ID   RNL2_CHICK              Reviewed;         121 AA.
AC   P81476;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Ribonuclease CL2;
DE            Short=RNase CL2;
DE            EC=3.1.27.-;
DE   AltName: Full=Poly C preferential ribonuclease;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RX   PubMed=8407869; DOI=10.1093/oxfordjournals.jbchem.a124132;
RA   Hayano K., Iwama M., Sakamoto H., Watanabe H., Sanda A., Ohgi K., Irie M.;
RT   "Characterization of poly C preferential ribonuclease from chicken liver.";
RL   J. Biochem. 114:156-162(1993).
CC   -!- FUNCTION: Pyrimidine-specific nuclease with preference for C.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000305}.
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DR   PIR; JX0279; JX0279.
DR   AlphaFoldDB; P81476; -.
DR   SMR; P81476; -.
DR   STRING; 9031.ENSGALP00000031533; -.
DR   PaxDb; P81476; -.
DR   VEuPathDB; HostDB:geneid_422633; -.
DR   eggNOG; ENOG502S9Q1; Eukaryota.
DR   HOGENOM; CLU_117006_3_1_1; -.
DR   InParanoid; P81476; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004540; F:ribonuclease activity; IBA:GO_Central.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
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;
KW   Nuclease; Reference proteome; Secreted.
FT   CHAIN           1..121
FT                   /note="Ribonuclease CL2"
FT                   /id="PRO_0000057164"
FT   ACT_SITE        11
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        114
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         6
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         9
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         43..47
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        26..81
FT                   /evidence="ECO:0000250"
FT   DISULFID        42..92
FT                   /evidence="ECO:0000250"
FT   DISULFID        60..107
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   121 AA;  13433 MW;  E421FF92B329104E CRC64;
     ETRYEKFLRQ HVDHPRTLGL MGHRYCAVML ARRQVTAPGR PCKPSNTFVH APAEDLVATC
     TRPADATGFH STSTPMDITA CRLRGGDTRP PCNYRARQLH HHVRVSCLDG LPVHLAGTHA
     S