ID   RN28_PANGI              Reviewed;         238 AA.
AC   P83618; P83232; Q6RI81;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 2.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Ribonuclease-like storage protein;
DE   AltName: Full=Root 28 kDa major protein;
DE   Flags: Precursor;
OS   Panax ginseng (Korean ginseng).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Araliaceae; Panax.
OX   NCBI_TaxID=4054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Root;
RX   PubMed=15310073; DOI=10.1016/j.jplph.2004.01.001;
RA   Kim S.I., Kweon S.M., Kim E.A., Kim J.Y., Kim S., Yoo J.S., Park Y.M.;
RT   "Characterization of RNase-like major storage protein from the ginseng root
RT   by proteomic approach.";
RL   J. Plant Physiol. 161:837-845(2004).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 24-39, AND FUNCTION.
RC   TISSUE=Root {ECO:0000269|PubMed:12091100};
RX   PubMed=12091100; DOI=10.1016/s1096-4959(02)00070-2;
RA   Yoon J.Y., Ha B.H., Woo J.S., Lim Y.H., Kim K.H.;
RT   "Purification and characterization of a 28-kDa major protein from ginseng
RT   root.";
RL   Comp. Biochem. Physiol. 132B:551-557(2002).
RN   [3]
RP   PROTEIN SEQUENCE OF 25-40.
RC   TISSUE=Root;
RX   PubMed=12362331;
RX   DOI=10.1002/1615-9861(200209)2:9<1123::aid-prot1123>3.0.co;2-s;
RA   Lum J.H.-K., Fung K.-L., Cheung P.-Y., Wong M.-S., Lee C.-H., Kwok F.S.-L.,
RA   Leung M.C.-P., Hui P.-K., Lo S.C.-L.;
RT   "Proteome of oriental ginseng Panax ginseng C. A. Meyer and the potential
RT   to use it as an identification tool.";
RL   Proteomics 2:1123-1130(2002).
CC   -!- FUNCTION: May act as a storage protein providing a nitrogen source.
CC       Seems to have no RNase activity although it has conserved the active
CC       site residues. {ECO:0000269|PubMed:12091100,
CC       ECO:0000269|PubMed:15310073}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000303|PubMed:12091100, ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Root.
CC   -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
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DR   EMBL; AY496964; AAR88098.1; -; mRNA.
DR   AlphaFoldDB; P83618; -.
DR   SMR; P83618; -.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   GO; GO:0033897; F:ribonuclease T2 activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   CDD; cd01061; RNase_T2_euk; 1.
DR   Gene3D; 3.90.730.10; -; 1.
DR   InterPro; IPR033697; Ribonuclease_T2_eukaryotic.
DR   InterPro; IPR001568; RNase_T2-like.
DR   InterPro; IPR036430; RNase_T2-like_sf.
DR   InterPro; IPR018188; RNase_T2_His_AS_1.
DR   InterPro; IPR033130; RNase_T2_His_AS_2.
DR   PANTHER; PTHR11240; PTHR11240; 1.
DR   Pfam; PF00445; Ribonuclease_T2; 1.
DR   SUPFAM; SSF55895; SSF55895; 1.
DR   PROSITE; PS00530; RNASE_T2_1; 1.
DR   PROSITE; PS00531; RNASE_T2_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Signal; Storage protein.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:12091100"
FT   CHAIN           24..238
FT                   /note="Ribonuclease-like storage protein"
FT                   /id="PRO_0000030972"
FT   ACT_SITE        61
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        113
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        117
FT                   /evidence="ECO:0000250"
FT   DISULFID        76..120
FT                   /evidence="ECO:0000250"
FT   CONFLICT        25
FT                   /note="Missing (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        29
FT                   /note="W -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        29
FT                   /note="W -> K (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        34
FT                   /note="L -> K (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        36
FT                   /note="L -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   238 AA;  27340 MW;  8F786DC3249D1F88 CRC64;
     MRAIYIISVI IVSLSIFSWG GNARSDYPWA MFALRLQWPA GFCEVNNACD TKSLLNTFTI
     HGLYPYNAKG TPALYCDGTA FDVNSVSDFL AEMHLAWPSH ETNTEDIQFW EHEWKKHGRC
     SEALLKQTDY FRTALAFRKA FDIVGLLNQE GIYPNNDLYR PKMIKEAIKK HLNAVPEIDF
     TKNENSEYVL TDINVCVNQQ ATRFVDCPTD DATDDYRLKF VRLPSKMKFA DPRTNSII