ID   RNAS1_CAMDR             Reviewed;         124 AA.
AC   P67928; P00670;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 64.
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   Camelus dromedarius (Dromedary) (Arabian camel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX   NCBI_TaxID=9838;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=1167157; DOI=10.1042/bj1470505;
RA   Welling G.W., Groen G., Beintema J.J.;
RT   "The amino acid sequence of dromedary pancreatic ribonuclease.";
RL   Biochem. J. 147:505-511(1975).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE, AND SEQUENCE REVISION.
RX   PubMed=3922790; DOI=10.1016/0014-5793(85)80752-3;
RA   Beintema J.J.;
RT   "Mammalian ribonucleases. The absence of a glycosylated Asn-Pro-Thr
RT   sequence in horse ribonuclease and the presence of tryptophan at position
RT   39 in horse and dromedary ribonuclease.";
RL   FEBS Lett. 185:115-120(1985).
RN   [3]
RP   VARIANT GLN-103.
RX   PubMed=962846; DOI=10.1007/bf00484770;
RA   Welling G.W., Mulder H., Beintema J.J.;
RT   "Allelic polymorphism in arabian camel ribonuclease and the amino acid
RT   sequence of bactrian camel ribonuclease.";
RL   Biochem. Genet. 14:309-317(1976).
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   PIR; A00815; NRCM.
DR   PIR; A90229; NRCMM.
DR   AlphaFoldDB; P67928; -.
DR   SMR; P67928; -.
DR   STRING; 9838.ENSCDRP00005002599; -.
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; Secreted.
FT   CHAIN           1..124
FT                   /note="Ribonuclease pancreatic"
FT                   /id="PRO_0000057185"
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   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         103
FT                   /note="K -> Q (in 25% of the molecules)"
FT                   /evidence="ECO:0000269|PubMed:962846"
SQ   SEQUENCE   124 AA;  13939 MW;  503ABA0BAAEFE92F CRC64;
     SETAAEKFER QHMDSYSSSS SNSNYCNQMM KRREMTDGWC KPVNTFIHES LEDVQAVCSQ
     KSVTCKNGQT NCHQSSTTMH ITDCRETGSS KYPNCAYKAS NLKKHIIIAC EGNPYVPVHF
     DASV