RNAS2_GORGO
ID RNAS2_GORGO Reviewed; 161 AA.
AC P47782;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
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 Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
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).
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.
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 Note=Matrix of eosinophil's large specific granule.
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
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DR EMBL; U24100; AAC50144.1; -; Genomic_DNA.
DR PIR; I37034; I37034.
DR RefSeq; XP_004054908.1; XM_004054860.1.
DR AlphaFoldDB; P47782; -.
DR SMR; P47782; -.
DR STRING; 9593.ENSGGOP00000004990; -.
DR Ensembl; ENSGGOT00000005117; ENSGGOP00000004990; ENSGGOG00000043975.
DR GeneID; 101147913; -.
DR KEGG; ggo:101147913; -.
DR CTD; 6036; -.
DR eggNOG; ENOG502TF52; Eukaryota.
DR GeneTree; ENSGT00940000162253; -.
DR HOGENOM; CLU_117006_0_1_1; -.
DR InParanoid; P47782; -.
DR OMA; MFYIVAC; -.
DR OrthoDB; 1482425at2759; -.
DR Proteomes; UP000001519; Chromosome 14.
DR Bgee; ENSGGOG00000043975; Expressed in frontal cortex and 2 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_0000030873"
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"
SQ SEQUENCE 161 AA; 18382 MW; 0D2257A950555F04 CRC64;
MVPKLFTSQI CLLLLLGLLA VEGSLHVKPP QFTWAQWFET QHINMTSQQC TNAMRVINNY
QRRCKNQNTF LLTTFANVVN VCGNPNMTCP SNKTRKNCHH SGSQVPLIHC NLTTPSPQNI
SNCRYAQTPA NMFYIVACDN RDQRRDPPQY PVVPVHLDRI I
