RNS4_ANTHI
ID RNS4_ANTHI Reviewed; 233 AA.
AC Q38717;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Ribonuclease S-4;
DE EC=4.6.1.19;
DE AltName: Full=S4-RNase;
DE AltName: Full=Stylar glycoprotein 4;
DE Flags: Precursor;
GN Name=S4;
OS Antirrhinum hispanicum (Snapdragon) (Antirrhinum glutinosum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Plantaginaceae; Antirrhineae; Antirrhinum.
OX NCBI_TaxID=49039;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Style;
RX PubMed=8672882; DOI=10.2307/3870283;
RA Xue Y., Carpenter R., Dickinson H.G., Coen E.S.;
RT "Origin of allelic diversity in antirrhinum S locus RNases.";
RL Plant Cell 8:805-814(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, self-
CC incompatibility is controlled by the single, multiallelic locus S.
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 -!- CAUTION: Gln-121 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; X96466; CAA65320.1; -; mRNA.
DR PIR; S71463; S71463.
DR AlphaFoldDB; Q38717; -.
DR SMR; Q38717; -.
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 2: Evidence at transcript level;
KW Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Lyase; Nuclease;
KW Secreted; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..233
FT /note="Ribonuclease S-4"
FT /id="PRO_0000030985"
FT REGION 211..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 66
FT /evidence="ECO:0000250"
FT ACT_SITE 125
FT /evidence="ECO:0000250"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 81..128
FT /evidence="ECO:0000250"
SQ SEQUENCE 233 AA; 26889 MW; BC62235B8111CA58 CRC64;
MAMIKKNRKV NPLSLLVVCV VPLNCCSTII AKCDYLKLVL QWPKSFCLIN SRKCQRNPLP
SNFTIHGLWP DNYTRQAPQS CTTNNFQRFT DTDIEQRMEE SWPDLKQQSI AGLSYNFWQD
QWRKHGSCCF PPHESEIYFL KALELKDRLD VLTILENNNF NPGTPQPFSV LRVFNTISRA
IGKTPILKCA QSYLKEVVIC VDNNGASVVH CPRSRPRPRP RRDPCPFSDV KFP