ID   RNS6_NICAL              Reviewed;         215 AA.
AC   Q40379;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Ribonuclease S-6;
DE            EC=4.6.1.19;
DE   AltName: Full=S6-RNase;
DE   AltName: Full=Stylar glycoprotein 6;
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 [GENOMIC DNA].
RX   PubMed=2535547; DOI=10.2307/3868968;
RA   Anderson M.A., McFadden G.I., Bernatzky R., Atkinson A., Orpin T.,
RA   Dedman H., Tregear G., Fernley R., Clarke A.E.;
RT   "Sequence variability of three alleles of the self-incompatibility gene of
RT   Nicotiana alata.";
RL   Plant Cell 1:483-491(1989).
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   PROTEIN SEQUENCE OF 23-36.
RX   PubMed=8232200; DOI=10.1007/bf00280196;
RA   Sassa H., Hirano H., Ikehashi H.;
RT   "Identification and characterization of stylar glycoproteins associated
RT   with self-incompatibility genes of Japanese pear, Pyrus serotina Rehd.";
RL   Mol. Gen. Genet. 241:17-25(1993).
RN   [4]
RP   STRUCTURE OF CARBOHYDRATES.
RX   PubMed=8922956; DOI=10.1093/glycob/6.6.611;
RA   Oxley D., Munro S.L., Craik D.J., Bacic A.;
RT   "Structure of N-glycans on the S3- and S6-allele stylar self-
RT   incompatibility ribonucleases of Nicotiana alata.";
RL   Glycobiology 6:611-618(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 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};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
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DR   EMBL; U08861; AAB40028.1; -; Genomic_DNA.
DR   PIR; JQ1079; LNNTS6.
DR   AlphaFoldDB; Q40379; -.
DR   SMR; Q40379; -.
DR   GlyConnect; 533; 14 N-Linked glycans.
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   Direct protein sequencing; Disulfide bond; Endonuclease; Glycoprotein;
KW   Hydrolase; Lyase; Nuclease; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..215
FT                   /note="Ribonuclease S-6"
FT                   /id="PRO_0000030974"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10045"
FT   ACT_SITE        109
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10045"
FT   ACT_SITE        113
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10045"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        160
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        172
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        67..116
FT                   /evidence="ECO:0000250"
FT   DISULFID        175..204
FT                   /evidence="ECO:0000250"
FT   CONFLICT        36
FT                   /note="A -> T (in Ref. 2; AAB40028)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183
FT                   /note="F -> E (in Ref. 2; AAB40028)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   215 AA;  24778 MW;  601A9A4B6680A74C CRC64;
     MFNLPLTSVF VIFLFALSPI YGAFEYMQLV LQWPTAFCHT TPCKNIPSNF TIHGLWPDNV
     STTLNFCGKE DDYNIIMDGP EKNGLYVRWP DLIREKADCM KTQNFWRREY IKHGTCCSEI
     YNQVQYFRLA MALKDKFDLL TSLKNHGIIR GYKYTVQKIN NTIKTVTKGY PNLSCTKGQE
     LWFVGICFDS TAKNVIDCPN PKTCKTASNQ GIMFP