OFT19_ARATH
ID OFT19_ARATH Reviewed; 638 AA.
AC Q9SH89;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=O-fucosyltransferase 19 {ECO:0000305};
DE Short=O-FucT-19 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000305};
DE AltName: Full=O-fucosyltransferase family protein {ECO:0000305};
GN Name=OFUT19 {ECO:0000305};
GN OrderedLocusNames=At2g37980 {ECO:0000312|Araport:AT2G37980};
GN ORFNames=T8P21.11 {ECO:0000305};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 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 [5]
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 [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).
RN [8]
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 -!- WEB RESOURCE: Name=The Arabidopsis GT Collection;
CC URL="http://gt.jbei.org/arabidopsis.html";
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DR EMBL; CP002685; AEC09474.1; -; Genomic_DNA.
DR EMBL; AF360259; AAK25969.1; -; mRNA.
DR EMBL; BT001965; AAN71964.1; -; mRNA.
DR PIR; E84799; E84799.
DR RefSeq; NP_181334.1; NM_129355.2.
DR AlphaFoldDB; Q9SH89; -.
DR iPTMnet; Q9SH89; -.
DR PaxDb; Q9SH89; -.
DR PRIDE; Q9SH89; -.
DR ProteomicsDB; 239026; -.
DR EnsemblPlants; AT2G37980.1; AT2G37980.1; AT2G37980.
DR GeneID; 818376; -.
DR Gramene; AT2G37980.1; AT2G37980.1; AT2G37980.
DR KEGG; ath:AT2G37980; -.
DR Araport; AT2G37980; -.
DR TAIR; locus:2065563; AT2G37980.
DR eggNOG; ENOG502QQ4D; Eukaryota.
DR HOGENOM; CLU_018420_7_0_1; -.
DR InParanoid; Q9SH89; -.
DR OMA; NFFANPF; -.
DR OrthoDB; 476565at2759; -.
DR PhylomeDB; Q9SH89; -.
DR PRO; PR:Q9SH89; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SH89; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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.
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..638
FT /note="O-fucosyltransferase 19"
FT /id="PRO_0000442081"
FT TRANSMEM 134..154
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000305"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 394..396
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 638 AA; 72660 MW; 442BD50B9700D24D CRC64;
MSAAGASPLA VAPITAPTTT TRRRVGDSLE TTSERPSISS DYCNTNTVNI AISPDIDDGE
TGLQGGACSS PSSIGSSSSG SHYHHDHHYH HHPTIRYFLL RKLRLPFLFD GVGSTAVVGQ
GWWLCSGRNV GRRILGLLMI FVVVSLFLRV SLMSGRVVDH AHRRDLNELV VMRALHEDWS
MAQRAMTENV VIEKLPIPEI WQKPESGNYR QCASRPKNRS RLRRKTNGYL LVHANGGLNQ
MRTGICDMVA AAKIMNATLV LPLLDHESFW TDPSTFKDIF DWRHFMNVLK DDVDIVEYLP
PRYAAMRPLL KAPVSWSKAS YYRSEMLPLL KKHKVIKFTH TDSRLANNGL PPSIQRLRCR
ANYQALGYSK EIEDFGKVLV NRLRNNSEPF IALHLRYEKD MLAFTGCSHN LTAGEAEELR
IMRYNVKHWK EKEIDSRERR IQGGCPMSPR EAAIFLKAMG YPSSTTVYIV AGEIYGGNSM
DAFREEYPNV FAHSYLATEE ELEPFKPYQN RLAALDYIVA LESDVFVYTY DGNMAKAVQG
HRRFEGFKKT INPDRLNFVR LIDHLDEGVM SWDEFSSEVK RLHNNRIGAP YARLPGEFPR
LEENFYANPQ PDCICNKSQP EQLLKSRESD RWRKSASR
