Reviewed, UniProtKB/Swiss-Prot P07998 (RNAS1_HUMAN)

Names and origin

Protein names

Recommended name:
    Ribonuclease pancreatic
    EC=3.1.27.5
Alternative name(s):
    RNase 1
    RNase A
    RNase UpI-1
    RIB-1
    HP-RNase

Gene names

Name:	RNASE1
Synonyms:	RIB1, RNS1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	156 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA.
Catalytic activity	Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates.
Subunit structure	Monomer.
Subcellular location	Secreted.
Tissue specificity	Pancreas and other tissues and body fluids (indicating it may have other physiological functions besides its role in digestion).
Post-translational modification	N-linked glycans are of complex type.
Sequence similarities	Belongs to the pancreatic ribonuclease family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from direct assay. Source: HPA extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: HPA
Molecular function	nucleic acid binding Inferred from electronic annotation. Source: InterPro pancreatic ribonuclease activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

28

Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Chain

29 – 156

128

Ribonuclease pancreatic

PRO_0000030921

Regions

Region

69 – 73

5

Substrate binding By similarity

Sites

Active site

40

1

Proton acceptor

Active site

147

1

Proton donor

Binding site

35

1

Substrate By similarity

Binding site

38

1

Substrate By similarity

Binding site

94

1

Substrate By similarity

Binding site

113

1

Substrate By similarity

Amino acid modifications

Glycosylation

62

1

N-linked (GlcNAc...); partial Ref.8

Glycosylation

104

1

N-linked (GlcNAc...) Ref.8

Glycosylation

116

1

N-linked (GlcNAc...) Ref.8

Disulfide bond

54 ↔ 112

Disulfide bond

68 ↔ 123

Disulfide bond

86 ↔ 138

Disulfide bond

93 ↔ 100

Experimental info

Mutagenesis

116 – 117

2

NG → RS: No effect on inhibition by RNase inhibitor 1. Ref.13

Sequence conflict

2

1

A → G in CAA55817. Ref.4

Sequence conflict

4

1

Missing in AAB35096. Ref.5

Sequence conflict

9 – 11

3

RLL → VLP in AAB35096. Ref.5

Sequence conflict

16 – 22

7

ILLVLGW → VLLLVR in AAB35096. Ref.5

Sequence conflict

151

1

S → T in CAA55817. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

156

Helix Strand Turn

Details...

Helix

32 – 40

9

Helix

53 – 60

8

Beta strand

65 – 67

3

Beta strand

70 – 75

6

Helix

79 – 84

6

Helix

85 – 87

3

Beta strand

88 – 91

4

Beta strand

100 – 102

3

Beta strand

107 – 114

8

Beta strand

125 – 139

15

Turn

140 – 143

4

Beta strand

144 – 152

9

Sequences

	Sequence		Length	Mass (Da)
	P07998-1 [UniParc]. Last modified February 1, 1996. Version 4. Checksum: F63B17B8B55115F9	FASTA	156	17,644
	10 20 30 40 50 60 MALEKSLVRL LLLVLILLVL GWVQPSLGKE SRAKKFQRQH MDSDSSPSSS STYCNQMMRR 70 80 90 100 110 120 RNMTQGRCKP VNTFVHEPLV DVQNVCFQEK VTCKNGQGNC YKSNSSMHIT DCRLTNGSRY 130 140 150 PNCAYRTSPK ERHIIVACEG SPYVPVHFDA SVEDST

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence encoding human pancreatic ribonuclease." Seno M., Fatami J.I., Kosaka M., Seno S., Yamada H. Biochim. Biophys. Acta 1218:466-468(1994) [PubMed: 8049276] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Pancreas.
[2]	"Duplication and divergence of two distinct pancreatic ribnuclease genes in leaf-eating African and Asian colobine monkeys." Schienman J.E., Holt R.A., Auerbach M.R., Stewart C.B. Mol. Biol. Evol. 23:1465-1479(2006) [PubMed: 16751256] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas and Prostate.
[4]	"Primary structure of the coding part of the gene for human pancreatic ribonuclease and its chromosomal location." Kochetov A.V., Lukasheva V.V., Filipenko M.L., Mertvetsov N.P., Rivkin M.I. Bioorg. Khim. 21:691-694(1995) [PubMed: 8588814] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-152. Tissue: Placenta.
[5]	"Expression in mammalian cells, purification and characterization of recombinant human pancreatic ribonuclease." Russo N., de Nigris M., Ciardiello A., Di Donato A., D'Alessio G. FEBS Lett. 369:352-352(1995) [PubMed: 7649283] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-155.
[6]	"The DNA sequences of the human and hamster secretory ribonucleases determined with the polymerase chain reaction (PCR)." Haugg M., Schein C.H. Nucleic Acids Res. 20:612-612(1992) [PubMed: 1741299] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-149. Tissue: Placenta.
[7]	"The amino acid sequence of human pancreatic ribonuclease." Beintema J.J., Wietzes P., Weickmann J.L., Glitz D.G. Anal. Biochem. 136:48-64(1984) [PubMed: 6201087] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-156. Tissue: Pancreas.
[8]	"Differences in glycosylation pattern of human secretory ribonucleases." Beintema J.J., Blank A., Schieven G.L., Dekker C.A., Sorrentino S., Libonati M. Biochem. J. 255:501-505(1988) [PubMed: 3202829] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-156, GLYCOSYLATION AT ASN-62; ASN-104 AND ASN-116.
[9]	"Purification and characterization of three ribonucleases from human kidney: comparison with urine ribonucleases." Mizuta K., Awazu S., Yasuda T., Kishi K. Arch. Biochem. Biophys. 281:144-151(1990) [PubMed: 2383019] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-47.
[10]	"A putative mouse oocyte maturation inhibitory protein from urine of pregnant women: N-terminal sequence homology with human nonsecretory ribonuclease." Sakakibara R., Hashida K., Tominaga N., Sakai K., Ishiguro M., Imamura S., Ohmatsu F., Sato E. Chem. Pharm. Bull. 39:146-149(1991) [PubMed: 2049798] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-43.
[11]	"Characterization of a unique nonsecretory ribonuclease from urine of pregnant women." Sakakibara R., Hashida K., Kitahara T., Ishiguro M. J. Biochem. 111:325-330(1992) [PubMed: 1587793] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-48. Tissue: Urine.
[12]	"Two distinct secretory ribonucleases from human cerebrum: purification, characterization and relationships to other ribonucleases." Yasuda T., Nadano D., Takeshita H., Kishi K. Biochem. J. 296:617-625(1993) [PubMed: 8280059] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-49.
[13]	"Three-dimensional structure of a human pancreatic ribonuclease variant, a step forward in the design of cytotoxic ribonucleases." Pous J., Canals A., Terzyan S.S., Guasch A., Benito A., Ribo M., Vilanova M., Coll M. J. Mol. Biol. 303:49-60(2000) [PubMed: 11021969] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 38-156, MUTAGENESIS OF 116-ASN-GLY-117.
[14]	"Three-dimensional structure of human RNase 1 delta N7 at 1.9 A resolution." Pous J., Mallorqui-Fernandez G., Peracaula R., Terzyan S.S., Futami J., Tada H., Yamada H., Seno M., de Llorens R., Gomis-Rueth F.-X., Coll M. Acta Crystallogr. D 57:498-505(2001) [PubMed: 11264578] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 35-153.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

D26129 mRNA. Translation: BAA05124.1.
DQ494867 Genomic DNA. Translation: ABF00144.1.
BC005324 mRNA. Translation: AAH05324.1.
BC022882 mRNA. Translation: AAH22882.1.
X79235 Genomic DNA. Translation: CAA55817.1.
S79281 mRNA. Translation: AAB35096.1.
X62946 Genomic DNA. Translation: CAA44718.1.

IPI

IPI00014048.

PIR

I53530.
NRHU1. S45003.

RefSeq

NP_002924.1.
NP_937875.1.
NP_937877.1.
NP_937878.1.

UniGene

Hs.78224

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DZA	X-ray	1.65	A/B	29-156	[»]
1E21	X-ray	1.90	A	29-156	[»]
1H8X	X-ray	2.00	A/B	29-156	[»]
1Z7X	X-ray	1.95	X/Z	29-156	[»]
2E0J	X-ray	1.60	A/B	29-156	[»]
2E0L	X-ray	1.60	A/B	29-156	[»]
2E0M	X-ray	1.70	A/B	29-156	[»]
2E0O	X-ray	2.00	A/B	29-156	[»]
2K11	NMR	-	A	29-155	[»]
2Q4G	X-ray	1.95	X/Z	29-156	[»]
3F8G	X-ray	2.60	A/B	29-153	[»]

ModBase

Search...

Proteomic databases

PeptideAtlas

P07998.

PRIDE

P07998.

Genome annotation databases

Ensembl

ENSG00000129538. Homo sapiens. [Contig view]

GeneID

6035.

KEGG

hsa:6035.

Organism-specific databases

GeneCards

GC14M020339.

H-InvDB

HIX0011495.

HGNC

HGNC:10044. RNASE1.

HPA

HPA001140.

MIM

180440. gene.

PharmGKB

PA34412.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P07998.

HOVERGEN

P07998.

OMA

P07998. NCAYRTS.

Enzyme and pathway databases

BRENDA

3.1.27.5. 247.

Gene expression databases

ArrayExpress

P07998.

Bgee

P07998.

CleanEx

HS_RNASE1.

GermOnline

ENSG00000129538. Homo sapiens.

Family and domain databases

InterPro

IPR001427. RNaseA.
[Graphical view]

Gene3D

G3DSA:3.10.130.10. RNaseA. 1 hit.

PANTHER

PTHR11437. RNaseA. 1 hit.

Pfam

PF00074. RnaseA. 1 hit.
[Graphical view]

PRINTS

PR00794. RIBONUCLEASE.

ProDom

PD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00092. RNAse_Pc. 1 hit.
[Graphical view]

PROSITE

PS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

23515.

SOURCE

Search...

Entry information

Entry name

RNAS1_HUMAN

Accession

Primary (citable) accession number: P07998
Secondary accession number(s): Q16830 , Q16869, Q1KHR2, Q9UCB4, Q9UCB5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 112 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)