ID RNAS1_PYGNE Reviewed; 156 AA. AC Q8SPN4; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 02-SEP-2026, entry version 81. DE RecName: Full=Ribonuclease pancreatic; DE EC=4.6.1.18; DE AltName: Full=RNase 1; DE AltName: Full=RNase A; DE Flags: Precursor; GN Name=RNASE1; Synonyms=RNS1; OS Pygathrix nemaeus (Red-shanked douc langur) (Simia nemaeus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Colobinae; Pygathrix. OX NCBI_TaxID=54133; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF ARG-29; ARG-32; RP LYS-34; ARG-60; ARG-67; PRO-70; ASP-111; ARG-126 AND ALA-150. RX PubMed=11925567; DOI=10.1038/ng852; RA Zhang J., Zhang Y.-P., Rosenberg H.F.; RT "Adaptive evolution of a duplicated pancreatic ribonuclease gene in a leaf- RT eating monkey."; RL Nat. Genet. 30:411-415(2002). CC -!- FUNCTION: Endonuclease that catalyzes the cleavage of RNA on the 3' CC side of pyrimidine nucleotides. Acts on single-stranded and double- CC stranded RNA (By 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 -!- 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 -!- SUBUNIT: Monomer. Interacts with and forms tight 1:1 complexes with CC RNH1. Dimerization of two such complexes may occur. Interaction with CC RNH1 inhibits this protein (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF449642; AAL87063.1; -; Genomic_DNA. DR AlphaFoldDB; Q8SPN4; -. DR SMR; Q8SPN4; -. DR GlyCosmos; Q8SPN4; 2 sites, No reported glycans. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0004522; F:ribonuclease A activity; IEA:UniProtKB-EC. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:TreeGrafter. DR CDD; cd06265; RNase_A_canonical; 1. DR FunFam; 3.10.130.10:FF:000001; Ribonuclease pancreatic; 1. DR Gene3D; 3.10.130.10; Ribonuclease A-like domain; 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; RIBONUCLEASE; 1. DR PANTHER; PTHR11437:SF24; RIBONUCLEASE PANCREATIC; 1. DR Pfam; PF00074; RnaseA; 1. DR PRINTS; PR00794; RIBONUCLEASE. DR SMART; SM00092; RNAse_Pc; 1. DR SUPFAM; SSF54076; RNase A-like; 1. DR PROSITE; PS00127; RNASE_PANCREATIC; 1. PE 1: Evidence at protein level; KW Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Lyase; Nuclease; KW Secreted; Signal. FT SIGNAL 1..28 FT /evidence="ECO:0000250" FT CHAIN 29..156 FT /note="Ribonuclease pancreatic" FT /id="PRO_0000030938" FT REGION 31..52 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 40 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 147 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 35 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 38 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 69..73 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 94 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 113 FT /ligand="substrate" FT /evidence="ECO:0000250" FT CARBOHYD 62 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 116 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 54..112 FT /evidence="ECO:0000250" FT DISULFID 68..123 FT /evidence="ECO:0000250" FT DISULFID 86..138 FT /evidence="ECO:0000250" FT DISULFID 93..100 FT /evidence="ECO:0000250" FT MUTAGEN 29 FT /note="R->G: Reduces activity towards double stranded RNA." FT /evidence="ECO:0000269|PubMed:11925567" FT MUTAGEN 32 FT /note="R->Q: Slightly reduces activity towards FT double-stranded RNA." FT /evidence="ECO:0000269|PubMed:11925567" FT MUTAGEN 34 FT /note="K->E: Reduces activity towards double stranded RNA." FT /evidence="ECO:0000269|PubMed:11925567" FT MUTAGEN 60 FT /note="R->L: Strongly reduces activity towards FT double-stranded RNA." FT /evidence="ECO:0000269|PubMed:11925567" FT MUTAGEN 67 FT /note="R->W: Reduces activity towards double stranded RNA." FT /evidence="ECO:0000269|PubMed:11925567" FT MUTAGEN 70 FT /note="P->S: Reduces activity towards double stranded RNA." FT /evidence="ECO:0000269|PubMed:11925567" FT MUTAGEN 111 FT /note="D->E: Strongly reduces activity towards FT double-stranded RNA." FT /evidence="ECO:0000269|PubMed:11925567" FT MUTAGEN 126 FT /note="R->Q: Reduces activity towards double stranded RNA." FT /evidence="ECO:0000269|PubMed:11925567" FT MUTAGEN 150 FT /note="A->D: Reduces activity towards double stranded RNA." FT /evidence="ECO:0000269|PubMed:11925567" SQ SEQUENCE 156 AA; 17498 MW; 8168684878BE9436 CRC64; MALDKSVILL PLLVVVLLVL GWAQPSLGRE SRAKKFQRQH MDSGSSPSSS STYCNQMMKR RNMTQGRCKP VNTFVHEPLV DVQNVCFQEK VTCKNGQTNC FKSNSKMHIT DCRLTNGSKY PNCAYRTSPK ERHIIVACEG SPYVPVHFDA SVEDST //