RNAS4_HUMAN
ID RNAS4_HUMAN Reviewed; 147 AA.
AC P34096;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Ribonuclease 4;
DE Short=RNase 4;
DE EC=3.1.27.-;
DE Flags: Precursor;
GN Name=RNASE4; Synonyms=RNS4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RX PubMed=7742370; DOI=10.1016/0167-4781(95)00040-n;
RA Seno M., Futami J., Tsushima Y., Akutagawa K., Kosaka M., Tada H.,
RA Yamada H.;
RT "Molecular cloning and expression of human ribonuclease 4 cDNA.";
RL Biochim. Biophys. Acta 1261:424-426(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-147.
RX PubMed=7501448; DOI=10.1093/nar/23.21.4290;
RA Rosenberg H.F., Dyer K.D.;
RT "Human ribonuclease 4 (RNase 4): coding sequence, chromosomal localization
RT and identification of two distinct transcripts in human somatic tissues.";
RL Nucleic Acids Res. 23:4290-4295(1995).
RN [4]
RP PROTEIN SEQUENCE OF 29-147, PYROGLUTAMATE FORMATION AT GLN-29, AND
RP DISULFIDE BONDS.
RC TISSUE=Plasma;
RX PubMed=8223579; DOI=10.1111/j.1432-1033.1993.tb18259.x;
RA Zhou H.-M., Strydom D.J.;
RT "The amino acid sequence of human ribonuclease 4, a highly conserved
RT ribonuclease that cleaves specifically on the 3' side of uridine.";
RL Eur. J. Biochem. 217:401-410(1993).
RN [5]
RP CHARACTERIZATION.
RX PubMed=3467790; DOI=10.1021/bi00371a002;
RA Shapiro R., Fett J.W., Strydom D.J., Vallee B.L.;
RT "Isolation and characterization of a human colon carcinoma-secreted enzyme
RT with pancreatic ribonuclease-like activity.";
RL Biochemistry 25:7255-7264(1986).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 29-147.
RX PubMed=9878400; DOI=10.1006/jmbi.1998.2288;
RA Terzyan S.S., Peracaula R., de Llorens R., Tsushima Y., Yamada H., Seno M.,
RA Gomis-Rueth F.-X., Coll M.;
RT "The three-dimensional structure of human RNase 4, unliganded and complexed
RT with d(Up), reveals the basis for its uridine selectivity.";
RL J. Mol. Biol. 285:205-214(1999).
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; D37931; BAA07150.1; -; mRNA.
DR EMBL; BC015520; AAH15520.1; -; mRNA.
DR EMBL; U36775; AAA96750.1; -; Genomic_DNA.
DR CCDS; CCDS9555.1; -.
DR PIR; I52489; I52489.
DR RefSeq; NP_001269121.1; NM_001282192.1.
DR RefSeq; NP_001269122.1; NM_001282193.1.
DR RefSeq; NP_002928.1; NM_002937.4.
DR RefSeq; NP_919412.1; NM_194431.2.
DR PDB; 1RNF; X-ray; 2.10 A; A/B=29-147.
DR PDB; 2RNF; X-ray; 2.40 A; A/B=29-147.
DR PDBsum; 1RNF; -.
DR PDBsum; 2RNF; -.
DR AlphaFoldDB; P34096; -.
DR SMR; P34096; -.
DR BioGRID; 111967; 13.
DR IntAct; P34096; 1.
DR STRING; 9606.ENSP00000452245; -.
DR DrugBank; DB03448; 2'-Deoxyuridine 3'-Monophosphate.
DR BioMuta; RNASE4; -.
DR DMDM; 1710614; -.
DR jPOST; P34096; -.
DR MassIVE; P34096; -.
DR PaxDb; P34096; -.
DR PeptideAtlas; P34096; -.
DR PRIDE; P34096; -.
DR ProteomicsDB; 54939; -.
DR Antibodypedia; 57712; 78 antibodies from 15 providers.
DR DNASU; 6038; -.
DR Ensembl; ENST00000397995.2; ENSP00000381081.2; ENSG00000258818.4.
DR Ensembl; ENST00000555597.1; ENSP00000451624.1; ENSG00000258818.4.
DR Ensembl; ENST00000555835.3; ENSP00000452245.1; ENSG00000258818.4.
DR GeneID; 6038; -.
DR KEGG; hsa:6038; -.
DR MANE-Select; ENST00000555835.3; ENSP00000452245.1; NM_002937.5; NP_002928.1.
DR CTD; 6038; -.
DR DisGeNET; 6038; -.
DR GeneCards; RNASE4; -.
DR HGNC; HGNC:10047; RNASE4.
DR HPA; ENSG00000258818; Tissue enriched (liver).
DR MalaCards; RNASE4; -.
DR MIM; 601030; gene.
DR neXtProt; NX_P34096; -.
DR OpenTargets; ENSG00000258818; -.
DR PharmGKB; PA34415; -.
DR VEuPathDB; HostDB:ENSG00000258818; -.
DR eggNOG; ENOG502S9Q1; Eukaryota.
DR GeneTree; ENSGT00940000157645; -.
DR HOGENOM; CLU_117006_3_1_1; -.
DR InParanoid; P34096; -.
DR OMA; VPNCRYR; -.
DR PhylomeDB; P34096; -.
DR TreeFam; TF333393; -.
DR PathwayCommons; P34096; -.
DR SignaLink; P34096; -.
DR BioGRID-ORCS; 6038; 10 hits in 1063 CRISPR screens.
DR ChiTaRS; RNASE4; human.
DR EvolutionaryTrace; P34096; -.
DR GeneWiki; Ribonuclease_4; -.
DR GenomeRNAi; 6038; -.
DR Pharos; P34096; Tbio.
DR PRO; PR:P34096; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P34096; protein.
DR Bgee; ENSG00000258818; Expressed in right lobe of liver and 93 other tissues.
DR ExpressionAtlas; P34096; baseline and differential.
DR Genevisible; P34096; HS.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004522; F:ribonuclease A activity; NAS:UniProtKB.
DR GO; GO:0004540; F:ribonuclease activity; IDA:BHF-UCL.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR GO; GO:0006379; P:mRNA cleavage; NAS:UniProtKB.
DR GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IDA:BHF-UCL.
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 3D-structure; Direct protein sequencing; Disulfide bond; Endonuclease;
KW Hydrolase; Nuclease; Pyrrolidone carboxylic acid; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:8223579"
FT CHAIN 29..147
FT /note="Ribonuclease 4"
FT /id="PRO_0000030883"
FT ACT_SITE 40
FT /note="Proton acceptor"
FT ACT_SITE 144
FT /note="Proton donor"
FT BINDING 38
FT /ligand="substrate"
FT BINDING 68..72
FT /ligand="substrate"
FT BINDING 93
FT /ligand="substrate"
FT BINDING 110
FT /ligand="substrate"
FT MOD_RES 29
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:8223579"
FT DISULFID 53..109
FT /evidence="ECO:0000269|PubMed:8223579"
FT DISULFID 67..120
FT /evidence="ECO:0000269|PubMed:8223579"
FT DISULFID 85..135
FT /evidence="ECO:0000269|PubMed:8223579"
FT DISULFID 92..99
FT /evidence="ECO:0000269|PubMed:8223579"
FT VARIANT 16
FT /note="T -> S (in dbSNP:rs3748338)"
FT /id="VAR_024618"
FT CONFLICT 54
FT /note="N -> D (in Ref. 3; AAA96750)"
FT /evidence="ECO:0000305"
FT HELIX 29..40
FT /evidence="ECO:0007829|PDB:1RNF"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:1RNF"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:1RNF"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:1RNF"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:1RNF"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:1RNF"
FT STRAND 99..111
FT /evidence="ECO:0007829|PDB:1RNF"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1RNF"
FT STRAND 122..136
FT /evidence="ECO:0007829|PDB:1RNF"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:1RNF"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:1RNF"
SQ SEQUENCE 147 AA; 16840 MW; 4C24FEA249F3EC2F CRC64;
MALQRTHSLL LLLLLTLLGL GLVQPSYGQD GMYQRFLRQH VHPEETGGSD RYCNLMMQRR
KMTLYHCKRF NTFIHEDIWN IRSICSTTNI QCKNGKMNCH EGVVKVTDCR DTGSSRAPNC
RYRAIASTRR VVIACEGNPQ VPVHFDG
