ID   RNS2_PYRPY              Reviewed;         221 AA.
AC   Q40965;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Ribonuclease S-2;
DE            EC=4.6.1.19;
DE   AltName: Full=S2-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 [MRNA].
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 28-204.
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   [3]
RP   GLYCOSYLATION AT ASN-91; ASN-137; ASN-153 AND ASN-195, AND STRUCTURE OF
RP   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: N-linked core structure at Asn-91, Asn-137, and Asn-153 contains
CC       xylose and at Asn-195 contains xylose and fucose.
CC       {ECO:0000269|PubMed:10469125}.
CC   -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
CC   -!- CAUTION: Gln-105 is present instead of the conserved Glu which is
CC       expected to act as an active site proton donor. {ECO:0000305}.
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DR   EMBL; D49527; BAA08473.1; -; mRNA.
DR   AlphaFoldDB; Q40965; -.
DR   SMR; Q40965; -.
DR   iPTMnet; Q40965; -.
DR   PRIDE; Q40965; -.
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   Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Lyase; Nuclease;
KW   Secreted; Signal.
FT   SIGNAL          1..20
FT   CHAIN           21..221
FT                   /note="Ribonuclease S-2"
FT                   /id="PRO_0000030978"
FT   ACT_SITE        55
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10045"
FT   ACT_SITE        109
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10045"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:10469125"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:10469125"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:10469125"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:10469125"
FT   DISULFID        70..112
FT                   /evidence="ECO:0000250"
FT   DISULFID        176..202
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   221 AA;  25750 MW;  BA828175306D1727 CRC64;
     MIYIFTMVFS LNVLILSSSA ARYDYFQFTQ QYQQAFCNSN PTPCKDPPDK LFTVHGLWPS
     TKVGRDPEYC KTKRYRKIQR LEPQLEIIWP NVSDRKANRG FWRKQWYKHG SCASPALPNQ
     KHYFETVIRM FLAEKQNVSR ILSMATIEPE GKNRTLLEIQ NAIRAGTNNM IPKLKCQKVN
     GMTELVEVTL CHDSNLTQFI NCPRPLPQAS PYFCPIDDIQ Y