ID   RNS2_SOLTU              Reviewed;         223 AA.
AC   Q01796;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 99.
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;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2038308; DOI=10.1007/bf00260659;
RA   Kaufmann H., Salamini F., Thompson R.D.;
RT   "Sequence variability and gene structure at the self-incompatibility locus
RT   of Solanum tuberosum.";
RL   Mol. Gen. Genet. 226:457-466(1991).
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   -!- 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   -!- TISSUE SPECIFICITY: Pistil.
CC   -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
CC   -!- CAUTION: Gln-112 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; X62727; CAA44600.1; -; Genomic_DNA.
DR   PIR; PQ0749; PQ0749.
DR   PIR; S16007; S16007.
DR   AlphaFoldDB; Q01796; -.
DR   SMR; Q01796; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q01796; baseline.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
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; IBA:GO_Central.
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   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..223
FT                   /note="Ribonuclease S-2"
FT                   /id="PRO_0000030986"
FT   ACT_SITE        55
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        116
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        71..119
FT                   /evidence="ECO:0000250"
FT   DISULFID        178..211
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   223 AA;  26075 MW;  9BAFCCF15D737FDE CRC64;
     MAKSQLVSAL FVFFFSLSPI YGDFDYMQLV LTWPRSFCYP RGFCNRIPPN NFTIHGLWPD
     KKPMRGQLQF CTSDDYIKFT PGSVLDALDH HWIQLKFERE IGIRDQPLWK DQYKKHGTCC
     LPRYNQLQYF LLAMRLKEKF DLLTTLRTHG ITPGTKHTFK KIQDAIKTVT QEVPDLKCVE
     NIQGVLELYE IGICFTPEAD SLFPCRQSKS CHPTENPLIL FRL