Neutrophil defensin 3 precursor - Homo sapiens (Human)

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P59666 (DEF3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 97. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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:

HP 3-56
Neutrophil defensin 2
Alternative name(s):
HNP-2
Short name=HP-2
Short name=HP2

Gene names

Name:	DEFA3
Synonyms:	DEF3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	94 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Antiviral defense
Cellular component	Secreted
Domain	Signal
Molecular function	Antibiotic Antimicrobial Defensin Fungicide
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW defense response to fungus Inferred from electronic annotation. Source: UniProtKB-KW defense response to virus Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Traceable author statement. Source: Reactome killing of cells of other organism Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi lumen Traceable author statement. Source: Reactome azurophil granule lumen Traceable author statement. Source: Reactome extracellular region Traceable author statement. Source: Reactome extracellular space Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

Propeptide

20 – 38

PRO_0000006777

Chain

39 – 94

HP 3-56

PRO_0000006778

Peptide

65 – 94

Neutrophil defensin 3 Ref.6

PRO_0000006779

Peptide

66 – 94

Neutrophil defensin 2

PRO_0000006780

Amino acid modifications

Disulfide bond

Disulfide bond

Disulfide bond

Secondary structure

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P59666 [UniParc].

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

FASTA

10,245

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

        70         80         90 
RKNMDCYCRI PACIAGERRY GTCIYQGRLW AFCC

« Hide

References

	« Hide 'large scale' referencesShow '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.

IPI

IPI00021827.

PIR

C40499.

RefSeq

NP_005208.1. NM_005217.3.

UniGene

Hs.654448.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DFN	X-ray	1.90	A/B	65-94	[»]
1ZMH	X-ray	1.50	A/B/C/D	66-94	[»]
1ZMI	X-ray	1.15	A/B/C/D	66-94	[»]
1ZMK	X-ray	1.30	A/B	66-94	[»]
2PM4	X-ray	1.95	A/B	65-94	[»]
2PM5	X-ray	2.40	A/B	65-94	[»]

ProteinModelPortal

P59666.

ModBase

Search...

Protein-protein interaction databases

IntAct

P59666. 2 interactions.

MINT

MINT-1409240.

STRING

9606.ENSP00000328359.

PTM databases

PhosphoSite

P59666.

Polymorphism databases

DMDM

30316323.

Proteomic databases

PaxDb

P59666.

PRIDE

P59666.

Protocols and materials databases

DNASU

1668.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000327857; ENSP00000328359; ENSG00000239839.

GeneID

1668.

KEGG

hsa:1668.

Organism-specific databases

CTD

1668.

GeneCards

GC08M006875.

HGNC

HGNC:2762. DEFA3.

HPA

HPA052517.

MIM

604522. gene.

neXtProt

NX_P59666.

PharmGKB

PA27239.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG86943.

HOGENOM

HOG000233351.

HOVERGEN

HBG011703.

InParanoid

P59666.

K05230.

OMA

IFVEDER.

OrthoDB

EOG4GF3GT.

PhylomeDB

P59666.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P59666.

Bgee

P59666.

CleanEx

HS_DEFA3.

Genevestigator

P59666.

GermOnline

ENSG00000185918. Homo sapiens.

Family and domain databases

InterPro

IPR016327. Alpha-defensin.
IPR006080. Defensin_beta/neutrophil.
IPR002366. Defensin_propep.
IPR006081. Mammalian_defensins.
[Graphical view]

Pfam

PF00323. Defensin_1. 1 hit.
PF00879. Defensin_propep. 1 hit.
[Graphical view]

PIRSF

PIRSF001875. Alpha-defensin. 1 hit.

SMART

SM00048. DEFSN. 1 hit.
[Graphical view]

PROSITE

PS00269. DEFENSIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P59666.

GenomeRNAi

1668.

NextBio

6864.

PMAP-CutDB

P59666.

SOURCE

Search...

Entry information

Entry name

DEF3_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

Human chromosome 8

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents