FUT12_ARATH
ID FUT12_ARATH Reviewed; 513 AA.
AC Q9FX97;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Putative fucosyltransferase-like protein;
DE AltName: Full=FucT2;
DE AltName: Full=FucTB;
DE AltName: Full=Fucosyltransferase 12;
DE Short=AtFUT12;
GN Name=FUT12; OrderedLocusNames=At1g49710; ORFNames=F14J22.8, F14J22_18;
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] (ISOFORMS LONG AND SHORT).
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=11420147; DOI=10.1016/s0304-4165(01)00151-9;
RA Wilson I.B., Rendic D., Freilinger A., Dumic J., Altmann F., Mucha J.,
RA Muller S., Hauser M.T.;
RT "Cloning and expression of cDNAs encoding alpha1,3-fucosyltransferase
RT homologues from Arabidopsis thaliana.";
RL Biochim. Biophys. Acta 1527:88-96(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC STRAIN=cv. Columbia; TISSUE=Silique;
RX PubMed=11696361; DOI=10.1016/s0014-5793(01)02999-4;
RA Bakker H., Schijlen E., de Vries T., Schiphorst W.E., Jordi W., Lommen A.,
RA Bosch D., van Die I.;
RT "Plant members of the alpha1-->3/4-fucosyltransferase gene family encode an
RT alpha1-->4-fucosyltransferase, potentially involved in Lewis(a)
RT biosynthesis, and two core alpha1-->3-fucosyltransferases.";
RL FEBS Lett. 507:307-312(2001).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
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).
CC -!- FUNCTION: May be involved in cell wall biosynthesis. May act as a
CC fucosyltransferase.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q9FX97-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q9FX97-2; Sequence=Not described;
CC -!- MISCELLANEOUS: [Isoform Short]: Unstable and lacks the key conserved
CC region and thus would presumably lack the catalytic activity.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000305}.
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DR EMBL; AJ404861; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AJ345085; CAC78980.1; -; mRNA.
DR EMBL; AC011807; AAG13053.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32462.1; -; Genomic_DNA.
DR EMBL; AY054522; AAK96713.1; -; mRNA.
DR EMBL; BT002570; AAO00930.1; -; mRNA.
DR PIR; F96533; F96533.
DR RefSeq; NP_175393.1; NM_103858.5. [Q9FX97-1]
DR AlphaFoldDB; Q9FX97; -.
DR BioGRID; 26619; 2.
DR STRING; 3702.AT1G49710.1; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR iPTMnet; Q9FX97; -.
DR PaxDb; Q9FX97; -.
DR PRIDE; Q9FX97; -.
DR ProteomicsDB; 230565; -. [Q9FX97-1]
DR EnsemblPlants; AT1G49710.1; AT1G49710.1; AT1G49710. [Q9FX97-1]
DR GeneID; 841394; -.
DR Gramene; AT1G49710.1; AT1G49710.1; AT1G49710. [Q9FX97-1]
DR KEGG; ath:AT1G49710; -.
DR Araport; AT1G49710; -.
DR TAIR; locus:2012217; AT1G49710.
DR eggNOG; KOG2619; Eukaryota.
DR HOGENOM; CLU_040484_0_0_1; -.
DR InParanoid; Q9FX97; -.
DR OMA; CEEWLMR; -.
DR PhylomeDB; Q9FX97; -.
DR BioCyc; ARA:AT1G49710-MON; -.
DR BioCyc; MetaCyc:AT1G49710-MON; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9FX97; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FX97; baseline and differential.
DR Genevisible; Q9FX97; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000138; C:Golgi trans 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:0046920; F:alpha-(1->3)-fucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008417; F:fucosyltransferase activity; ISS:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0036065; P:fucosylation; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.11660; -; 1.
DR InterPro; IPR001503; Glyco_trans_10.
DR InterPro; IPR038577; GT10-like_C_sf.
DR PANTHER; PTHR11929; PTHR11929; 1.
DR Pfam; PF00852; Glyco_transf_10; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..513
FT /note="Putative fucosyltransferase-like protein"
FT /id="PRO_0000221125"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..513
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 513 AA; 57308 MW; 2122AEDACBB0E4E5 CRC64;
MGVFSNLRGP RAGATHDEFP ATNGSPSSSS SPSSSIKRKL SNLLPLCVAL VVIAEIGFLG
RLDKVALVDT LTDFFTQSPS LSQSPPARSD RKKIGLFTDR SCEEWLMRED SVTYSRDFTK
DPIFISGGEK DFQWCSVDCT FGDSSGKTPD AAFGLGQKPG TLSIIRSMES AQYYPENDLA
QARRRGYDIV MTTSLSSDVP VGYFSWAEYD IMSPVQPKTE RAIAAAFISN CGARNFRLQA
LEALMKTNIK IDSYGGCHRN RDGKVDKVEA LKRYKFSLAF ENTNEEDYVT EKFFQSLVAG
SVPVVVGPPN IEEFAPASDS FLHIKTMEDV EPVAKRMKYL AANPAAYNQT LRWKYEGPSD
SFKALVDMAA VHSSCRLCIF LATRVREQEE ESPNFKKRPC KCSRGGSDTV YHVFVRERGR
FEMESVFLRG KSVTQEALES AVLAKFKSLK HEAVWKKERP GNLKGDKELK IHRIYPLGLT
QRQALYNFKF EGNSSLSSHI QNNPCAKFEV VFV
