F8H_ARATH
ID F8H_ARATH Reviewed; 469 AA.
AC Q6NMM8; Q9FFB4;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Probable glucuronoxylan glucuronosyltransferase F8H;
DE EC=2.4.1.-;
DE AltName: Full=FRA8 homolog;
DE AltName: Full=Protein FRAGILE FIBER 8 homolog;
GN Name=F8H; OrderedLocusNames=At5g22940; ORFNames=MRN17.17;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19224953; DOI=10.1093/pcp/pcp025;
RA Lee C., Teng Q., Huang W., Zhong R., Ye Z.H.;
RT "The F8H glycosyltransferase is a functional paralog of FRA8 involved in
RT glucuronoxylan biosynthesis in Arabidopsis.";
RL Plant Cell Physiol. 50:812-827(2009).
CC -!- FUNCTION: Involved in the synthesis of the hemicellulose
CC glucuronoxylan, a major component of secondary cell walls. Probably
CC involved in the synthesis of the glycosyl sequence at the
CC glucuronoxylan reducing end. {ECO:0000269|PubMed:19224953}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:19224953}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:19224953}.
CC -!- TISSUE SPECIFICITY: Expressed in xylem cells in stems and in roots.
CC {ECO:0000269|PubMed:19224953}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:19224953}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10615.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB005243; BAB10615.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93099.1; -; Genomic_DNA.
DR EMBL; BT011629; AAS47635.1; -; mRNA.
DR EMBL; BT014962; AAT47813.1; -; mRNA.
DR RefSeq; NP_001330046.1; NM_001343782.1.
DR RefSeq; NP_197685.2; NM_122200.4.
DR AlphaFoldDB; Q6NMM8; -.
DR SMR; Q6NMM8; -.
DR STRING; 3702.AT5G22940.1; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR PaxDb; Q6NMM8; -.
DR PRIDE; Q6NMM8; -.
DR EnsemblPlants; AT5G22940.1; AT5G22940.1; AT5G22940.
DR GeneID; 832358; -.
DR Gramene; AT5G22940.1; AT5G22940.1; AT5G22940.
DR KEGG; ath:AT5G22940; -.
DR Araport; AT5G22940; -.
DR TAIR; locus:2172676; AT5G22940.
DR eggNOG; KOG1021; Eukaryota.
DR HOGENOM; CLU_039682_1_0_1; -.
DR InParanoid; Q6NMM8; -.
DR OMA; HIFVAAH; -.
DR OrthoDB; 789556at2759; -.
DR PhylomeDB; Q6NMM8; -.
DR PRO; PR:Q6NMM8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q6NMM8; baseline and differential.
DR Genevisible; Q6NMM8; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0010417; P:glucuronoxylan biosynthetic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR InterPro; IPR004263; Exostosin.
DR InterPro; IPR040911; Exostosin_GT47.
DR PANTHER; PTHR11062; PTHR11062; 1.
DR Pfam; PF03016; Exostosin; 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..469
FT /note="Probable glucuronoxylan glucuronosyltransferase F8H"
FT /id="PRO_0000407575"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..469
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 469 AA; 53809 MW; 13B860CA19D1F729 CRC64;
MSLDIKKPNI TKTKKKKTGF VVKMQLNNNR GGNKRNIFIF FFFRNYYTWI LWFCLSLYFF
TSYFSVEDQS SPSSIRLLSN HKTSSSLPSR ALIESSAIKT TSIGLFTGMK IYVYDLPASY
NDDWVTASDR CASHLFAAEV AIHRALLSSD VRTLDPDEAD YFFVPVYVSC NFSTSNGFPS
LSHARSLLSS AVDFLSDHYP FWNRSQGSDH VFVASHDFGA CFHAMEDMAI EEGIPKFMKR
SIILQTFGVK YKHPCQEVEH VVIPPYIPPE SVQKAIEKAP VNGRRDIWAF FRGKMEVNPK
NISGRFYSKG VRTAILKKFG GRRRFYLNRH RFAGYRSEIV RSVFCLCPLG WAPWSPRLVE
SAVLGCVPVV IADGIQLPFS ETVQWPEISL TVAEKDVRNL RKVLEHVAAT NLSAIQRNLH
EPVFKRALLY NVPMKEGDAT WHILESLWRK LDDRSYRRSR VLSQREVDM
