RNAS1_GIRCA
ID RNAS1_GIRCA Reviewed; 124 AA.
AC P00662; Q29534; Q29541;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Ribonuclease pancreatic;
DE EC=4.6.1.18;
DE AltName: Full=RNase 1;
DE AltName: Full=RNase A;
GN Name=RNASE1; Synonyms=RNS1;
OS Giraffa camelopardalis (Giraffe).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Giraffidae;
OC Giraffa.
OX NCBI_TaxID=9894;
RN [1]
RP PROTEIN SEQUENCE.
RA Gaastra W.;
RL Thesis (1975), University of Groningen, Netherlands.
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=4855009; DOI=10.1016/0014-5793(74)81218-4;
RA Gaastra W., Groen G., Welling G.W., Beintema J.J.;
RT "The primary structure of giraffe pancreatic ribonuclease.";
RL FEBS Lett. 41:227-232(1974).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8587129; DOI=10.1007/bf00173164;
RA Confalone E., Beintema J.J., Sasso M.P., Carsana A., Palmieri M.,
RA Vento M.T., Furia A.;
RT "Molecular evolution of genes encoding ribonucleases in ruminant species.";
RL J. Mol. Evol. 41:850-858(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-114.
RX PubMed=8360916; DOI=10.1007/bf00170459;
RA Breukelman H.J., Beintema J.J., Confalone E., Costanzo C., Sasso M.P.,
RA Carsana A., Palmieri M., Furia A.;
RT "Sequences related to the ox pancreatic ribonuclease coding region in the
RT genomic DNA of mammalian species.";
RL J. Mol. Evol. 37:29-35(1993).
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.
CC -!- TISSUE SPECIFICITY: Pancreas.
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
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DR EMBL; S81739; AAB36133.1; -; Genomic_DNA.
DR EMBL; S65127; AAB27932.1; -; Genomic_DNA.
DR PIR; A94452; NRGF.
DR AlphaFoldDB; P00662; -.
DR SMR; P00662; -.
DR iPTMnet; P00662; -.
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; Glycoprotein;
KW Hydrolase; Lyase; Nuclease; Secreted.
FT CHAIN 1..124
FT /note="Ribonuclease pancreatic"
FT /id="PRO_0000057198"
FT REGION 1..23
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 CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:4855009"
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"
FT VARIANT 76
FT /note="Y -> N"
FT CONFLICT 28
FT /note="E -> Q (in Ref. 1; AA sequence and 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 124 AA; 13704 MW; CE97EBDC792612DA CRC64;
KESAAAKFER QHIDSSTSSV SSSNYCNEMM TSRNLTQDRC KPVNTFVHES LADVQAVCSQ
KNVACKNGQT NCYQSYSAMS ITDCRETGNS KYPNCAYQTT QAEKHIIVAC EGNPYVPVHY
DASV
