RNS2_NICAL
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 25-MAY-2022, entry version 102.
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=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}.
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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; 531; 4 N-Linked glycans (3 sites).
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 CHAIN 23..214
FT /note="Ribonuclease S-2"
FT /id="PRO_0000030973"
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 /id="CAR_000106"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /id="CAR_000107"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /id="CAR_000108"
FT DISULFID 67..116
FT /evidence="ECO:0000250"
FT DISULFID 175..204
FT /evidence="ECO:0000250"
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