RGP1_PEA
ID RGP1_PEA Reviewed; 364 AA.
AC O04300;
DT 09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Probable UDP-arabinopyranose mutase 1 {ECO:0000305};
DE EC=5.4.99.30 {ECO:0000250|UniProtKB:Q8H8T0};
DE AltName: Full=Reversibly glycosylated polypeptide 1 {ECO:0000303|PubMed:9207152};
DE Short=RGP1 {ECO:0000303|PubMed:9207152};
DE AltName: Full=UDP-L-arabinose mutase 1 {ECO:0000305};
DE AltName: Full=UDP-glucose:protein transglucosylase {ECO:0000305};
DE Short=UPTG {ECO:0000305};
GN Name=UPTG {ECO:0000305}; Synonyms=RGP1 {ECO:0000303|PubMed:9207152};
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888 {ECO:0000312|EMBL:AAB88408.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-37 AND 159-173,
RP FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RC STRAIN=cv. Early Alaska {ECO:0000269|PubMed:9207152};
RC TISSUE=Stem {ECO:0000312|EMBL:AAB88408.1};
RX PubMed=9207152; DOI=10.1073/pnas.94.14.7679;
RA Dhugga K.S., Tiwari S.C., Ray P.M.;
RT "A reversibly glycosylated polypeptide (RGP1) possibly involved in plant
RT cell wall synthesis: purification, gene cloning, and trans-Golgi
RT localization.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7679-7684(1997).
RN [2]
RP SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=1834664; DOI=10.1016/s0021-9258(18)54733-5;
RA Dhugga K.S., Ulvskov P., Gallagher S.R., Ray P.M.;
RT "Plant polypeptides reversibly glycosylated by UDP-glucose. Possible
RT components of Golgi beta-glucan synthase in pea cells.";
RL J. Biol. Chem. 266:21977-21984(1991).
CC -!- FUNCTION: Probable UDP-L-arabinose mutase involved in the biosynthesis
CC of cell wall non-cellulosic polysaccharides (By similarity). Was
CC initially shown to possess an autoglycosylating activity which is
CC dependent on the presence of UDP-glucose and manganese
CC (PubMed:9207152). {ECO:0000250|UniProtKB:Q8H8T0,
CC ECO:0000269|PubMed:9207152}.
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:Q8H8T0};
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 -!- ACTIVITY REGULATION: Inhibited by inhibitor protein (IP) which may be a
CC form of sucrose synthase. {ECO:0000250}.
CC -!- SUBUNIT: Homopentamer or homohexamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:9207152}.
CC Cell junction, plasmodesma {ECO:0000269|PubMed:9207152}. Golgi
CC apparatus {ECO:0000269|PubMed:9207152}. Note=Cell wall-associated, with
CC highest concentrations on plasmodesmata. Also located in the Golgi
CC apparatus. {ECO:0000269|PubMed:9207152}.
CC -!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
CC {ECO:0000250|UniProtKB:Q8H8T0}.
CC -!- PTM: Reversibly glycosylated by UDP-glucose, UDP-xylose and UDP-
CC galactose, but not UDP-mannose. {ECO:0000269|PubMed:1834664,
CC ECO:0000269|PubMed:9207152}.
CC -!- SIMILARITY: Belongs to the RGP family. {ECO:0000305}.
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DR EMBL; U31565; AAB88408.1; -; mRNA.
DR PIR; T06507; T06507.
DR AlphaFoldDB; O04300; -.
DR CAZy; GT75; Glycosyltransferase Family 75.
DR PRIDE; O04300; -.
DR EnsemblPlants; Psat2g132960.1; Psat2g132960.1.cds; Psat2g132960.
DR Gramene; Psat2g132960.1; Psat2g132960.1.cds; Psat2g132960.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; IDA:UniProtKB.
DR GO; GO:0052691; F:UDP-arabinopyranose mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0071669; P:plant-type cell wall organization or biogenesis; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IDA:UniProtKB.
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 junction; Cell wall; Cell wall biogenesis/degradation;
KW Cellulose biosynthesis; Direct protein sequencing; Glycoprotein;
KW Golgi apparatus; Isomerase; Secreted.
FT CHAIN 1..364
FT /note="Probable UDP-arabinopyranose mutase 1"
FT /id="PRO_0000221194"
FT MOTIF 103..105
FT /note="DXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q8H8T0"
FT SITE 151
FT /note="Required for activity"
FT /evidence="ECO:0000250|UniProtKB:Q8H8T0"
FT SITE 158
FT /note="Required for activity"
FT /evidence="ECO:0000250|UniProtKB:Q8H8T0"
FT CARBOHYD 151
FT /note="N-linked (Glc...) arginine"
FT /evidence="ECO:0000250|UniProtKB:P80607"
SQ SEQUENCE 364 AA; 41573 MW; 006F92870246DF2D CRC64;
MASLPKPTPL LKDELDIVIP TIRNLDFLEM WRPFFEQYHL IIVQDGDPSK VIKVPEGFDY
ELYNRNDINR ILGPKASCIS FKDSACRCFG YMVSKKKYIY TIDDDCFVAK DPTGHEINAL
EQHIKNLLSP STPFFFNTLY DPYREGTDFV RGYPFSLREG VPTAVSHGLW LNIPDYDAPT
QLVKPHERNT RFVDAVLTIP KGSLFPMCGM NLAFNRELIG PAMYFGLMGD GQPIGRYDDM
WAGWCIKVIC DHLGYGVKTG LPYIWHSKAS NPFVNLKKEY KGIFWQEEII PFFQAATLSK
DCTSVQKCYI ELSKQVKEKL GTIDPYFIKL ADAMVTWVEA WDEINNNKSE ETTSTKASEV
AATK
