ID RNAS4_RAT Reviewed; 147 AA. AC O55004; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 24-JAN-2024, entry version 147. DE RecName: Full=Ribonuclease 4; DE Short=RNase 4; DE EC=3.1.27.- {ECO:0000250|UniProtKB:P34096}; DE AltName: Full=RL3; DE Flags: Precursor; GN Name=Rnase4; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RX PubMed=9602056; DOI=10.1016/s0167-4838(97)00213-6; RA Zhao W., Kote-Jarai Z., van Santen Y., Hofsteenge J., Beintema J.J.; RT "Ribonucleases from rat and bovine liver: purification, specificity and RT structural characterization."; RL Biochim. Biophys. Acta 1384:55-65(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Heart; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Cleaves preferentially after uridine bases. Has antimicrobial CC activity against uropathogenic E.coli (UPEC). Probably contributes to CC urinary tract sterility. {ECO:0000250|UniProtKB:P34096}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P34096}. CC Note=Detected in urine. {ECO:0000250|UniProtKB:P34096}. CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF041066; AAC23487.1; -; mRNA. DR EMBL; BC070953; AAH70953.1; -; mRNA. DR RefSeq; NP_064467.1; NM_020082.2. DR RefSeq; XP_006251968.1; XM_006251906.2. DR RefSeq; XP_006251969.1; XM_006251907.3. DR AlphaFoldDB; O55004; -. DR SMR; O55004; -. DR STRING; 10116.ENSRNOP00000043003; -. DR jPOST; O55004; -. DR PaxDb; 10116-ENSRNOP00000043003; -. DR Ensembl; ENSRNOT00000041495.5; ENSRNOP00000043003.2; ENSRNOG00000025625.6. DR Ensembl; ENSRNOT00000089631.2; ENSRNOP00000073131.2; ENSRNOG00000025625.6. DR Ensembl; ENSRNOT00055042281; ENSRNOP00055034513; ENSRNOG00055024574. DR Ensembl; ENSRNOT00055042293; ENSRNOP00055034525; ENSRNOG00055024574. DR Ensembl; ENSRNOT00055042314; ENSRNOP00055034546; ENSRNOG00055024574. DR Ensembl; ENSRNOT00055042319; ENSRNOP00055034551; ENSRNOG00055024574. DR Ensembl; ENSRNOT00060046679; ENSRNOP00060038815; ENSRNOG00060026945. DR Ensembl; ENSRNOT00060046708; ENSRNOP00060038840; ENSRNOG00060026945. DR Ensembl; ENSRNOT00060046729; ENSRNOP00060038859; ENSRNOG00060026945. DR Ensembl; ENSRNOT00060046748; ENSRNOP00060038877; ENSRNOG00060026945. DR Ensembl; ENSRNOT00065055665; ENSRNOP00065045831; ENSRNOG00065032343. DR Ensembl; ENSRNOT00065055675; ENSRNOP00065045841; ENSRNOG00065032343. DR Ensembl; ENSRNOT00065055680; ENSRNOP00065045846; ENSRNOG00065032343. DR Ensembl; ENSRNOT00065055685; ENSRNOP00065045851; ENSRNOG00065032343. DR GeneID; 56759; -. DR KEGG; rno:56759; -. DR UCSC; RGD:61823; rat. DR AGR; RGD:61823; -. DR CTD; 6038; -. DR RGD; 61823; Rnase4. DR eggNOG; ENOG502S9Q1; Eukaryota. DR GeneTree; ENSGT00940000157645; -. DR HOGENOM; CLU_117006_3_1_1; -. DR InParanoid; O55004; -. DR OMA; MMHRRRM; -. DR OrthoDB; 4596772at2759; -. DR PhylomeDB; O55004; -. DR TreeFam; TF333393; -. DR PRO; PR:O55004; -. DR Proteomes; UP000002494; Chromosome 15. DR Bgee; ENSRNOG00000025625; Expressed in liver and 18 other cell types or tissues. DR ExpressionAtlas; O55004; baseline. DR GO; GO:0005576; C:extracellular region; ISO:RGD. DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB. 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:RNA nuclease activity; ISO:RGD. DR GO; GO:0019731; P:antibacterial humoral response; ISS:UniProtKB. DR GO; GO:0009267; P:cellular response to starvation; ISO:RGD. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central. DR CDD; cd06265; RNase_A_canonical; 1. DR Gene3D; 3.10.130.10; Ribonuclease A-like domain; 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; RIBONUCLEASE; 1. DR PANTHER; PTHR11437:SF53; RIBONUCLEASE 4; 1. DR Pfam; PF00074; RnaseA; 1. DR PRINTS; PR00794; RIBONUCLEASE. DR SMART; SM00092; RNAse_Pc; 1. DR SUPFAM; SSF54076; RNase A-like; 1. DR PROSITE; PS00127; RNASE_PANCREATIC; 1. DR Genevisible; O55004; RN. PE 1: Evidence at protein level; KW Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond; KW Endonuclease; Hydrolase; Nuclease; Pyrrolidone carboxylic acid; KW Reference proteome; Secreted; Signal. FT SIGNAL 1..28 FT /evidence="ECO:0000250" FT CHAIN 29..147 FT /note="Ribonuclease 4" FT /id="PRO_0000030887" FT ACT_SITE 40 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:Q9H1E1" FT ACT_SITE 144 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:Q9H1E1" FT BINDING 35 FT /ligand="dUMP" FT /ligand_id="ChEBI:CHEBI:246422" FT /evidence="ECO:0000250|UniProtKB:P15468" FT BINDING 40 FT /ligand="dUMP" FT /ligand_id="ChEBI:CHEBI:246422" FT /evidence="ECO:0000250|UniProtKB:P15468" FT BINDING 68 FT /ligand="dUMP" FT /ligand_id="ChEBI:CHEBI:246422" FT /evidence="ECO:0000250|UniProtKB:P15468" FT BINDING 71 FT /ligand="dUMP" FT /ligand_id="ChEBI:CHEBI:246422" FT /evidence="ECO:0000250|UniProtKB:P15468" FT BINDING 72 FT /ligand="dUMP" FT /ligand_id="ChEBI:CHEBI:246422" FT /evidence="ECO:0000250|UniProtKB:P15468" FT BINDING 145 FT /ligand="dUMP" FT /ligand_id="ChEBI:CHEBI:246422" FT /evidence="ECO:0000250|UniProtKB:P15468" FT MOD_RES 29 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000250|UniProtKB:P15467" FT DISULFID 53..109 FT /evidence="ECO:0000250|UniProtKB:P34096" FT DISULFID 67..120 FT /evidence="ECO:0000250|UniProtKB:P34096" FT DISULFID 85..135 FT /evidence="ECO:0000250|UniProtKB:P34096" FT DISULFID 92..99 FT /evidence="ECO:0000250|UniProtKB:P34096" SQ SEQUENCE 147 AA; 16903 MW; 110D54CF7C691BB3 CRC64; MDIQRTQSLL LLLLLTLLGL GLVQPSYGQD RMYQRFLRQH VDPEGTGGSD NYCNVMMQRR RMTSTQCKRF NTFIHEDIWN IRSICDTANI PCKNGNMNCH EGIVRVTDCR ETGSSVPHNC RYRARASTRR VVIACEGTPE VPVHFDR //