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Protein

Ribonuclease-like 3

Gene

rnasel3

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Ribonuclease. Angiogenic. Plays a role in host defense. Exhibits strong antibacterial activity against Gram-negative bacteria but mild antibacterial activity against Gram-positive bacteria. The RNase activity is not required for the bactericidal activity.4 Publications

Miscellaneous

Although the OmpT protease is absent in Gram-positive bacteria, LF-ZF3 generated by a Gram-negative bacterium can penetrate a Gram-positive bacterium and exert its cytotoxicity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei38Proton acceptor1 Publication1
Active sitei142Proton donor1 Publication1

GO - Molecular functioni

  • endonuclease activity Source: UniProtKB-KW
  • ribonuclease activity Source: ZFIN
  • RNA binding Source: ZFIN

GO - Biological processi

Keywordsi

Molecular functionAntibiotic, Antimicrobial, Developmental protein, Endonuclease, Hydrolase, Nuclease
Biological processAngiogenesis, Differentiation, Immunity

Enzyme and pathway databases

BRENDAi3.1.27.5 928

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease-like 31 Publication (EC:3.1.27.-)
Short name:
RNase ZF-31 Publication
Short name:
RNase-like 31 Publication
Short name:
ZF-RNase-31 Publication
Alternative name(s):
Dr-RNase 11 Publication
Cleaved into the following 2 chains:
N-terminal peptide1 Publication
LF-ZF31 Publication
Gene namesi
Name:rnasel3Imported
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Unplaced

Organism-specific databases

ZFINiZDB-GENE-050809-5 rnasel3

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 221 PublicationAdd BLAST22
ChainiPRO_000039440423 – 149Ribonuclease-like 3Sequence analysisAdd BLAST127
PeptideiPRO_000039440523 – 55N-terminal peptide1 PublicationAdd BLAST33
PeptideiPRO_000039440656 – 149LF-ZF31 PublicationAdd BLAST94

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei23Pyrrolidone carboxylic acidBy similarity1
Disulfide bondi48 ↔ 1091 Publication
Disulfide bondi66 ↔ 1201 Publication
Disulfide bondi84 ↔ 1351 Publication

Post-translational modificationi

Cleavage between Arg-55 and Arg-56 is catalyzed by a membrane-localized Gram-negative bacterium protease (OmpT in E.coli). The excised fragment is then transported to the bacterium cytosol for cleavage of the disulfide bridge linking Cys-48 and Cys-109, thus separating the N-terminal and LF-ZF3. LF-ZF3 but not the N-terminal peptide possesses bactericidal activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei55Cleavage1 Publication1

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiA5HAK0

Expressioni

Tissue specificityi

Strongly expressed in the adult liver and gut, and weakly in the heart and testis.1 Publication

Developmental stagei

Only expressed in adults.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi7955.ENSDARP00000123763

Structurei

Secondary structure

1149
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi28 – 38Combined sources11
Helixi48 – 54Combined sources7
Beta strandi58 – 63Combined sources6
Beta strandi68 – 75Combined sources8
Helixi77 – 81Combined sources5
Helixi82 – 84Combined sources3
Beta strandi87 – 90Combined sources4
Beta strandi92 – 94Combined sources3
Beta strandi97 – 102Combined sources6
Beta strandi104 – 113Combined sources10
Beta strandi121 – 136Combined sources16
Beta strandi139 – 147Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VQ9X-ray1.85A23-149[»]
SMRiA5HAK0
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA5HAK0

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni67 – 71Substrate binding1 Publication5

Sequence similaritiesi

Belongs to the pancreatic ribonuclease family.Sequence analysis

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IZBW Eukaryota
ENOG410Y4FD LUCA
HOGENOMiHOG000276883
HOVERGENiHBG008396
InParanoidiA5HAK0
KOiK16631
PhylomeDBiA5HAK0

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.

A5HAK0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGIHQCTAVV LLLLCASLST YGQPAEIRRR YEHFLTQHVY GGITEQTCDR
60 70 80 90 100
VMRQRRITRF PTGNDCKEVN TFIQANGNHV RTVCTGGGTR QTDNRDLYMS
110 120 130 140
NNQFTVITCT LRSGERHPNC RYRGKESSRK IVVACEGEWP THYEKGVIV
Length:149
Mass (Da):17,011
Last modified:June 15, 2010 - v2
Checksum:i096E21A32D5B6479
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti25A → M no nucleotide entry (PubMed:16861230).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti5Q → R in allele ZF-3d and allele ZF-3e. 1 Publication1
Natural varianti56R → G in allele ZF-3a and allele ZF-3c. 2 Publications1
Natural varianti93D → E in allele ZF-3c. 1 Publication1
Natural varianti102N → D in allele ZF-3e. 1 Publication1
Natural varianti137G → S in allele ZF-3c. 1 Publication1
Natural varianti141T → A in allele ZF-3e. 1 Publication1
Natural varianti145K → R in allele ZF-3d and allele ZF-3e. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF382669 mRNA Translation: ABQ23783.1
BX465197 Genomic DNA No translation available.
RefSeqiNP_001092923.1, NM_001099453.1
UniGeneiDr.134029

Genome annotation databases

GeneIDi798787
KEGGidre:798787

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiRNSL3_DANRE
AccessioniPrimary (citable) accession number: A5HAK0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: April 25, 2018
This is version 65 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health