ID   PLY18_SOLLC             Reviewed;         404 AA.
AC   P24396;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Probable pectate lyase P18;
DE            EC=4.2.2.2;
DE   AltName: Full=Style development-specific protein 9612;
DE   Flags: Precursor;
GN   Name=9612;
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].
RC   STRAIN=cv. VF36; TISSUE=Pistil;
RX   PubMed=2277637; DOI=10.1007/bf00271551;
RA   Budelier K.A., Smith A.G., Gasser C.S.;
RT   "Regulation of a stylar transmitting tissue-specific gene in wild-type and
RT   transgenic tomato and tobacco.";
RL   Mol. Gen. Genet. 224:183-192(1990).
CC   -!- FUNCTION: May have a role in the development of the transmitting tissue
CC       of the style and/or in the events related to pollination such as some
CC       aspect in the facilitation of compatible pollen tube growth.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan to give
CC         oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at
CC         their non-reducing ends.; EC=4.2.2.2;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion. Required for its activity. {ECO:0000250};
CC   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC       gluconate from pectin: step 2/5.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Predominantly found in the pistil where it is found
CC       in the outer five layers of the strands of transmitting tissue within
CC       the upper two-thirds of the style. Found at much lower levels in the
CC       anthers and vegetative organs.
CC   -!- DEVELOPMENTAL STAGE: Maximum levels are found during anthesis.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC       {ECO:0000305}.
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DR   EMBL; X55193; CAA38979.1; -; mRNA.
DR   PIR; S12209; S12209.
DR   RefSeq; NP_001234029.2; NM_001247100.2.
DR   AlphaFoldDB; P24396; -.
DR   SMR; P24396; -.
DR   STRING; 4081.Solyc02g093580.2.1; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   PaxDb; P24396; -.
DR   PRIDE; P24396; -.
DR   GeneID; 778293; -.
DR   KEGG; sly:778293; -.
DR   eggNOG; ENOG502QVCJ; Eukaryota.
DR   InParanoid; P24396; -.
DR   OrthoDB; 924221at2759; -.
DR   UniPathway; UPA00545; UER00824.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; P24396; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR018082; AmbAllergen.
DR   InterPro; IPR002022; Pec_lyase.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR045032; PEL.
DR   PANTHER; PTHR31683; PTHR31683; 1.
DR   Pfam; PF00544; Pectate_lyase_4; 1.
DR   PRINTS; PR00807; AMBALLERGEN.
DR   SMART; SM00656; Amb_all; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Glycoprotein; Lyase; Metal-binding; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..404
FT                   /note="Probable pectate lyase P18"
FT                   /id="PRO_0000024889"
FT   ACT_SITE        280
FT                   /evidence="ECO:0000255"
FT   BINDING         200
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   404 AA;  44298 MW;  B26ED69B128D8675 CRC64;
     MSTLFFTFSL LLLAPLLVIS SIQDPELVVQ DVHRSINASL TRRNLGYLSC GSGNPIDRLL
     AMQPQLGKKS PAFSYCAIGF GKNAIGGKNG RIYVVTDSGN DDPVNPKPGT LRHAVIQDEP
     LWIIFKRDMV IQLKQELVMN SYKTIDGRGA SVHISGGPCI TIHHTSNIII HGINIHDCKQ
     SGNGNIRDSP NHSGWWDVSD GDGISIFGGK NIWVDHCSLS NCHDGLIDAI HGSTAITISN
     NYFTHHDKVM LLGHSDSFTQ DKGMQVTVAF NHFGEGLVQR MPRCRHGYFH VVNNDYTHWE
     MYAIGGSAAP TINSQGNRFL APNEKYRKEV TKHEDAPESQ WRSWNWRSEG DLMLNGAYFR
     QTGAGASSSS TYARASSLSA RPSSLVGSIT TNAGPVNCKK GSRC