RNS1_PANGI
ID RNS1_PANGI Reviewed; 154 AA.
AC P80889; Q9S9I2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Ribonuclease 1;
DE EC=3.1.-.-;
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 PROTEIN SEQUENCE.
RC STRAIN=cv. R1; TISSUE=Callus;
RX PubMed=9166900; DOI=10.1016/s0014-5793(97)00337-2;
RA Moiseyev G.P., Fedoreyeva L.I., Zhuravlev Y.N., Yasnetskaya E.G.,
RA Jekel P.A., Beintema J.J.;
RT "Primary structures of two ribonucleases from ginseng calluses. New members
RT of the PR-10 family of intracellular pathogenesis-related plant proteins.";
RL FEBS Lett. 407:207-210(1997).
RN [2]
RP PROTEIN SEQUENCE OF 1-20 AND 68-87.
RX PubMed=7764876; DOI=10.1007/bf00201828;
RA Moiseyev G.P., Beintema J.J., Fedoreyeva L.I., Yakovlev G.I.;
RT "High sequence similarity between a ribonuclease from ginseng calluses and
RT fungus-elicited proteins from parsley indicates that intracellular
RT pathogenesis-related proteins are ribonucleases.";
RL Planta 193:470-472(1994).
RN [3]
RP PROTEIN SEQUENCE OF 7-22.
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).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RA Yasnetskaya E.G., Bulgakov V.P., Gorbach V.I., Shevchenko N.M.,
RA Fedoreyeva L.I., Zhuravlev Y.N., Kiselev K.V.;
RT "Ethephon- and jasmonate-elicited pathogenesis-related ribonucleases in
RT cultured ginseng cells.";
RL Russ. J. Plant Physiol. 4:492-498(2003).
CC -!- FUNCTION: Catalyzes the two-stage endonucleolytic cleavage to 3'-
CC phosphomononucleotides and 3'-phosphooligonucleotides with 2',3'-cyclic
CC phosphate intermediates. {ECO:0000269|Ref.4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By ethephon and jasmonic acid. {ECO:0000269|Ref.4}.
CC -!- SIMILARITY: Belongs to the BetVI family. {ECO:0000305}.
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DR AlphaFoldDB; P80889; -.
DR SMR; P80889; -.
DR Allergome; 10131; Pan g 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0010427; F:abscisic acid binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:InterPro.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009607; P:response to biotic stimulus; IEA:UniProtKB-KW.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR000916; Bet_v_I/MLP.
DR InterPro; IPR024949; Bet_v_I_allergen.
DR InterPro; IPR023393; START-like_dom_sf.
DR Pfam; PF00407; Bet_v_1; 1.
DR PRINTS; PR00634; BETALLERGEN.
DR SMART; SM01037; Bet_v_1; 1.
DR PROSITE; PS00451; PATHOGENESIS_BETVI; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Endonuclease; Hydrolase; Nuclease;
KW Pathogenesis-related protein; Plant defense.
FT CHAIN 1..154
FT /note="Ribonuclease 1"
FT /id="PRO_0000154155"
SQ SEQUENCE 154 AA; 16424 MW; 4E58218CD4C01F26 CRC64;
GVQKTEVEAT STVPAQKLYA GLLLDIDDIL PKAFPQAIKS SEIIEGDGGV GTVKLVTLGE
ASQFNTMKQR IDAIDKDALT YTYSIIGGDI LLDIIESIVN HFTIVPTPDG GSIVKNTTIY
NTIGDAVIPE ENIKDATEKA GLIFKAVEAY LLAN