Ribonuclease 4

RNASE4

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1RNF, 2RNF

Identifiers

Aliases

RNASE4, RAB1, RNS4, Ribonuclease 4, ribonuclease A family member 4

External IDs

MGI: 1926217 HomoloGene: 10576 GeneCards: RNASE4

Gene ontology
Molecular function	• nuclease activity • endonuclease activity • ribonuclease activity • hydrolase activity • ribonuclease A activity • nucleic acid binding
Cellular component	• extracellular region • extracellular exosome
Biological process	• mRNA cleavage • RNA phosphodiester bond hydrolysis, endonucleolytic
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


6038


58809

Ensembl


ENSG00000258818


ENSMUSG00000021876

UniProt


P34096


Q9JJH1

RefSeq (mRNA)


NM_194431 NM_001282192 NM_001282193 NM_002937 NM_194430


NM_021472 NM_201239

RefSeq (protein)


NP_001269121.1 NP_001269122.1 NP_002928.1 NP_919412.1


n/a

Location (UCSC)

Chr 14: 20.68 – 20.7 Mb

Chr 14: 51.09 – 51.11 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Ribonuclease 4 is an enzyme that in humans is encoded by the RNASE4 gene.^[3]^[4]

The protein encoded by this gene belongs to the pancreatic ribonuclease family. It plays an important role in mRNA cleavage and has marked specificity towards the 3' side of uridine nucleotides. Alternative splicing results in two transcript variants encoding the same protein. This gene and the gene that encodes angiogenin share promoters and 5' exons. Each gene splices to a unique downstream exon that contains its complete coding region.^[4]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Rosenberg HF, Dyer KD (Jan 1996). "Human ribonuclease 4 (RNase 4): coding sequence, chromosomal localization and identification of two distinct transcripts in human somatic tissues". Nucleic Acids Res. 23 (21): 4290–5. doi:10.1093/nar/23.21.4290. PMC 307382. PMID 7501448.
1 2 "Entrez Gene: RNASE4 ribonuclease, RNase A family, 4".

Shapiro R, Fett JW, Strydom DJ, Vallee BL (1987). "Isolation and characterization of a human colon carcinoma-secreted enzyme with pancreatic ribonuclease-like activity.". Biochemistry. 25 (23): 7255–64. doi:10.1021/bi00371a002. PMID 3467790.
Seno M, Futami J, Tsushima Y, et al. (1995). "Molecular cloning and expression of human ribonuclease 4 cDNA.". Biochim. Biophys. Acta. 1261 (3): 424–6. doi:10.1016/0167-4781(95)00040-n. PMID 7742370.
Zhou HM, Strydom DJ (1993). "The amino acid sequence of human ribonuclease 4, a highly conserved ribonuclease that cleaves specifically on the 3' side of uridine.". Eur. J. Biochem. 217 (1): 401–10. doi:10.1111/j.1432-1033.1993.tb18259.x. PMID 8223579.
Egesten A, Dyer KD, Batten D, et al. (1997). "Ribonucleases and host defense: identification, localization and gene expression in adherent monocytes in vitro.". Biochim. Biophys. Acta. 1358 (3): 255–60. doi:10.1016/S0167-4889(97)00081-5. PMID 9366257.
Terzyan SS, Peracaula R, de Llorens R, et al. (1999). "The three-dimensional structure of human RNase 4, unliganded and complexed with d(Up), reveals the basis for its uridine selectivity.". J. Mol. Biol. 285 (1): 205–14. doi:10.1006/jmbi.1998.2288. PMID 9878400.
Xu XR, Huang J, Xu ZG, et al. (2002). "Insight into hepatocellular carcinogenesis at transcriptome level by comparing gene expression profiles of hepatocellular carcinoma with those of corresponding noncancerous liver.". Proc. Natl. Acad. Sci. U.S.A. 98 (26): 15089–94. doi:10.1073/pnas.241522398. PMC 64988. PMID 11752456.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.

PDB gallery

1rnf: X-RAY CRYSTAL STRUCTURE OF UNLIGANDED HUMAN RIBONUCLEASE 4

2rnf: X-RAY CRYSTAL STRUCTURE OF HUMAN RIBONUCLEASE 4 IN COMPLEX WITH D(UP)

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases

Lipase

Phospholipase
- A1
- A2
- B

3.1.2: Thioesterase

3.1.3: Phosphatase

3.1.4: Phosphodiesterase

3.1.6: Sulfatase

Nuclease (includes
deoxyribonuclease and
ribonuclease)

3.1.11-16: Exonuclease

Exodeoxyribonuclease	RecBCD

Exoribonuclease	Oligonucleotidase

3.1.21-31: Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme UvrABC endonuclease

Endoribonuclease	RNase III RNase H 1 2A 2B 2C RNase P RNase A 1 2 3 4/5 RNase T1 RNA-induced silencing complex

either deoxy- or ribo-	Aspergillus nuclease S1 Micrococcal nuclease

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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Ribonuclease 4

References

Further reading