RNAS4_MOUSE
ID RNAS4_MOUSE Reviewed; 148 AA.
AC Q9JJH1;
DT 19-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Ribonuclease 4;
DE Short=RNase 4;
DE EC=3.1.27.-;
DE Flags: Precursor;
GN Name=Rnase4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ikegawa S., Nakamura Y.;
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: This RNase has marked specificity towards the 3' side of
CC uridine nucleotides. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
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DR EMBL; AB041044; BAA96476.1; -; mRNA.
DR EMBL; BC005569; AAH05569.1; -; mRNA.
DR CCDS; CCDS27035.1; -.
DR AlphaFoldDB; Q9JJH1; -.
DR SMR; Q9JJH1; -.
DR STRING; 10090.ENSMUSP00000127274; -.
DR MaxQB; Q9JJH1; -.
DR PaxDb; Q9JJH1; -.
DR PeptideAtlas; Q9JJH1; -.
DR PRIDE; Q9JJH1; -.
DR ProteomicsDB; 300455; -.
DR MGI; MGI:1926217; Rnase4.
DR eggNOG; ENOG502S9Q1; Eukaryota.
DR InParanoid; Q9JJH1; -.
DR PhylomeDB; Q9JJH1; -.
DR ChiTaRS; Rnase4; mouse.
DR PRO; PR:Q9JJH1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9JJH1; protein.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
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; ISO:MGI.
DR GO; GO:0009267; P:cellular response to starvation; IEP:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; ISO:MGI.
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 Disulfide bond; Endonuclease; Hydrolase; Nuclease;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000250"
FT CHAIN 30..148
FT /note="Ribonuclease 4"
FT /id="PRO_0000030885"
FT ACT_SITE 41
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 145
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 69..73
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 30
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P15467"
FT DISULFID 54..110
FT /evidence="ECO:0000250|UniProtKB:P34096"
FT DISULFID 68..121
FT /evidence="ECO:0000250|UniProtKB:P34096"
FT DISULFID 86..136
FT /evidence="ECO:0000250|UniProtKB:P34096"
FT DISULFID 93..100
FT /evidence="ECO:0000250|UniProtKB:P34096"
SQ SEQUENCE 148 AA; 17025 MW; 470DB6629AFC87A3 CRC64;
MMDLQRTQSL LLLLVLTLLG LGLVQPSYGQ DRMYQRFLRQ HVDPQATGGN DNYCNVMMQR
RKMTSVQCKR FNTFIHEDIW NIRGICSTTN ILCKNGQMNC HEGVVKVTDC RETGNSKAPN
CRYRARTSTR RVVIACEGDP EVPVHFDR
