ID   RNS2_NICAL              Reviewed;         214 AA.
AC   P04007;
DT   23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-1986, sequence version 1.
DT   04-NOV-2026, entry version 112.
DE   RecName: Full=Ribonuclease S-2;
DE            EC=4.6.1.19 {ECO:0000255|PROSITE-ProRule:PRU10046};
DE   AltName: Full=S2-RNase;
DE   AltName: Full=Stylar glycoprotein 2;
DE   Flags: Precursor;
GN   Name=S-2;
OS   Nicotiana alata (Winged tobacco) (Persian tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Anderson M.A., Cornish E.C., Mau S.-L., Williams E.G., Hoggart R.,
RA   Atkinson A., Bonig I., Grego B., Simpson R., Roche P.J., Haley J.D.,
RA   Penschow J.D., Niall H.D., Tregear G.W., Coghlan J.P., Crawford R.J.,
RA   Clarke A.E.;
RT   "Cloning of cDNA for a stylar glycoprotein associated with expression of
RT   self-incompatibility in Nicotiana alata.";
RL   Nature 321:38-44(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7640357; DOI=10.1007/bf00042070;
RA   Matton D.P., Mau S.L., Okamoto S., Clarke A.E., Newbigin E.;
RT   "The S-locus of Nicotiana alata: genomic organization and sequence analysis
RT   of two S-RNase alleles.";
RL   Plant Mol. Biol. 28:847-858(1995).
RN   [3]
RP   FUNCTION.
RX   PubMed=2594090; DOI=10.1038/342955a0;
RA   McClure B.A., Haring V., Ebert P.R., Anderson M.A., Simpson R.J.,
RA   Sakiyama F., Clarke A.E.;
RT   "Style self-incompatibility gene products of Nicotiana alata are
RT   ribonucleases.";
RL   Nature 342:955-957(1989).
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 of the
CC       Solanaceae, self-incompatibility is controlled by the single,
CC       multiallelic locus S. This stylar glycoprotein is associated with
CC       expression of self-incompatibility in potato.
CC       {ECO:0000269|PubMed:2594090}.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X03803; CAA27428.1; -; mRNA.
DR   EMBL; M24600; AAA34083.1; -; mRNA.
DR   EMBL; U08860; AAB40027.1; -; Genomic_DNA.
DR   PIR; S57782; LNNTSA.
DR   AlphaFoldDB; P04007; -.
DR   SMR; P04007; -.
DR   GlyConnect; P04007; 3 N-Linked glycans (3 sites).
DR   GlyCosmos; P04007; 3 sites, 5 glycans.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0033897; F:ribonuclease T2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:TreeGrafter.
DR   CDD; cd01061; RNase_T2_euk; 1.
DR   Gene3D; 3.90.730.10; Ribonuclease T2-like; 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:SF81; RIBONUCLEASE S-2; 1.
DR   PANTHER; PTHR11240; RIBONUCLEASE T2; 1.
DR   Pfam; PF00445; Ribonuclease_T2; 1.
DR   SUPFAM; SSF55895; Ribonuclease Rh-like; 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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..214
FT                   /note="Ribonuclease S-2"
FT                   /id="PRO_0000030973"
FT   ACT_SITE        53
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SID5,
FT                   ECO:0000255|PROSITE-ProRule:PRU10045"
FT   ACT_SITE        109
FT                   /evidence="ECO:0000250|UniProtKB:P08056"
FT   ACT_SITE        113
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SID5,
FT                   ECO:0000255|PROSITE-ProRule:PRU10045"
FT   BINDING         53
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /ligand_part="a 3'-terminal ribonucleotide 3'-phosphate
FT                   residue"
FT                   /ligand_part_id="ChEBI:CHEBI:83062"
FT                   /evidence="ECO:0000250|UniProtKB:P23540"
FT   BINDING         91..92
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /ligand_part="a 3'-terminal ribonucleotide 3'-phosphate
FT                   residue"
FT                   /ligand_part_id="ChEBI:CHEBI:83062"
FT                   /evidence="ECO:0000250|UniProtKB:P23540"
FT   BINDING         94
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /ligand_part="a 3'-terminal ribonucleotide 3'-phosphate
FT                   residue"
FT                   /ligand_part_id="ChEBI:CHEBI:83062"
FT                   /evidence="ECO:0000250|UniProtKB:P23540"
FT   BINDING         105
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /ligand_part="a 3'-terminal ribonucleotide 3'-phosphate
FT                   residue"
FT                   /ligand_part_id="ChEBI:CHEBI:83062"
FT                   /evidence="ECO:0000250|UniProtKB:P23540"
FT   BINDING         112..113
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /ligand_part="a 3'-terminal ribonucleotide 3'-phosphate
FT                   residue"
FT                   /ligand_part_id="ChEBI:CHEBI:83062"
FT                   /evidence="ECO:0000250|UniProtKB:P23540"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT                   /id="CAR_000106"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT                   /id="CAR_000107"
FT   CARBOHYD        160
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT                   /id="CAR_000108"
FT   DISULFID        38..43
FT                   /evidence="ECO:0000250|UniProtKB:Q7SID5"
FT   DISULFID        67..116
FT                   /evidence="ECO:0000250|UniProtKB:P08056"
FT   DISULFID        175..204
FT                   /evidence="ECO:0000250|UniProtKB:P08056"
FT   DISULFID        187..198
FT                   /evidence="ECO:0000250|UniProtKB:P23540"
SQ   SEQUENCE   214 AA;  24876 MW;  62343152A6F02C40 CRC64;
     MSKSQLTSVF FILLCALSPI YGAFEYMQLV LTWPITFCRI KHCERTPTNF TIHGLWPDNH
     TTMLNYCDRS KPYNMFTDGK KKNDLDERWP DLTKTKFDSL DKQAFWKDEY VKHGTCCSDK
     FDREQYFDLA MTLRDKFDLL SSLRNHGISR GFSYTVQNLN NTIKAITGGF PNLTCSRLRE
     LKEIGICFDE TVKNVIDCPN PKTCKPTNKG VMFP
//