RNAS1_PYGNE
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 03-AUG-2022, entry version 74.
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).
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}.
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DR EMBL; AF449642; AAL87063.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8SPN4; -.
DR SMR; Q8SPN4; -.
DR GO; GO:0005576; C:extracellular region; 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 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 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 double-
FT 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 double-
FT 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 double-
FT 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
