ID   RNS7_NICAL              Reviewed;         218 AA.
AC   Q40381;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Ribonuclease S-7;
DE            EC=4.6.1.19;
DE   AltName: Full=S7-RNase;
DE   AltName: Full=Stylar glycoprotein 7;
DE   Flags: Precursor;
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].
RC   TISSUE=Flower;
RX   PubMed=7784516; DOI=10.1104/pp.108.1.427;
RA   Vissers A., Dodds P., Golz J.F., Clarke A.E.;
RT   "Cloning and nucleotide sequence of the S7-RNase from Nicotiana alata Link
RT   and Otto.";
RL   Plant Physiol. 108:427-428(1995).
RN   [2]
RP   GLYCOSYLATION AT ASN-49; ASN-59 AND ASN-162, AND STRUCTURE OF
RP   CARBOHYDRATES.
RX   PubMed=9562634; DOI=10.1093/oxfordjournals.jbchem.a022033;
RA   Oxley D., Munro S.L., Craik D.J., Bacic A.;
RT   "Structure and distribution of N-glycans on the S7-allele stylar self-
RT   incompatibility ribonuclease of Nicotiana alata.";
RL   J. Biochem. 123:978-983(1998).
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   -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
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DR   EMBL; U13255; AAA87898.1; -; mRNA.
DR   AlphaFoldDB; Q40381; -.
DR   SMR; Q40381; -.
DR   GlyConnect; 534; 9 N-Linked glycans (3 sites).
DR   PRIDE; Q40381; -.
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   1: Evidence at protein level;
KW   Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Lyase; Nuclease;
KW   Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..218
FT                   /note="Ribonuclease S-7"
FT                   /id="PRO_0000030975"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        109
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        113
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:9562634"
FT                   /id="CAR_000109"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:9562634"
FT                   /id="CAR_000110"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:9562634"
FT                   /id="CAR_000111"
FT   DISULFID        67..116
FT                   /evidence="ECO:0000250"
FT   DISULFID        177..207
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   218 AA;  25178 MW;  B9B1DE2E7A06B986 CRC64;
     MLNSPLTSVL FVLLFVLSPI YGAFEYMQLV LQWPTAFCHT TPCKRIPNNF TIHGLWPDNV
     STTLNYCAAK ENFKNIEDDT KKDDLYKRWP DLTTAETYCK QHQNFWRHEY NKHGKCCSES
     YNREQYFDLA MALKDKFDLL SSLRNHGIIP GRGMKYTVQK INSTIKKITQ GYPNLSCTKG
     IMELVEIGIC FDSMVKNVIN CPHPKTCKPT GSNEIKFP