ID   EGC_CITJA               Reviewed;         131 AA.
AC   Q9ZP41;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=EG45-like domain containing protein;
DE   AltName: Full=Blight-associated protein p12;
DE   AltName: Full=Plant natriuretic peptide;
DE            Short=PNP;
DE   Flags: Precursor;
GN   Name=CjBAp12;
OS   Citrus jambhiri (Rough lemon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=64884;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-59, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Root;
RX   PubMed=9862495; DOI=10.1023/a:1006039016393;
RA   Ceccardi T.L., Barthe G.A., Derrick K.S.;
RT   "A novel protein associated with citrus blight has sequence similarities to
RT   expansin.";
RL   Plant Mol. Biol. 38:775-783(1998).
RN   [2]
RP   FUNCTION.
RX   PubMed=11965432; DOI=10.1007/s00239-001-0055-4;
RA   Ludidi N.N., Heazlewood J.L., Seoighe C., Irving H.R., Gehring C.A.;
RT   "Expansin-like molecules: novel functions derived from common domains.";
RL   J. Mol. Evol. 54:587-594(2002).
CC   -!- FUNCTION: Might have a systemic role in water and solute homeostasis.
CC       Has no expansin-like activity. {ECO:0000269|PubMed:11965432}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in the outer layer of xylem and the
CC       vascular cambial zone of roots, in shoot cambium, but not in leaves.
CC       {ECO:0000269|PubMed:9862495}.
CC   -!- INDUCTION: By citrus blight. Not expressed in healthy plants.
CC   -!- MISCELLANEOUS: Accumulation of the protein in leaf tissues indicates a
CC       systemic mobility.
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DR   EMBL; AF015782; AAD03398.1; -; mRNA.
DR   AlphaFoldDB; Q9ZP41; -.
DR   SMR; Q9ZP41; -.
DR   GO; GO:0048046; C:apoplast; IEA:InterPro.
DR   GO; GO:0009627; P:systemic acquired resistance; IEA:InterPro.
DR   Gene3D; 2.40.40.10; -; 1.
DR   InterPro; IPR044206; EGC1/2.
DR   InterPro; IPR007112; Expansin/allergen_DPBB_dom.
DR   InterPro; IPR009009; RlpA-like_DPBB.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   PANTHER; PTHR47295; PTHR47295; 1.
DR   Pfam; PF03330; DPBB_1; 1.
DR   SMART; SM00837; DPBB_1; 1.
DR   SUPFAM; SSF50685; SSF50685; 1.
DR   PROSITE; PS50842; EXPANSIN_EG45; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..131
FT                   /note="EG45-like domain containing protein"
FT                   /id="PRO_5000053366"
FT   DOMAIN          27..131
FT                   /note="Expansin-like EG45; incomplete"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00079"
FT   DISULFID        73..85
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00079"
SQ   SEQUENCE   131 AA;  13600 MW;  61C8548CFC68A70F CRC64;
     MGVGTKVLVI TTMAICLISS AAYASEGTAT FYTPPYVPSA CNGYKNDGVM IAAASYAIWN
     NGAVCNKSFR VKCTGATNQG TPHPCRGGSV LVKIVDLCPA GCQATIDLSQ EAFSQIANPD
     AGKIKIEFNQ A