ID   RNS2_ANTHI              Reviewed;         235 AA.
AC   Q38716;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Ribonuclease S-2;
DE            EC=4.6.1.19;
DE   AltName: Full=S2-RNase;
DE   AltName: Full=Stylar glycoprotein 2;
DE   Flags: Precursor;
GN   Name=S2;
OS   Antirrhinum hispanicum (Snapdragon) (Antirrhinum glutinosum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Plantaginaceae; Antirrhineae; Antirrhinum.
OX   NCBI_TaxID=49039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Style;
RX   PubMed=8672882; DOI=10.2307/3870283;
RA   Xue Y., Carpenter R., Dickinson H.G., Coen E.S.;
RT   "Origin of allelic diversity in antirrhinum S locus RNases.";
RL   Plant Cell 8:805-814(1996).
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, ECO:0000255|PROSITE-ProRule:PRU10046};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
CC   -!- CAUTION: Gln-122 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; X96465; CAA65319.1; -; mRNA.
DR   PIR; S71462; S71462.
DR   AlphaFoldDB; Q38716; -.
DR   SMR; Q38716; -.
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   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   2: Evidence at transcript level;
KW   Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Lyase; Nuclease;
KW   Secreted; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..235
FT                   /note="Ribonuclease S-2"
FT                   /id="PRO_0000030984"
FT   ACT_SITE        66
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        80..129
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   235 AA;  26767 MW;  DE86AEFAEE97D7D0 CRC64;
     MATVQKSQHS HFFLLVGCIV HLSNFCSTTT AQFDYFKLVL QWPNSYCSLK TTHCPRTRLP
     SQFTIHGLWP DNKSWPLSNC RDTSADVLKI TDKGLIQDLA VHWPDLTRRQ RKVPGQKFWV
     TQWKKHGACA LPMYSFNDYF VKALELKKRN NVLDMLSRKS LTPGDQRVDV SDVNGAITKV
     TGGIAILKCP EGYLTEVIIC FDPSGFPVID CPGPFPCKDD PLEFQVLSRR KFQDL