P84844 (RNAS1_CHEMY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Ribonuclease EC=3.1.27.5
Organism	Chelonia mydas (Green sea-turtle) (Chelonia agassizi)
Taxonomic identifier	8469 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Testudines › Cryptodira › Chelonioidea › Cheloniidae › Chelonia

Protein attributes

Sequence length	119 AA.
Sequence status	Complete.
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 By similarity. UniProtKB P07998
Catalytic activity	Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates. UniProtKB P07998
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 Ref.1.
Sequence similarities	Belongs to the pancreatic ribonuclease family.
Mass spectrometry	Molecular mass is 12942.1 Da from positions 1 - 119. Determined by MALDI. Ref.1 Molecular mass is 12967.8 Da from positions 1 - 119. Determined by MALDI. Variant Leu-37. Ref.1

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	nucleic acid binding Inferred from electronic annotation. Source: InterPro pancreatic ribonuclease activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 119

119

Ribonuclease

PRO_0000234484

Regions

Region

41 – 45

5

Substrate binding By similarity UniProtKB P07998

Sites

Active site

11

1

Proton acceptor By similarity UniProtKB P07998

Active site

114

1

Proton donor By similarity UniProtKB P07998

Binding site

6

1

Substrate By similarity UniProtKB P07998

Binding site

9

1

Substrate By similarity UniProtKB P07998

Binding site

82

1

Substrate By similarity UniProtKB P07998

Amino acid modifications

Disulfide bond

26 ↔ 81

Ref.2 UniProtKB P07998

Disulfide bond

40 ↔ 92

Ref.2 UniProtKB P07998

Disulfide bond

58 ↔ 107

Ref.2 UniProtKB P07998

Natural variations

Natural variant

37

1

S → L. Ref.1

Secondary structure

1

.

.

.

.

.

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.

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.

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.

.

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119

Helix Strand Turn

Details...

Helix

3 – 11

9

Helix

22 – 32

11

Beta strand

37 – 39

3

Beta strand

42 – 47

6

Helix

51 – 55

5

Beta strand

69 – 71

3

Beta strand

76 – 83

8

Beta strand

98 – 101

4

Beta strand

103 – 107

5

Beta strand

112 – 118

7

Sequences

	Sequence		Length	Mass (Da)
	P84844 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: 702C2F204A28056E	FASTA	119	12,947
	10 20 30 40 50 60 ETRYEKFLRQ HVDYPRTAAP DTRTYCNQMM QRRGMTSPVC KFTNTFVHAS AASITTICGP 70 80 90 100 110 GGAPAGGNLR DSTASFALTT CRLQGGSQRP PCNYNGGTST QRIRIACDGG LPVHYDRAI

References

[1]	"The complete amino acid sequence of green turtle (Chelonia mydas) egg white ribonuclease." Katekaew S., Torikata T., Araki T. Protein J. 25:316-327(2006) [PubMed: 16947078] [Abstract] Cited for: PROTEIN SEQUENCE, SUBCELLULAR LOCATION, MASS SPECTROMETRY, VARIANT LEU-37. Tissue: Egg white.
[2]	"Structure of the newly found green turtle egg-white ribonuclease." Katekaew S., Kuaprasert B., Torikata T., Kakuta Y., Kimura M., Yoneda K., Araki T. Acta Crystallogr. F 66:755-759(2010) [PubMed: 20606267] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), DISULFIDE BONDS.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ZPO	X-ray	1.60	A	1-119	[»]

ProteinModelPortal

P84844.

SMR

P84844. Positions 1-119.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG008396.

Family and domain databases

InterPro

IPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[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]

SUPFAM

SSF54076. RNaseA. 1 hit.

PROSITE

PS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RNAS1_CHEMY

Accession

Primary (citable) accession number: P84844

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	May 16, 2006
Last modified:	May 31, 2011
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program