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Protein

Seminal ribonuclease

Gene

SRN

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This enzyme hydrolyzes both single- and double-stranded RNA.

Catalytic activityi

Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates.1 Publication

Enzyme regulationi

Allosteric regulation by both substrate and reaction products.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei33Substrate1
Binding sitei36Substrate1
Active sitei38Proton acceptor1
Binding sitei92Substrate1
Binding sitei111Substrate1
Active sitei145Proton donor1

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • nucleic acid binding Source: InterPro
  • ribonuclease A activity Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Enzyme and pathway databases

BRENDAi3.1.27.5. 908.
SABIO-RKP00669.

Names & Taxonomyi

Protein namesi
Recommended name:
Seminal ribonuclease (EC:3.1.27.5)
Short name:
S-RNase
Short name:
Seminal RNase
Alternative name(s):
Ribonuclease BS-1
Gene namesi
Name:SRN
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 10

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1075179.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 261 PublicationAdd BLAST26
ChainiPRO_000003091027 – 150Seminal ribonucleaseAdd BLAST124

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi52 ↔ 110
Disulfide bondi57Interchain
Disulfide bondi58Interchain
Disulfide bondi66 ↔ 121
Disulfide bondi84 ↔ 136
Disulfide bondi91 ↔ 98
Modified residuei93Deamidated asparagine; by deterioration1 Publication1

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP00669.
PeptideAtlasiP00669.
PRIDEiP00669.

Expressioni

Tissue specificityi

Seminal plasma. Can reach 3% of the protein content of this fluid.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself7EBI-8524799,EBI-8524799

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

MINTiMINT-8050403.
STRINGi9913.ENSBTAP00000036091.

Chemistry databases

BindingDBiP00669.

Structurei

Secondary structure

1150
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi30 – 38Combined sources9
Helixi48 – 50Combined sources3
Helixi51 – 58Combined sources8
Turni59 – 62Combined sources4
Beta strandi63 – 65Combined sources3
Beta strandi68 – 73Combined sources6
Helixi77 – 81Combined sources5
Helixi82 – 85Combined sources4
Beta strandi86 – 89Combined sources4
Beta strandi92 – 94Combined sources3
Beta strandi98 – 100Combined sources3
Beta strandi105 – 112Combined sources8
Beta strandi123 – 137Combined sources15
Turni138 – 141Combined sources4
Beta strandi142 – 150Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
11BAX-ray2.06A/B27-150[»]
11BGX-ray1.90A/B27-150[»]
1BSRX-ray1.90A/B27-150[»]
1N1XX-ray1.45A27-150[»]
1N3ZX-ray1.65A27-150[»]
1QWQNMR-A27-150[»]
1R3MX-ray2.20A/B27-150[»]
1R5CX-ray2.10A/B27-150[»]
1R5DX-ray2.50A/B27-150[»]
1TQ9X-ray2.00A/B27-150[»]
1Y92X-ray2.20A/B27-150[»]
1Y94X-ray2.20A/B27-150[»]
2LFJNMR-A27-150[»]
3BCMX-ray2.25A/B27-150[»]
3BCOX-ray2.25A/B27-150[»]
3BCPX-ray2.57A/B/C/D27-150[»]
3DJOX-ray1.60A/B27-150[»]
3DJPX-ray1.60A/B27-150[»]
3DJQX-ray1.53A/B27-150[»]
3DJVX-ray1.60A/B27-150[»]
3DJXX-ray1.69A/B27-150[»]
4N4CX-ray2.48A/B27-150[»]
ProteinModelPortaliP00669.
SMRiP00669.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00669.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni67 – 71Substrate binding5

Sequence similaritiesi

Belongs to the pancreatic ribonuclease family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IYEN. Eukaryota.
ENOG41113F1. LUCA.
GeneTreeiENSGT00840000129759.
HOGENOMiHOG000276883.
HOVERGENiHBG008396.
InParanoidiP00669.
KOiK01168.
OMAiKSTMRIT.
OrthoDBiEOG091G15X3.
TreeFamiTF333393.

Family and domain databases

Gene3Di3.10.130.10. 1 hit.
InterProiIPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view]
PANTHERiPTHR11437. PTHR11437. 1 hit.
PfamiPF00074. RnaseA. 1 hit.
[Graphical view]
PRINTSiPR00794. RIBONUCLEASE.
ProDomiPD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00092. RNAse_Pc. 1 hit.
[Graphical view]
SUPFAMiSSF54076. SSF54076. 1 hit.
PROSITEiPS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00669-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALKSLVVLP LLVLVLLLVR VQPSLGKESA AAKFERQHMD SGNSPSSSSN
60 70 80 90 100
YCNLMMCCRK MTQGKCKPVN TFVHESLADV KAVCSQKKVT CKNGQTNCYQ
110 120 130 140 150
SKSTMRITDC RETGSSKYPN CAYKTTQVEK HIIVACGGKP SVPVHFDASV
Length:150
Mass (Da):16,377
Last modified:April 1, 1990 - v2
Checksum:iF7A05C930FB83A83
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51337 mRNA. Translation: CAA35716.1.
AJ000518 Genomic DNA. Translation: CAA04155.1.
S81747 Genomic DNA. Translation: AAB36140.1.
X03029 mRNA. Translation: CAA26832.1.
PIRiS08392. NRBOS.
RefSeqiNP_861526.1. NM_181810.1.
UniGeneiBt.22955.

Genome annotation databases

EnsembliENSBTAT00000036229; ENSBTAP00000036091; ENSBTAG00000025663.
GeneIDi280930.
KEGGibta:280930.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51337 mRNA. Translation: CAA35716.1.
AJ000518 Genomic DNA. Translation: CAA04155.1.
S81747 Genomic DNA. Translation: AAB36140.1.
X03029 mRNA. Translation: CAA26832.1.
PIRiS08392. NRBOS.
RefSeqiNP_861526.1. NM_181810.1.
UniGeneiBt.22955.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
11BAX-ray2.06A/B27-150[»]
11BGX-ray1.90A/B27-150[»]
1BSRX-ray1.90A/B27-150[»]
1N1XX-ray1.45A27-150[»]
1N3ZX-ray1.65A27-150[»]
1QWQNMR-A27-150[»]
1R3MX-ray2.20A/B27-150[»]
1R5CX-ray2.10A/B27-150[»]
1R5DX-ray2.50A/B27-150[»]
1TQ9X-ray2.00A/B27-150[»]
1Y92X-ray2.20A/B27-150[»]
1Y94X-ray2.20A/B27-150[»]
2LFJNMR-A27-150[»]
3BCMX-ray2.25A/B27-150[»]
3BCOX-ray2.25A/B27-150[»]
3BCPX-ray2.57A/B/C/D27-150[»]
3DJOX-ray1.60A/B27-150[»]
3DJPX-ray1.60A/B27-150[»]
3DJQX-ray1.53A/B27-150[»]
3DJVX-ray1.60A/B27-150[»]
3DJXX-ray1.69A/B27-150[»]
4N4CX-ray2.48A/B27-150[»]
ProteinModelPortaliP00669.
SMRiP00669.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-8050403.
STRINGi9913.ENSBTAP00000036091.

Chemistry databases

BindingDBiP00669.
ChEMBLiCHEMBL1075179.

Proteomic databases

PaxDbiP00669.
PeptideAtlasiP00669.
PRIDEiP00669.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000036229; ENSBTAP00000036091; ENSBTAG00000025663.
GeneIDi280930.
KEGGibta:280930.

Organism-specific databases

CTDi6035.

Phylogenomic databases

eggNOGiENOG410IYEN. Eukaryota.
ENOG41113F1. LUCA.
GeneTreeiENSGT00840000129759.
HOGENOMiHOG000276883.
HOVERGENiHBG008396.
InParanoidiP00669.
KOiK01168.
OMAiKSTMRIT.
OrthoDBiEOG091G15X3.
TreeFamiTF333393.

Enzyme and pathway databases

BRENDAi3.1.27.5. 908.
SABIO-RKP00669.

Miscellaneous databases

EvolutionaryTraceiP00669.
PROiP00669.

Family and domain databases

Gene3Di3.10.130.10. 1 hit.
InterProiIPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view]
PANTHERiPTHR11437. PTHR11437. 1 hit.
PfamiPF00074. RnaseA. 1 hit.
[Graphical view]
PRINTSiPR00794. RIBONUCLEASE.
ProDomiPD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00092. RNAse_Pc. 1 hit.
[Graphical view]
SUPFAMiSSF54076. SSF54076. 1 hit.
PROSITEiPS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRNS_BOVIN
AccessioniPrimary (citable) accession number: P00669
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1990
Last modified: November 2, 2016
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Progressive deamidation of Asn-93 transforms the homodimer (beta- 2) into and heterodimer (alpha-beta) and finally a doubly deamidated dimer (alpha-2).1 Publication

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.