Q40965 (RNS2_PYRPY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Ribonuclease S-2 EC=3.1.27.1 Alternative name(s): S2-RNase
Organism	Pyrus pyrifolia (Chinese pear) (Pyrus serotina)
Taxonomic identifier	3767 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Rosales › Rosaceae › Amygdaloideae › Maleae › Pyrus

Protein attributes

Sequence length	221 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Self-incompatibility (SI) is the inherited ability of a flowering plant to prevent self-fertilization by discriminating between self and non-self pollen during pollination. In many species, self-incompatibility is controlled by the single, multiallelic locus S.
Catalytic activity	Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Subcellular location	Secreted › extracellular space.
Post-translational modification	N-linked core structure at Asn-91, Asn-137, and Asn-153 contains xylose and at Asn-195 contains xylose and fucose.
Sequence similarities	Belongs to the RNase T2 family.
Caution	Gln-105 is present instead of the conserved Glu which is expected to act as an active site proton donor.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological_process	nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC
Cellular_component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	RNA binding Inferred from electronic annotation. Source: InterPro ribonuclease T2 activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20
	Chain	21 – 221	201	Ribonuclease S-2		PRO_0000030978
Sites
	Active site	55	1	By similarity
	Active site	109	1	By similarity
Amino acid modifications
	Glycosylation	91	1	N-linked (GlcNAc...) Ref.3
	Glycosylation	137	1	N-linked (GlcNAc...) Ref.3
	Glycosylation	153	1	N-linked (GlcNAc...) Ref.3
	Glycosylation	195	1	N-linked (GlcNAc...) Ref.3
	Disulfide bond	70 ↔ 112		By similarity
	Disulfide bond	176 ↔ 202		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q40965 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: BA828175306D1727	FASTA	221	25,750
	10 20 30 40 50 60 MIYIFTMVFS LNVLILSSSA ARYDYFQFTQ QYQQAFCNSN PTPCKDPPDK LFTVHGLWPS 70 80 90 100 110 120 TKVGRDPEYC KTKRYRKIQR LEPQLEIIWP NVSDRKANRG FWRKQWYKHG SCASPALPNQ 130 140 150 160 170 180 KHYFETVIRM FLAEKQNVSR ILSMATIEPE GKNRTLLEIQ NAIRAGTNNM IPKLKCQKVN 190 200 210 220 GMTELVEVTL CHDSNLTQFI NCPRPLPQAS PYFCPIDDIQ Y

References

[1]	"Nucleotide sequences of cDNAs encoding S2- and S4-RNases from Japanese pear (Pyrus pyrifolia Nakai 1)." Norioka N., Ohnishi Y., Norioka S., Ishimizu T., Nakanishi T., Sakiyama F. Plant Gene Register PGR95-020 Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Nijisseiki. Tissue: Style.
[2]	"Molecular cloning and nucleotide sequences of cDNAs encoding S-allele specific stylar RNases in a self-incompatible cultivar and its self-compatible mutant of Japanese pear, Pyrus pyrifolia Nakai." Norioka N., Norioka S., Ohnishi Y., Ishimizu T., Oneyama C., Nakanishi T., Sakiyama F. J. Biochem. 120:335-345(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-204. Strain: cv. Nijisseiki.
[3]	"Presence of asparagine-linked N-acetylglucosamine and chitobiose in Pyrus pyrifolia S-RNases associated with gametophytic self-incompatibility." Ishimizu T., Mitsukami Y., Shinkawa T., Natsuka S., Hase S., Miyagi M., Sakiyama F., Norioka S. Eur. J. Biochem. 263:624-634(1999) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-91; ASN-137; ASN-153 AND ASN-195, STRUCTURE OF CARBOHYDRATES. Strain: cv. Nijisseiki. Tissue: Style.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D49527 mRNA. Translation: BAA08473.1.
3D structure databases
ProteinModelPortal	Q40965.
SMR	Q40965. Positions 23-221.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.90.730.10. 1 hit.
InterPro	IPR001568. RNase_T2-like. IPR018188. RNase_T2_AS. [Graphical view]
PANTHER	PTHR11240. PTHR11240. 1 hit.
Pfam	PF00445. Ribonuclease_T2. 1 hit. [Graphical view]
SUPFAM	SSF55895. RNase_T2. 1 hit.
PROSITE	PS00530. RNASE_T2_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RNS2_PYRPY

Accession

Primary (citable) accession number: Q40965

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program