RNAS2_PANTR
ID RNAS2_PANTR Reviewed; 161 AA.
AC P47785; P60017; Q9GK98;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Non-secretory ribonuclease;
DE EC=4.6.1.18 {ECO:0000250|UniProtKB:P47784};
DE AltName: Full=Eosinophil-derived neurotoxin;
DE AltName: Full=RNase UpI-2;
DE AltName: Full=Ribonuclease 2;
DE Short=RNase 2;
DE AltName: Full=Ribonuclease US;
DE Flags: Precursor;
GN Name=RNASE2; Synonyms=EDN, RNS2;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7663519; DOI=10.1038/ng0695-219;
RA Rosenberg H.F., Dyer K.D., Tiffany H.L., Gonzalez M.;
RT "Rapid evolution of a unique family of primate ribonuclease genes.";
RL Nat. Genet. 10:219-223(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT CYS-95.
RX PubMed=11102386; DOI=10.1093/genetics/156.4.1949;
RA Zhang J., Rosenberg H.F.;
RT "Sequence variation at two eosinophil-associated ribonuclease loci in
RT humans.";
RL Genetics 156:1949-1958(2000).
CC -!- FUNCTION: This is a non-secretory ribonuclease. It is a pyrimidine
CC specific nuclease with a slight preference for U. Cytotoxin and
CC helminthotoxin. Possesses a wide variety of biological activities (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-
CC phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18;
CC Evidence={ECO:0000250|UniProtKB:P47784};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-
CC phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18;
CC Evidence={ECO:0000250|UniProtKB:P47784};
CC -!- SUBUNIT: Interacts with and forms a tight 1:1 complex with RNH1.
CC Dimerization of two such complexes may occur (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000305}. Cytoplasmic granule
CC {ECO:0000250}. Note=Matrix of eosinophil's large specific granule.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
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DR EMBL; U24102; AAC50149.1; -; Genomic_DNA.
DR EMBL; AF294016; AAG31586.1; -; Genomic_DNA.
DR EMBL; AF294017; AAG31587.1; -; Genomic_DNA.
DR EMBL; AF294018; AAG31588.1; -; Genomic_DNA.
DR PIR; I61898; I61898.
DR RefSeq; NP_001009133.1; NM_001009133.1.
DR RefSeq; XP_009425659.1; XM_009427384.2.
DR AlphaFoldDB; P47785; -.
DR SMR; P47785; -.
DR STRING; 9598.ENSPTRP00000052810; -.
DR PaxDb; P47785; -.
DR Ensembl; ENSPTRT00000059611; ENSPTRP00000052810; ENSPTRG00000006106.
DR GeneID; 473325; -.
DR KEGG; ptr:473325; -.
DR CTD; 6036; -.
DR VGNC; VGNC:12521; RNASE2.
DR eggNOG; ENOG502TF52; Eukaryota.
DR GeneTree; ENSGT00940000162253; -.
DR HOGENOM; CLU_117006_0_1_1; -.
DR InParanoid; P47785; -.
DR OMA; MFYIVAC; -.
DR OrthoDB; 1482425at2759; -.
DR TreeFam; TF333393; -.
DR Proteomes; UP000002277; Chromosome 14.
DR Bgee; ENSPTRG00000006106; Expressed in bone marrow and 11 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004522; F:ribonuclease A activity; IEA:UniProtKB-EC.
DR GO; GO:0004540; F:ribonuclease activity; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
DR GO; GO:0002227; P:innate immune response in mucosa; IBA:GO_Central.
DR Gene3D; 3.10.130.10; -; 1.
DR InterPro; IPR001427; RNaseA.
DR InterPro; IPR036816; RNaseA-like_dom_sf.
DR InterPro; IPR023411; RNaseA_AS.
DR InterPro; IPR023412; RNaseA_domain.
DR PANTHER; PTHR11437; PTHR11437; 1.
DR Pfam; PF00074; RnaseA; 1.
DR PRINTS; PR00794; RIBONUCLEASE.
DR SMART; SM00092; RNAse_Pc; 1.
DR SUPFAM; SSF54076; SSF54076; 1.
DR PROSITE; PS00127; RNASE_PANCREATIC; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Lyase; Lysosome;
KW Nitration; Nuclease; Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT CHAIN 28..161
FT /note="Non-secretory ribonuclease"
FT /id="PRO_0000030878"
FT ACT_SITE 42
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 156
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 65..69
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 60
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P10153"
FT CARBOHYD 34
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P10153"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..110
FT /evidence="ECO:0000250"
FT DISULFID 64..123
FT /evidence="ECO:0000250"
FT DISULFID 82..138
FT /evidence="ECO:0000250"
FT DISULFID 89..98
FT /evidence="ECO:0000250"
FT VARIANT 95
FT /note="R -> C (in haplotype 3)"
FT /evidence="ECO:0000269|PubMed:11102386"
FT /id="VAR_021254"
SQ SEQUENCE 161 AA; 18345 MW; 8321F4596CBF8938 CRC64;
MVPKLFTSQI CLLLLLGLLA VEGSLHVKPP QFTWAQWFET QHINMTSQQC TNAMQVINNY
QRRCKNQNTF LLTTFANVVN VCGNPNMTCP SNKTRKNCHQ SGSQVPLIHC NLTTPSPQNI
SNCRYAQTPA NMFYIVACDN RDQRRDPPQY PVVPVHLDRI I
