVNKSLDWS
     EFEGAVMNGH KNRQGQLRLR KQKQSIYTYP APDCMCKVA
 
 
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