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RGP4_ARATH
ID   RGP4_ARATH              Reviewed;         364 AA.
AC   Q9LUE6;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Probable UDP-arabinopyranose mutase 4 {ECO:0000305};
DE            EC=5.4.99.30 {ECO:0000250|UniProtKB:Q9SRT9};
DE   AltName: Full=Reversibly glycosylated polypeptide 4 {ECO:0000303|PubMed:21478444};
DE            Short=AtRGP4 {ECO:0000303|PubMed:21478444};
DE   AltName: Full=UDP-L-arabinose mutase 4 {ECO:0000305};
GN   Name=RGP4 {ECO:0000303|PubMed:21478444};
GN   OrderedLocusNames=At5g50750 {ECO:0000312|Araport:AT5G50750};
GN   ORFNames=MFB16.25 {ECO:0000312|EMBL:BAA96988.1};
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].
RA   Delgado I.J., Keegstra K., Raikhel N.V.;
RT   "Arabidopsis reversibly glycosylated polypeptides.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(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 [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   [5]
RP   SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=21478444; DOI=10.1105/tpc.111.083931;
RA   Rautengarten C., Ebert B., Herter T., Petzold C.J., Ishii T.,
RA   Mukhopadhyay A., Usadel B., Scheller H.V.;
RT   "The interconversion of UDP-L-arabinopyranose and UDP-L-arabinofuranose is
RT   indispensable for plant development in Arabidopsis.";
RL   Plant Cell 23:1373-1390(2011).
CC   -!- FUNCTION: Probable UDP-L-arabinose mutase involved in the biosynthesis
CC       of cell wall non-cellulosic polysaccharides.
CC       {ECO:0000250|UniProtKB:Q9SRT9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=UDP-beta-L-arabinofuranose = UDP-beta-L-arabinopyranose;
CC         Xref=Rhea:RHEA:28350, ChEBI:CHEBI:61457, ChEBI:CHEBI:61463;
CC         EC=5.4.99.30; Evidence={ECO:0000250|UniProtKB:Q9SRT9};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q8H8T0};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q8H8T0};
CC   -!- SUBUNIT: Heteromers with RGP1 and RGP2. {ECO:0000269|PubMed:21478444}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21478444}.
CC       Golgi apparatus {ECO:0000269|PubMed:21478444}. Note=Soluble and
CC       membrane-associated.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in developing seeds.
CC       {ECO:0000269|PubMed:21478444}.
CC   -!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
CC       {ECO:0000250|UniProtKB:Q8H8T0}.
CC   -!- PTM: Reversibly glycosylated in vitro by UDP-glucose, UDP-xylose and
CC       UDP-galactose, but not UDP-mannose. {ECO:0000250|UniProtKB:Q9SRT9}.
CC   -!- SIMILARITY: Belongs to the RGP family. {ECO:0000305}.
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DR   EMBL; AF329280; AAK60126.1; -; mRNA.
DR   EMBL; AB023037; BAA96988.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95988.1; -; Genomic_DNA.
DR   EMBL; BT004025; AAO42061.1; -; mRNA.
DR   EMBL; BT005194; AAO50727.1; -; mRNA.
DR   RefSeq; NP_199888.1; NM_124453.3.
DR   AlphaFoldDB; Q9LUE6; -.
DR   STRING; 3702.AT5G50750.1; -.
DR   CAZy; GT75; Glycosyltransferase Family 75.
DR   PaxDb; Q9LUE6; -.
DR   PRIDE; Q9LUE6; -.
DR   ProteomicsDB; 236936; -.
DR   DNASU; 835147; -.
DR   EnsemblPlants; AT5G50750.1; AT5G50750.1; AT5G50750.
DR   GeneID; 835147; -.
DR   Gramene; AT5G50750.1; AT5G50750.1; AT5G50750.
DR   KEGG; ath:AT5G50750; -.
DR   Araport; AT5G50750; -.
DR   TAIR; locus:2163305; AT5G50750.
DR   eggNOG; ENOG502QSDP; Eukaryota.
DR   HOGENOM; CLU_061976_0_0_1; -.
DR   InParanoid; Q9LUE6; -.
DR   OMA; NGLFWQE; -.
DR   OrthoDB; 662486at2759; -.
DR   PhylomeDB; Q9LUE6; -.
DR   BioCyc; ARA:AT5G50750-MON; -.
DR   PRO; PR:Q9LUE6; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LUE6; baseline and differential.
DR   Genevisible; Q9LUE6; AT.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0016866; F:intramolecular transferase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009832; P:plant-type cell wall biogenesis; IBA:GO_Central.
DR   GO; GO:0033356; P:UDP-L-arabinose metabolic process; IBA:GO_Central.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR004901; RGP.
DR   InterPro; IPR037595; RGP_fam.
DR   PANTHER; PTHR31682; PTHR31682; 1.
DR   Pfam; PF03214; RGP; 1.
DR   PIRSF; PIRSF016429; UPTG; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Cytoplasm; Glycoprotein; Golgi apparatus;
KW   Isomerase; Reference proteome.
FT   CHAIN           1..364
FT                   /note="Probable UDP-arabinopyranose mutase 4"
FT                   /id="PRO_0000410987"
FT   MOTIF           106..108
FT                   /note="DXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q8H8T0"
FT   SITE            154
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q8H8T0"
FT   SITE            161
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q8H8T0"
FT   CARBOHYD        154
FT                   /note="N-linked (Glc...) arginine"
FT                   /evidence="ECO:0000250|UniProtKB:P80607"
SQ   SEQUENCE   364 AA;  41866 MW;  65301D7E0AA3F01D CRC64;
     MAGYNLEAIE AAPLKDDLDI VIPTIRSLDF LEQWRPFLHH YHLIIVQDGD PSIKIRVPEG
     YDYELYNRND INRILGPRAN CISYKDGGCR CFGFMVSKKK YIYTIDDDCF VAKDPSGKDI
     NVIAQHIKNL ETPSTPHYFN TLYDPFRDGT DFVRGYPFSL REGVQTAISH GLWLNIPDYD
     APTQLVKPRE RNTRYVDAVM TIPKRVLYPM CGMNLAFNRE LVGPAMYFGL MGEGQPISRY
     DDMWAGWAAK VVCDHLGFGV KTGLPYLWHS KASNPFVNLK KEHKGLHWQE DMVPFFQNLR
     LSKESDTAAK CYMEISNMTK EKLTKVDPYF EKLADAMVVW IEAWEELNPP VKKKQSDGKD
     VKAK
 
 
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