Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P59666 (DEF3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Neutrophil defensin 3
Alternative name(s):
Defensin, alpha 3
HNP-3
Short name=HP-3
Short name=HP3

Cleaved into the following 2 chains:

  1. HP 3-56
  2. Neutrophil defensin 2
    Alternative name(s):
    HNP-2
    Short name=HP-2
    Short name=HP2
Gene names
Name:DEFA3
Synonyms:DEF3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length94 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Defensin 2 and defensin 3 have antibiotic, fungicide and antiviral activities. Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane. Ref.9 Ref.10 Ref.11 Ref.12

Subunit structure

Dimer. Ref.10 Ref.12

Subcellular location

Secreted.

Sequence similarities

Belongs to the alpha-defensin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919
Propeptide20 – 3819
PRO_0000006777
Chain39 – 9456HP 3-56
PRO_0000006778
Peptide65 – 9430Neutrophil defensin 3 Ref.6
PRO_0000006779
Peptide66 – 9429Neutrophil defensin 2
PRO_0000006780

Amino acid modifications

Disulfide bond66 ↔ 94 Ref.7 Ref.11
Disulfide bond68 ↔ 83 Ref.7 Ref.11
Disulfide bond73 ↔ 93 Ref.7 Ref.11

Secondary structure

...... 94
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P59666 [UniParc].

Last modified April 30, 2003. Version 1.
Checksum: 0E0F8E957376C6AF

FASTA9410,245
        10         20         30         40         50         60 
MRTLAILAAI LLVALQAQAE PLQARADEVA AAPEQIAADI PEVVVSLAWD ESLAPKHPGS 

        70         80         90 
RKNMDCYCRI PACIAGERRY GTCIYQGRLW AFCC 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of human defensin cDNA clones."
Daher K.A., Lehrer R.I., Ganz T., Kronenberg M.
Proc. Natl. Acad. Sci. U.S.A. 85:7327-7331(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Differentiation stage-specific expression of a gene during granulopoiesis."
Wiedemann L.M., Francis G.E., Lamb R.F., Burns J.H., Winnie J.N., McKenzie E.D., Birnie G.D.
Leukemia 3:227-234(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The structure of neutrophil defensin genes."
Linzmeier R., Michaelson D., Liu L., Ganz T.
FEBS Lett. 321:267-273(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]Erratum
Linzmeier R., Michaelson D., Liu L., Ganz T.
FEBS Lett. 326:299-300(1993) [PubMed] [Europe PMC] [Abstract]
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreas and Spleen.
[6]"Primary structures of three human neutrophil defensins."
Selsted M.E., Harwig S.S.L., Ganz T., Schilling J.W., Lehrer R.I.
J. Clin. Invest. 76:1436-1439(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 65-94.
[7]"Determination of the disulfide array in the human defensin HNP-2. A covalently cyclized peptide."
Selsted M.E., Harwig S.S.L.
J. Biol. Chem. 264:4003-4007(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[8]"Posttranslational processing of defensins in immature human myeloid cells."
Valore E.V., Ganz T.
Blood 79:1538-1544(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[9]"Antibacterial activity and specificity of the six human alpha-defensins."
Ericksen B., Wu Z., Lu W., Lehrer R.I.
Antimicrob. Agents Chemother. 49:269-275(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization."
Hill C.P., Yee J., Selsted M.E., Eisenberg D.
Science 251:1481-1485(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF DEFENSIN 3, SUBUNIT, FUNCTION.
[11]"Reconstruction of the conserved beta-bulge in mammalian defensins using D-amino acids."
Xie C., Prahl A., Ericksen B., Wu Z., Zeng P., Li X., Lu W.-Y., Lubkowski J., Lu W.
J. Biol. Chem. 280:32921-32929(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 66-94, DISULFIDE BONDS, FUNCTION.
[12]"Toward understanding the cationicity of defensins. Arg and Lys versus their noncoded analogs."
Zou G., de Leeuw E., Li C., Pazgier M., Li C., Zeng P., Lu W.-Y., Lubkowski J., Lu W.
J. Biol. Chem. 282:19653-19665(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 65-94, FUNCTION, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M21131 mRNA. Translation: AAA35753.2.
M23281 mRNA. Translation: AAA52304.1.
L12691 Genomic DNA. Translation: AAB57722.1.
X13621 mRNA. Translation: CAA31952.1.
BC027917 mRNA. Translation: AAH27917.1.
PIRC40499.
RefSeqNP_005208.1. NM_005217.3.
UniGeneHs.654448.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DFNX-ray1.90A/B65-94[»]
1ZMHX-ray1.50A/B/C/D66-94[»]
1ZMIX-ray1.15A/B/C/D66-94[»]
1ZMKX-ray1.30A/B66-94[»]
2PM4X-ray1.95A/B65-94[»]
2PM5X-ray2.40A/B65-94[»]
ProteinModelPortalP59666.
SMRP59666. Positions 66-94.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP59666. 2 interactions.
MINTMINT-1409240.
STRING9606.ENSP00000328359.

PTM databases

PhosphoSiteP59666.

Polymorphism databases

DMDM30316323.

Proteomic databases

PaxDbP59666.
PRIDEP59666.

Protocols and materials databases

DNASU1668.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000327857; ENSP00000328359; ENSG00000239839.
GeneID1668.
KEGGhsa:1668.

Organism-specific databases

CTD1668.
GeneCardsGC08M006875.
HGNCHGNC:2762. DEFA3.
HPAHPA052517.
MIM604522. gene.
neXtProtNX_P59666.
PharmGKBPA27239.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG86943.
HOGENOMHOG000233351.
HOVERGENHBG011703.
InParanoidP59666.
KOK05230.
OMAQERDDEA.
OrthoDBEOG75TMFQ.
PhylomeDBP59666.
TreeFamTF338414.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

BgeeP59666.
CleanExHS_DEFA3.
GenevestigatorP59666.

Family and domain databases

InterProIPR016327. Alpha-defensin.
IPR006080. Defensin_beta/neutrophil.
IPR002366. Defensin_propep.
IPR006081. Mammalian_defensins.
[Graphical view]
PANTHERPTHR11876. PTHR11876. 1 hit.
PfamPF00323. Defensin_1. 1 hit.
PF00879. Defensin_propep. 1 hit.
[Graphical view]
PIRSFPIRSF001875. Alpha-defensin. 1 hit.
SMARTSM00048. DEFSN. 1 hit.
[Graphical view]
PROSITEPS00269. DEFENSIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP59666.
GeneWikiDEFA3.
GenomeRNAi1668.
NextBio6864.
PMAP-CutDBP59666.
PROP59666.
SOURCESearch...

Entry information

Entry nameDEF3_HUMAN
AccessionPrimary (citable) accession number: P59666
Secondary accession number(s): P11479, Q14125
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 30, 2003
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM