RNS4_PYRPY
ID RNS4_PYRPY Reviewed; 228 AA.
AC Q40966;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Ribonuclease S-4;
DE EC=4.6.1.19;
DE AltName: Full=S4-RNase;
DE Flags: Precursor;
OS Pyrus pyrifolia (Chinese pear) (Pyrus serotina).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Pyrus.
OX NCBI_TaxID=3767;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Nijisseiki;
RX PubMed=9573352; DOI=10.1016/s0378-1119(98)00105-x;
RA Ushijima K., Sassa H., Hirano H.;
RT "Characterization of the flanking regions of the S-RNase genes of Japanese
RT pear (Pyrus serotina) and apple (Malus x domestica).";
RL Gene 211:159-167(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 6-228.
RC STRAIN=cv. Nijisseiki; TISSUE=Style;
RA Norioka N., Ohnishi Y., Norioka S., Ishimizu T., Nakanishi T., Sakiyama F.;
RT "Nucleotide sequences of cDNAs encoding S2- and S4-RNases from Japanese
RT pear (Pyrus pyrifolia Nakai 1).";
RL (er) Plant Gene Register PGR95-020(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Nijisseiki;
RA Norioka N., Norioka S.;
RT "The genomic structures of S-RNases in Japanese pear.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. Nijisseiki;
RX PubMed=8889819; DOI=10.1093/oxfordjournals.jbchem.a021418;
RA Norioka N., Norioka S., Ohnishi Y., Ishimizu T., Oneyama C., Nakanishi T.,
RA Sakiyama F.;
RT "Molecular cloning and nucleotide sequences of cDNAs encoding S-allele
RT specific stylar RNases in a self-incompatible cultivar and its self-
RT compatible mutant of Japanese pear, Pyrus pyrifolia Nakai.";
RL J. Biochem. 120:335-345(1996).
RN [5]
RP GLYCOSYLATION AT ASN-87; ASN-101; ASN-144; ASN-160 AND ASN-175, AND
RP STRUCTURE OF CARBOHYDRATES.
RC STRAIN=cv. Nijisseiki; TISSUE=Style;
RX PubMed=10469125; DOI=10.1046/j.1432-1327.1999.00499.x;
RA Ishimizu T., Mitsukami Y., Shinkawa T., Natsuka S., Hase S., Miyagi M.,
RA Sakiyama F., Norioka S.;
RT "Presence of asparagine-linked N-acetylglucosamine and chitobiose in Pyrus
RT pyrifolia S-RNases associated with gametophytic self-incompatibility.";
RL Eur. J. Biochem. 263:624-634(1999).
CC -!- FUNCTION: Self-incompatibility (SI) is the inherited ability of a
CC flowering plant to prevent self-fertilization by discriminating between
CC self and non-self pollen during pollination. In many species, self-
CC incompatibility is controlled by the single, multiallelic locus S.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-
CC phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA +
CC H(+); Xref=Rhea:RHEA:68052, Rhea:RHEA-COMP:10463, Rhea:RHEA-
CC COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:83062, ChEBI:CHEBI:138284,
CC ChEBI:CHEBI:173118; EC=4.6.1.19; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10045};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- PTM: The N-glycans attached at Asn-101, Asn-160 and Asn-175 consist
CC predominantly of disaccharide (GlcNAc-GlcNAc). The N-glycan at 87 is
CC 53% monosaccharide and 47% disaccharide. The N-glycan at Asn-144
CC contains mannose and xylose.
CC -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
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DR EMBL; AB009385; BAA28354.1; -; Genomic_DNA.
DR EMBL; D49528; BAA08474.1; -; mRNA.
DR EMBL; AB014072; BAA77692.1; -; Genomic_DNA.
DR PIR; JC4869; JC4869.
DR PIR; S39932; S39932.
DR AlphaFoldDB; Q40966; -.
DR SMR; Q40966; -.
DR iPTMnet; Q40966; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0033897; F:ribonuclease T2 activity; IEA:UniProtKB-EC.
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 PANTHER; PTHR11240; PTHR11240; 1.
DR Pfam; PF00445; Ribonuclease_T2; 1.
DR SUPFAM; SSF55895; SSF55895; 1.
DR PROSITE; PS00530; RNASE_T2_1; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Endonuclease; Glycoprotein;
KW Hydrolase; Lyase; Nuclease; Secreted; Signal.
FT SIGNAL 1..27
FT CHAIN 28..228
FT /note="Ribonuclease S-4"
FT /id="PRO_0000030980"
FT ACT_SITE 60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10045"
FT ACT_SITE 112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10045"
FT ACT_SITE 116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10045"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc) asparagine"
FT /evidence="ECO:0000269|PubMed:10469125"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10469125"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10469125"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10469125"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10469125"
FT DISULFID 75..119
FT /evidence="ECO:0000250"
FT DISULFID 183..210
FT /evidence="ECO:0000250"
SQ SEQUENCE 228 AA; 25858 MW; C8A95158FF1A7CCD CRC64;
MGITGMTYMF TMVLSLIVLI FSASTVGFDY FQFTQQYQPA VCNSNPTPCN DPTDKLFTVH
GLWPSNRNGP DPEKCKTTTM NSQKIGNMTA QLEIIWPNVL NRSDHVGFWE REWLKHGTCG
YPTIKDDMHY LKTVIKMYIT QKQNVSAILS KATIQPNGNN RSLVDIENAI RSGNNNTKPK
FKCQKNTRTT TELVEVTLCS NRDLTKFINC PHGPPKGSRY FCPANVKY
