FUT4_ARATH
ID FUT4_ARATH Reviewed; 535 AA.
AC Q9SJP2;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Probable fucosyltransferase 4;
DE Short=AtFUT4;
DE EC=2.4.1.-;
GN Name=FUT4; OrderedLocusNames=At2g15390; ORFNames=F26H6.9;
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] (ISOFORM 2).
RX PubMed=11743104; DOI=10.1104/pp.010596;
RA Sarria R., Wagner T.A., O'Neill M.A., Faik A., Wilkerson C.G., Keegstra K.,
RA Raikhel N.V.;
RT "Characterization of a family of Arabidopsis genes related to xyloglucan
RT fucosyltransferase1.";
RL Plant Physiol. 127:1595-1606(2001).
RN [2]
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 [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).
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=1;
CC IsoId=Q9SJP2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SJP2-2; Sequence=VSP_041309, VSP_041310;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers,
CC siliques and seedlings.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 37 family.
CC {ECO:0000305}.
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DR EMBL; AF417474; AAL50623.1; -; mRNA.
DR EMBL; AC006920; AAD22285.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06395.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06396.1; -; Genomic_DNA.
DR PIR; D84528; D84528.
DR RefSeq; NP_179141.1; NM_127099.3. [Q9SJP2-2]
DR RefSeq; NP_973468.2; NM_201739.3. [Q9SJP2-1]
DR AlphaFoldDB; Q9SJP2; -.
DR SMR; Q9SJP2; -.
DR STRING; 3702.AT2G15390.2; -.
DR CAZy; GT37; Glycosyltransferase Family 37.
DR PaxDb; Q9SJP2; -.
DR PRIDE; Q9SJP2; -.
DR ProteomicsDB; 230048; -. [Q9SJP2-1]
DR EnsemblPlants; AT2G15390.1; AT2G15390.1; AT2G15390. [Q9SJP2-2]
DR EnsemblPlants; AT2G15390.2; AT2G15390.2; AT2G15390. [Q9SJP2-1]
DR GeneID; 816031; -.
DR Gramene; AT2G15390.1; AT2G15390.1; AT2G15390. [Q9SJP2-2]
DR Gramene; AT2G15390.2; AT2G15390.2; AT2G15390. [Q9SJP2-1]
DR KEGG; ath:AT2G15390; -.
DR Araport; AT2G15390; -.
DR TAIR; locus:2047208; AT2G15390.
DR eggNOG; ENOG502SC60; Eukaryota.
DR InParanoid; Q9SJP2; -.
DR OMA; SIGECRY; -.
DR OrthoDB; 364119at2759; -.
DR BioCyc; ARA:AT2G15390-MON; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9SJP2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJP2; baseline and differential.
DR Genevisible; Q9SJP2; AT.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031127; F:alpha-(1,2)-fucosyltransferase activity; IGI:TAIR.
DR GO; GO:0008417; F:fucosyltransferase activity; IMP:TAIR.
DR GO; GO:0008107; F:galactoside 2-alpha-L-fucosyltransferase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009969; P:xyloglucan biosynthetic process; IBA:GO_Central.
DR InterPro; IPR004938; XG_FTase.
DR PANTHER; PTHR31889; PTHR31889; 1.
DR Pfam; PF03254; XG_FTase; 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..535
FT /note="Probable fucosyltransferase 4"
FT /id="PRO_0000193913"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..535
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..32
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11743104"
FT /id="VSP_041309"
FT VAR_SEQ 33..54
FT /note="LSVMLLSFSNNFNNKLFAATIN -> MFCHSLLAQRILLLTFFFVICS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:11743104"
FT /id="VSP_041310"
SQ SEQUENCE 535 AA; 61484 MW; BEC5C005D3632535 CRC64;
MYHIFQISGE VIKGLGLKTK ILITIVFSTL LILSVMLLSF SNNFNNKLFA ATINDESETP
GRDRLIGGLL TADFDEGSCL SRYHKTFLYR KPSPYKPSEY LVSKLRSYEM LHKRCGPGTK
AYKEATKHLS HDENYNASKS DGECRYVVWL ADYGLGNRLL TLASVFLYAL LTDRIILVDN
RKDIGDLLCE PFPGTSWLLP LDFPLMKYAD GYHKGYSRCY GTMLENHSIN STSFPPHLYM
HNLHDSRDSD KMFFCQKDQS LIDKVPWLIF RANVYFVPSL WFNPTFQTEL TKLFPQKETV
FHHLGRYLFH PKNQVWDIVT KYYHDHLSKA DERLGIQIRV FRDQGGYYQH VMDQVISCTQ
REKLLPELAT QEESKVNISN IPKSKAVLVT SLSPEYSKKL ENMFSERANM TGEIIKVYQP
SGERYQQTDK KVHDQKALAE MYLLSLTDNI VASSRSTFGY VAYSLGGLKP WLLYLPNDNK
APDPPCVRST SMEPCFLTPP THGCEPDAWG TESGKVVPFV RYCEDIWGLK LFDEL
