RNAS4_BOVIN
ID RNAS4_BOVIN Reviewed; 147 AA.
AC P15467; F1N6N1; Q3T184; Q58DP6; Q9TV33;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 5.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Ribonuclease 4;
DE Short=RNase 4;
DE EC=3.1.27.-;
DE AltName: Full=Ribonuclease BL4;
DE Flags: Precursor;
GN Name=RNASE4; Synonyms=RNS4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford;
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 29-147, SIGNAL SEQUENCE CLEAVAGE SITE, AND
RP PYROGLUTAMATE FORMATION AT GLN-29.
RC TISSUE=Liver;
RX PubMed=2358434; DOI=10.1093/oxfordjournals.jbchem.a123095;
RA Hosoya K., Nagareda Y., Hasemi S., Sanda A., Takizawa Y., Watanabe H.,
RA Ohgi K., Irie M.;
RT "Primary structure of an alkaline ribonuclease from bovine liver.";
RL J. Biochem. 107:613-618(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-147.
RA Deming M.S., Dyer K.D., Seekamp R.L., Rosenberg H.F.;
RT "Evolution of three primate ribonuclease genes: comparative analysis of
RT RNase 4, RNase k6, and RNase 2 (eosinophil-derived neurotoxin).";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This RNase has marked specificity towards the 3' side of
CC uridine nucleotides.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
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DR EMBL; BT021551; AAX46398.1; -; mRNA.
DR EMBL; BC102072; AAI02073.2; -; mRNA.
DR EMBL; AF078116; AAD48530.1; -; Genomic_DNA.
DR PIR; JX0115; JX0115.
DR RefSeq; NP_001035680.1; NM_001040590.1.
DR AlphaFoldDB; P15467; -.
DR SMR; P15467; -.
DR STRING; 9913.ENSBTAP00000026127; -.
DR PaxDb; P15467; -.
DR PRIDE; P15467; -.
DR Ensembl; ENSBTAT00000026127; ENSBTAP00000026127; ENSBTAG00000019612.
DR GeneID; 616089; -.
DR KEGG; bta:616089; -.
DR CTD; 6038; -.
DR VEuPathDB; HostDB:ENSBTAG00000019612; -.
DR VGNC; VGNC:33998; RNASE4.
DR eggNOG; ENOG502S9Q1; Eukaryota.
DR GeneTree; ENSGT00940000162981; -.
DR HOGENOM; CLU_117006_3_1_1; -.
DR InParanoid; P15467; -.
DR OMA; GARNPNC; -.
DR OrthoDB; 1549558at2759; -.
DR TreeFam; TF333393; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000019612; Expressed in liver and 105 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; Pyrrolidone carboxylic acid; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:2358434"
FT CHAIN 29..147
FT /note="Ribonuclease 4"
FT /id="PRO_0000057162"
FT ACT_SITE 40
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 144
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 68..72
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 29
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:2358434"
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"
FT CONFLICT 31
FT /note="R -> G (in Ref. 4; AAD48530)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="E -> Q (in Ref. 4; AAD48530)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="K -> G (in Ref. 4; AAD48530)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 147 AA; 16938 MW; 25F75B2E465BC81E CRC64;
MALQRTQAFL LLLLLTLLGL GLVQPSYGQD RMYQRFLRQH VDPDETGGND SYCNLMMQRR
KMTSHQCKRF NTFIHEDLWN IRSICSTTNI QCKNGQMNCH EGVVRVTDCR ETGSSRAPNC
RYRAKASTRR VVIACEGNPE VPVHFDK
