FUT13_ARATH
ID FUT13_ARATH Reviewed; 401 AA.
AC Q9C8W3; Q8RYC1;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Alpha-(1,4)-fucosyltransferase;
DE EC=2.4.1.-;
DE AltName: Full=FT4-M;
DE AltName: Full=FucTC;
DE AltName: Full=Fucosyltransferase 13;
DE Short=AtFUT13;
DE AltName: Full=Galactoside 3(4)-L-fucosyltransferase;
GN Name=FUT13; OrderedLocusNames=At1g71990; ORFNames=F17M19.14;
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; 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 [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 [MRNA] OF 9-401.
RX PubMed=12070072; DOI=10.1093/glycob/12.5.299;
RA Leonard R., Costa G., Darrambide E., Lhernould S., Fleurat-Lessard P.,
RA Carlue M., Gomord V., Faye L., Maftah A.;
RT "The presence of Lewis a epitopes in Arabidopsis thaliana glycoconjugates
RT depends on an active alpha4-fucosyltransferase gene.";
RL Glycobiology 12:299-306(2002).
CC -!- FUNCTION: May be involved in cell wall synthesis. Catalyzes alpha-1,4
CC glycosidic linkages and generates Lewis-a epitopes.
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 -!- TISSUE SPECIFICITY: Present in root, stem, flower buds and green
CC siliques.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52222.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ404862; CAC38049.1; -; mRNA.
DR EMBL; AC021665; AAG52222.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE35261.1; -; Genomic_DNA.
DR EMBL; AY026941; AAK11728.1; -; mRNA.
DR PIR; H96742; H96742.
DR RefSeq; NP_177344.2; NM_105857.4.
DR AlphaFoldDB; Q9C8W3; -.
DR BioGRID; 28750; 1.
DR IntAct; Q9C8W3; 1.
DR STRING; 3702.AT1G71990.1; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR PaxDb; Q9C8W3; -.
DR PRIDE; Q9C8W3; -.
DR ProteomicsDB; 230538; -.
DR EnsemblPlants; AT1G71990.1; AT1G71990.1; AT1G71990.
DR GeneID; 843530; -.
DR Gramene; AT1G71990.1; AT1G71990.1; AT1G71990.
DR KEGG; ath:AT1G71990; -.
DR Araport; AT1G71990; -.
DR TAIR; locus:2016054; AT1G71990.
DR eggNOG; KOG2619; Eukaryota.
DR HOGENOM; CLU_062112_0_0_1; -.
DR InParanoid; Q9C8W3; -.
DR OMA; FRKWDSQ; -.
DR OrthoDB; 551308at2759; -.
DR PhylomeDB; Q9C8W3; -.
DR BioCyc; MetaCyc:GQT-3947-MON; -.
DR BRENDA; 2.4.1.214; 399.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9C8W3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8W3; baseline and differential.
DR Genevisible; Q9C8W3; AT.
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: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:0010493; P:Lewis a epitope biosynthetic process; IDA:TAIR.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.11660; -; 1.
DR InterPro; IPR017177; Alpha-1_3/4-FUT_pln.
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.
DR PIRSF; PIRSF037334; Alpha1_3/4FUT_pln; 1.
PE 2: Evidence at transcript level;
KW Cell wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..401
FT /note="Alpha-(1,4)-fucosyltransferase"
FT /id="PRO_0000221126"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..401
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 401 AA; 45098 MW; E2DB2B48550C36D6 CRC64;
MPMRYLNAMA ALLMMFFTLL ILSFTGILEF PSASTSMEHS IDPEPKLSDS TSDPFSDVLV
AYKKWDFEVG CARFRENHKD AILGNVSSGS LQEFGCGKLK MKHVKVLVKG WTWIPDNLEN
LYSCRCGMTC LWTKSSVLAD SPDALLFETT TPPLQRRVGD PLRVYMELEA GRKRSGREDI
FISYHAKDDV QTTYAGSLFH NNRNYHISPH KNNDVLVYWS SSRCLPHRDR LAKSLLDLIP
HHSFGKCLNN VGGLDSALSM YPECVAEHNA EAKWYDHLHC AMSHYKFVLA IENTAVESYV
TEKLFYALDS GSVPIYFGAS NVQDFVPPHS VIDGSKFGSM QELAAYVKRL GDDPVAYSEY
HAWRRCGLMG NYGKTRAVSL DTLPCRLCEE ISRRGGKNAG V