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   24-JAN-2024, entry version 87.
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=10.1105/tpc.4.9.1147;
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=10.1105/tpc.6.11.1623;
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.Q40161; -.
DR   GlyCosmos; Q40161; 6 sites, No reported glycans.
DR   PaxDb; 4081-Solyc05g005560-2-1; -.
DR   GeneID; 543991; -.
DR   KEGG; sly:543991; -.
DR   eggNOG; ENOG502QT2V; Eukaryota.
DR   HOGENOM; CLU_011822_5_0_1; -.
DR   InParanoid; Q40161; -.
DR   OrthoDB; 1208871at2759; -.
DR   PhylomeDB; Q40161; -.
DR   BioCyc; MetaCyc:MONOMER-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   PANTHER; PTHR31458; POLYGALACTURONASE 1 BETA-LIKE PROTEIN 2; 1.
DR   PANTHER; PTHR31458:SF2; POLYGALACTURONASE 1 BETA-LIKE PROTEIN 2; 1.
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
//