RNS1A_CAVPO
ID RNS1A_CAVPO Reviewed; 124 AA.
AC P00678;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Ribonuclease pancreatic A;
DE Short=RNase IA;
DE EC=4.6.1.18;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Pancreas;
RX PubMed=862624; DOI=10.1111/j.1432-1033.1977.tb11507.x;
RA van den Berg A., van den Hende-Timmer L., Hofsteenge J., Gaastra W.,
RA Beintema J.J.;
RT "Guinea-pig pancreatic ribonucleases. Isolation, properties, primary
RT structure and glycosidation.";
RL Eur. J. Biochem. 75:91-100(1977).
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Pancreas.
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
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DR PIR; A00825; NRGPA.
DR AlphaFoldDB; P00678; -.
DR SMR; P00678; -.
DR PRIDE; P00678; -.
DR eggNOG; ENOG502SQ4K; Eukaryota.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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 Direct protein sequencing; Disulfide bond; Endonuclease; Hydrolase; Lyase;
KW Nuclease; Reference proteome; Secreted.
FT CHAIN 1..124
FT /note="Ribonuclease pancreatic A"
FT /id="PRO_0000057188"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 12
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 119
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 7
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 41..45
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 26..84
FT /evidence="ECO:0000250"
FT DISULFID 40..95
FT /evidence="ECO:0000250"
FT DISULFID 58..110
FT /evidence="ECO:0000250"
FT DISULFID 65..72
FT /evidence="ECO:0000250"
SQ SEQUENCE 124 AA; 13845 MW; E683A87A1DB54DEC CRC64;
AESSAMKFER QHVDSGGSSS SNANYCNEMM KKREMTKDRC KPVNTFVHEP LAEVQAVCSQ
RNVSCKNGQT NCYQSYSSMH ITECRLTSGS KFPNCSYRTS QAQKSIIVAC EGKPYVPVHF
DNSV
