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Protein

Seminal ribonuclease

Gene

SRN

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

Functioni

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

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

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

  • endonuclease activity Source: GO_Central
  • identical protein binding Source: IntAct
  • nucleic acid binding Source: InterPro
  • ribonuclease A activity Source: UniProtKB-EC
  • ribonuclease activity Source: UniProtKB

GO - Biological processi

  • RNA phosphodiester bond hydrolysis Source: UniProtKB

Keywordsi

Molecular functionAllosteric enzyme, Endonuclease, Hydrolase, Nuclease

Enzyme and pathway databases

BRENDAi3.1.27.5 908
SABIO-RKiP00669

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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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

MINTiP00669
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

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
GeneTreeiENSGT00900000140967
HOGENOMiHOG000276883
HOVERGENiHBG008396
InParanoidiP00669
KOiK01168
OMAiHIIVACH
OrthoDBiEOG091G15X3
TreeFamiTF333393

Family and domain databases

Gene3Di3.10.130.10, 1 hit
InterProiView protein in InterPro
IPR001427 RNaseA
IPR036816 RNaseA-like_dom_sf
IPR023411 RNaseA_AS
IPR023412 RNaseA_domain
PANTHERiPTHR11437 PTHR11437, 1 hit
PfamiView protein in Pfam
PF00074 RnaseA, 1 hit
PRINTSiPR00794 RIBONUCLEASE
ProDomiView protein in ProDom or Entries sharing at least one domain
PD000535 RNaseA, 1 hit
SMARTiView protein in SMART
SM00092 RNAse_Pc, 1 hit
SUPFAMiSSF54076 SSF54076, 1 hit
PROSITEiView protein in PROSITE
PS00127 RNASE_PANCREATIC, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiRNS_BOVIN
AccessioniPrimary (citable) accession number: P00669
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1990
Last modified: February 28, 2018
This is version 158 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, 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

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