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P00662 (RNAS1_GIRCA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease pancreatic

EC=3.1.27.5
Alternative name(s):
RNase 1
RNase A
Gene names
Name:RNASE1
Synonyms:RNS1
OrganismGiraffa camelopardalis (Giraffe)
Taxonomic identifier9894 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraGiraffidaeGiraffa

Protein attributes

Sequence length124 AA.
Sequence statusComplete.
Protein existenceEvidence 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 By similarity.

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. Interacts with and forms tight 1:1 complexes with RNH1. Dimerization of two such complexes may occur. Interaction with RNH1 inhibits this protein By similarity.

Subcellular location

Secreted.

Tissue specificity

Pancreas.

Sequence similarities

Belongs to the pancreatic ribonuclease family.

Ontologies

Keywords
   Cellular componentSecreted
   Molecular functionEndonuclease
Hydrolase
Nuclease
   PTMDisulfide bond
Glycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionnucleic acid binding

Inferred from electronic annotation. Source: InterPro

pancreatic ribonuclease activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 124124Ribonuclease pancreatic
PRO_0000057198

Regions

Region41 – 455Substrate binding By similarity

Sites

Active site121Proton acceptor By similarity
Active site1191Proton donor By similarity
Binding site71Substrate By similarity
Binding site101Substrate By similarity
Binding site661Substrate By similarity
Binding site851Substrate By similarity

Amino acid modifications

Glycosylation341N-linked (GlcNAc...) Ref.2
Disulfide bond26 ↔ 84 By similarity
Disulfide bond40 ↔ 95 By similarity
Disulfide bond58 ↔ 110 By similarity
Disulfide bond65 ↔ 72 By similarity

Natural variations

Natural variant761Y → N.

Experimental info

Sequence conflict281E → Q AA sequence Ref.1
Sequence conflict281E → Q AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P00662 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: CE97EBDC792612DA

FASTA12413,704
        10         20         30         40         50         60 
KESAAAKFER QHIDSSTSSV SSSNYCNEMM TSRNLTQDRC KPVNTFVHES LADVQAVCSQ 

        70         80         90        100        110        120 
KNVACKNGQT NCYQSYSAMS ITDCRETGNS KYPNCAYQTT QAEKHIIVAC EGNPYVPVHY 


DASV 

« Hide

References

[1]Gaastra W.
Thesis (1975), University of Groningen, Netherlands
Cited for: PROTEIN SEQUENCE.
[2]"The primary structure of giraffe pancreatic ribonuclease."
Gaastra W., Groen G., Welling G.W., Beintema J.J.
FEBS Lett. 41:227-232(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[3]"Molecular evolution of genes encoding ribonucleases in ruminant species."
Confalone E., Beintema J.J., Sasso M.P., Carsana A., Palmieri M., Vento M.T., Furia A.
J. Mol. Evol. 41:850-858(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Sequences related to the ox pancreatic ribonuclease coding region in the genomic DNA of mammalian species."
Breukelman H.J., Beintema J.J., Confalone E., Costanzo C., Sasso M.P., Carsana A., Palmieri M., Furia A.
J. Mol. Evol. 37:29-35(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-114.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S81739 Genomic DNA. Translation: AAB36133.1.
S65127 Genomic DNA. Translation: AAB27932.1.
PIRNRGF. A94452.

3D structure databases

ProteinModelPortalP00662.
SMRP00662. Positions 1-124.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG008396.

Family and domain databases

Gene3D3.10.130.10. 1 hit.
InterProIPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view]
PANTHERPTHR11437. PTHR11437. 1 hit.
PfamPF00074. RnaseA. 1 hit.
[Graphical view]
PRINTSPR00794. RIBONUCLEASE.
ProDomPD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00092. RNAse_Pc. 1 hit.
[Graphical view]
SUPFAMSSF54076. SSF54076. 1 hit.
PROSITEPS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRNAS1_GIRCA
AccessionPrimary (citable) accession number: P00662
Secondary accession number(s): Q29534, Q29541
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families