GP1_SOLLC
ID GP1_SOLLC Reviewed; 630 AA.
AC Q40161; O04735;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Polygalacturonase-1 non-catalytic subunit beta;
DE AltName: Full=AroGP1;
DE AltName: Full=Polygalacturonase converter;
DE Short=PG converter;
DE Flags: Precursor;
GN Name=GP1;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 109-120; 160-171; 230-236
RP AND 243-252, PROPEPTIDES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INTERACTION WITH PG POLYPEPTIDES.
RC STRAIN=cv. Ailsa Craig; TISSUE=Fruit;
RX PubMed=1392611; DOI=10.2307/3869483;
RA Zheng L., Heupel R.C., DellaPenna D.;
RT "The beta subunit of tomato fruit polygalacturonase isoenzyme 1: isolation,
RT characterization, and identification of unique structural features.";
RL Plant Cell 4:1147-1156(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. VFNT Cherry;
RA Watson C.F., Schuchman B., Liu J., DellaPenna D.;
RT "Gene encoding tomato polygalacturonase 1 (PG1) beta subunit.";
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH PG2, AND TISSUE SPECIFICITY.
RX PubMed=6489331; DOI=10.1111/j.1432-1033.1984.tb08452.x;
RA Pressey R.;
RT "Purification and characterization of tomato polygalacturonase converter.";
RL Eur. J. Biochem. 144:217-221(1984).
RN [4]
RP INTERACTION WITH PG2, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX DOI=10.1007/BF00240897;
RA Pogson B.J., Brady C.J.;
RT "Accumulation of the beta-subunit of polygalacturonase 1 in normal and
RT mutant tomato fruit.";
RL Planta 191:71-78(1993).
RN [5]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=7827495; DOI=10.2307/3869948;
RA Watson C.F., Zheng L., DellaPenna D.;
RT "Reduction of tomato polygalacturonase beta subunit expression affects
RT pectin solubilization and degradation during fruit ripening.";
RL Plant Cell 6:1623-1634(1994).
RN [6]
RP DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RX PubMed=12232274; DOI=10.1104/pp.105.4.1189;
RA Zheng L., Watson C.F., DellaPenna D.;
RT "Differential expression of the two subunits of tomato polygalacturonase
RT isoenzyme 1 in wild-type and in tomato fruit.";
RL Plant Physiol. 105:1189-1195(1994).
RN [7]
RP FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=12232422; DOI=10.1104/pp.106.4.1461;
RA Moore T., Bennett A.B.;
RT "Tomato fruit polygalacturonase isozyme 1 -- characterization of the beta
RT subunit and its state of assembly in vivo.";
RL Plant Physiol. 106:1461-1469(1994).
CC -!- FUNCTION: Non-catalytic subunit of the polygalacturonase isozyme 1
CC (PG1). Necessary and sufficient to convert the polygalacturonase from
CC its monomeric form PG2 to its heterodimeric form PG1. Seems to limit
CC the depolymerization and solubilization of cell wall polyuronides
CC mediated by PG2 during ripening, probably by recruiting PG2 to form
CC PG1. {ECO:0000269|PubMed:12232422, ECO:0000269|PubMed:7827495}.
CC -!- SUBUNIT: Interacts with polygalacturonase-2 (isoenzymes PG2A and PG2B)
CC to form heterodimers called polygalacturonase-1 (PG1).
CC {ECO:0000269|PubMed:12232422, ECO:0000269|PubMed:1392611,
CC ECO:0000269|PubMed:6489331, ECO:0000269|Ref.4}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:12232274}. Secreted, cell wall
CC {ECO:0000269|PubMed:12232274}. Note=Associated to the cell wall.
CC -!- TISSUE SPECIFICITY: Mostly expressed in fruit pericarp. Also detected
CC at low levels in cell wall of roots, leaves and flowers (at protein
CC level). {ECO:0000269|PubMed:12232274, ECO:0000269|PubMed:12232422,
CC ECO:0000269|PubMed:1392611, ECO:0000269|PubMed:6489331,
CC ECO:0000269|Ref.4}.
CC -!- DEVELOPMENTAL STAGE: Expressed in ripening fruits from the 20th day
CC after anthesis and increase during the ripening (at protein level).
CC {ECO:0000269|PubMed:12232274, ECO:0000269|PubMed:1392611,
CC ECO:0000269|PubMed:7827495, ECO:0000269|Ref.4}.
CC -!- INDUCTION: Transiently repressed by ethylene.
CC {ECO:0000269|PubMed:12232274}.
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DR EMBL; M98466; AAA34181.1; -; mRNA.
DR EMBL; U63374; AAB39547.1; -; Genomic_DNA.
DR PIR; JQ1670; JQ1670.
DR RefSeq; NP_001234835.1; NM_001247906.1.
DR AlphaFoldDB; Q40161; -.
DR STRING; 4081.Solyc05g005560.2.1; -.
DR PaxDb; Q40161; -.
DR PRIDE; Q40161; -.
DR GeneID; 543991; -.
DR KEGG; sly:543991; -.
DR eggNOG; ENOG502QT2V; Eukaryota.
DR HOGENOM; CLU_011822_5_0_1; -.
DR InParanoid; Q40161; -.
DR OrthoDB; 724379at2759; -.
DR PhylomeDB; Q40161; -.
DR BioCyc; MetaCyc:MON-2524; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; Q40161; baseline and differential.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009835; P:fruit ripening; IEA:UniProtKB-KW.
DR InterPro; IPR004873; BURP_dom.
DR Pfam; PF03181; BURP; 1.
DR SMART; SM01045; BURP; 1.
DR PROSITE; PS51277; BURP; 1.
PE 1: Evidence at protein level;
KW Apoplast; Cell wall; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Fruit ripening; Glycoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..108
FT /evidence="ECO:0000269|PubMed:1392611"
FT /id="PRO_0000042959"
FT CHAIN 109..?397
FT /note="Polygalacturonase-1 non-catalytic subunit beta"
FT /id="PRO_0000042960"
FT PROPEP ?398..630
FT /id="PRO_0000042961"
FT DOMAIN 415..629
FT /note="BURP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00604"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 250
FT /note="E -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 630 AA; 68960 MW; 31D585305D216AFE CRC64;
MHTKIHLPPC ILLLLLFSLP SFNVVVGGDG ESGNPFTPKG YLIRYWKKQI SNDLPKPWFL
LNKASPLNAA QYATYTKLVA DQNALTTQLH TFCSSANLMC APDLSPSLEK HSGDIHFATY
SDKNFTNYGT NEPGIGVNTF KNYSEGENIP VNSFRRYGRG SPRDNKFDNY ASDGNVIDQS
FNSYSTSTAG GSGKFTNYAA NANDPNLHFT SYSDQGTGGV QKFTIYSQEA NAGDQYFKSY
GKNGNGANGE FVSYGNDTNV IGSTFTNYGQ TANGGDQKFT SYGFNGNVPE NHFTNYGAGG
NGPSETFNSY RDQSNVGDDT FTTYVKDANG GEANFTNYGQ SFNEGTDVFT TYGKGGNDPH
INFKTYGVNN TFKDYVKDTA TFSNYHNKTS QVLASLMEVN GGKKVNNRWV EPGKFFREKM
LKSGTIMPMP DIKDKMPKRS FLPRVIASKL PFSTSKIAEL KKIFHAGDES QVEKMIGDAL
SECERAPSAG ETKRCVNSAE DMIDFATSVL GRNVVVRTTE DTKGSNGNIM IGSVKGINGG
KVTKSVSCHQ TLYPYLLYYC HSVPKVRVYE ADILDPNSKV KINHGVAICH VDTSSWGPSH
GAFVALGSGP GKIEVCHWIF ENDMTWAIAD
