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Protein

Neutrophil defensin 1

Gene

DEFA1

more
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Defensin 1 and defensin 2 have antibacterial, 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.2 Publications

GO - Biological processi

  • antibacterial humoral response Source: UniProtKB
  • chemotaxis Source: ProtInc
  • defense response to fungus Source: UniProtKB-KW
  • defense response to Gram-positive bacterium Source: UniProtKB
  • defense response to virus Source: UniProtKB-KW
  • immune response Source: ProtInc
  • innate immune response Source: UniProtKB
  • innate immune response in mucosa Source: UniProtKB
  • intracellular estrogen receptor signaling pathway Source: UniProtKB
  • killing of cells of other organism Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Defensin, Fungicide

Keywords - Biological processi

Antiviral defense

Enzyme and pathway databases

ReactomeiR-HSA-1461973. Defensins.
R-HSA-1462054. Alpha-defensins.
R-HSA-6798695. Neutrophil degranulation.

Protein family/group databases

TCDBi1.C.19.1.1. the defensin (defensin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Neutrophil defensin 1
Alternative name(s):
Defensin, alpha 1
HNP-1
Short name:
HP-1
Short name:
HP1
Cleaved into the following 2 chains:
Alternative name(s):
HNP-2
Short name:
HP-2
Short name:
HP2
Gene namesi
Name:DEFA1
Synonyms:DEF1, DEFA2, MRS
AND
Name:DEFA1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:2761. DEFA1.
HGNC:33596. DEFA1B.

Subcellular locationi

GO - Cellular componenti

  • azurophil granule lumen Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • Golgi lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi1667.
728358.
OpenTargetsiENSG00000206047.
ENSG00000240247.
PharmGKBiPA165585475.

Polymorphism and mutation databases

DMDMi30316322.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
PropeptideiPRO_000000677120 – 38Add BLAST19
ChainiPRO_000000677239 – 94HP 1-56Add BLAST56
PeptideiPRO_000000677365 – 94Neutrophil defensin 1Add BLAST30
PeptideiPRO_000000677466 – 94Neutrophil defensin 2Add BLAST29

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi66 ↔ 941 Publication
Disulfide bondi68 ↔ 831 Publication
Disulfide bondi73 ↔ 931 Publication
Modified residuei78ADP-ribosylarginine; by ART11 Publication1
Modified residuei85Phosphotyrosine1 Publication1
Modified residuei88ADP-ribosylarginine; by ART11 Publication1

Post-translational modificationi

ADP-ribosylation drastically reduces cytotoxic and antibacterial activities, and enhances IL8 production.
Phosphorylation at Tyr-85 has been found in some cancer cell lines, and interferes with ADP-ribosylation.1 Publication

Keywords - PTMi

ADP-ribosylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP59665.
PeptideAtlasiP59665.
PRIDEiP59665.
TopDownProteomicsiP59665.

PTM databases

iPTMnetiP59665.
PhosphoSitePlusiP59665.

Miscellaneous databases

PMAP-CutDBP59665.

Expressioni

Gene expression databases

BgeeiENSG00000206047.
CleanExiHS_DEFA1.
GenevisibleiP59665. HS.

Organism-specific databases

HPAiCAB032548.
HPA052517.

Interactioni

Subunit structurei

Dimer.1 Publication

Protein-protein interaction databases

BioGridi108031. 83 interactors.
608786. 3 interactors.
IntActiP59665. 6 interactors.
MINTiMINT-6631351.
STRINGi9606.ENSP00000372136.

Structurei

Secondary structure

194
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi66 – 72Combined sources7
Beta strandi79 – 85Combined sources7
Beta strandi88 – 93Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KHTNMR-A65-94[»]
2PM1X-ray1.60A65-94[»]
3GNYX-ray1.56A/B65-94[»]
3H6CX-ray1.63A/B65-94[»]
3HJ2X-ray1.40A/B65-94[»]
3HJDX-ray1.65A/B65-94[»]
3LO1X-ray1.60A65-94[»]
3LO2X-ray1.56A/B65-94[»]
3LO4X-ray1.75A/B65-94[»]
3LO6X-ray1.56A/B65-94[»]
3LO9X-ray1.56A/B65-94[»]
3LOEX-ray1.56A65-94[»]
3LVXX-ray1.63A/B65-94[»]
4DU0X-ray1.90A/B/C/D65-94[»]
4LB1X-ray2.00A/B/D/E65-94[»]
4LB7X-ray1.90A/B/D/E65-94[»]
4LBBX-ray1.72A/B65-94[»]
4LBFX-ray1.70A/B/C/D/E/F/G/H65-94[»]
ProteinModelPortaliP59665.
SMRiP59665.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP59665.

Family & Domainsi

Sequence similaritiesi

Belongs to the alpha-defensin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410JK0K. Eukaryota.
ENOG41116GP. LUCA.
GeneTreeiENSGT00730000111183.
HOGENOMiHOG000233351.
HOVERGENiHBG011703.
InParanoidiP59665.
KOiK05230.
OMAiRVWAFCC.
OrthoDBiEOG091G12GE.
PhylomeDBiP59665.
TreeFamiTF338414.

Family and domain databases

InterProiIPR006081. Alpha-defensin.
IPR016327. Alpha-defensin_pro.
IPR006080. Defensin_beta/alpha.
IPR002366. Defensin_propep.
[Graphical view]
PANTHERiPTHR11876. PTHR11876. 1 hit.
PfamiPF00323. Defensin_1. 1 hit.
PF00879. Defensin_propep. 1 hit.
[Graphical view]
PIRSFiPIRSF001875. Alpha-defensin. 1 hit.
SMARTiSM00048. DEFSN. 1 hit.
[Graphical view]
PROSITEiPS00269. DEFENSIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P59665-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTLAILAAI LLVALQAQAE PLQARADEVA AAPEQIAADI PEVVVSLAWD
60 70 80 90
ESLAPKHPGS RKNMACYCRI PACIAGERRY GTCIYQGRLW AFCC
Length:94
Mass (Da):10,201
Last modified:April 30, 2003 - v1
Checksum:i0E0F8E95737396FA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21130 mRNA. Translation: AAA52302.1.
M26602 mRNA. Translation: AAA52303.1.
L12690 Genomic DNA. Translation: AAA36382.1.
X52053 mRNA. Translation: CAA36280.1.
AF200455 Genomic DNA. Translation: AAT68875.1.
AF200455 Genomic DNA. Translation: AAT68878.1.
AF200455 Genomic DNA. Translation: AAT68879.1.
AF200455 Genomic DNA. Translation: AAT68880.1.
AF238378 Genomic DNA. Translation: AAT68883.1.
AF238378 Genomic DNA. Translation: AAT68884.1.
BC069423 mRNA. Translation: AAH69423.1.
BC093791 mRNA. Translation: AAH93791.1.
BC112188 mRNA. Translation: AAI12189.1.
CCDSiCCDS34797.1.
CCDS43691.1.
PIRiS32499. A40499.
RefSeqiNP_001035965.1. NM_001042500.1.
NP_004075.1. NM_004084.3.
UniGeneiHs.380781.

Genome annotation databases

EnsembliENST00000382679; ENSP00000372126; ENSG00000206047.
ENST00000382689; ENSP00000372136; ENSG00000240247.
ENST00000382692; ENSP00000372139; ENSG00000206047.
GeneIDi1667.
728358.
KEGGihsa:1667.
hsa:728358.
UCSCiuc003wqv.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21130 mRNA. Translation: AAA52302.1.
M26602 mRNA. Translation: AAA52303.1.
L12690 Genomic DNA. Translation: AAA36382.1.
X52053 mRNA. Translation: CAA36280.1.
AF200455 Genomic DNA. Translation: AAT68875.1.
AF200455 Genomic DNA. Translation: AAT68878.1.
AF200455 Genomic DNA. Translation: AAT68879.1.
AF200455 Genomic DNA. Translation: AAT68880.1.
AF238378 Genomic DNA. Translation: AAT68883.1.
AF238378 Genomic DNA. Translation: AAT68884.1.
BC069423 mRNA. Translation: AAH69423.1.
BC093791 mRNA. Translation: AAH93791.1.
BC112188 mRNA. Translation: AAI12189.1.
CCDSiCCDS34797.1.
CCDS43691.1.
PIRiS32499. A40499.
RefSeqiNP_001035965.1. NM_001042500.1.
NP_004075.1. NM_004084.3.
UniGeneiHs.380781.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KHTNMR-A65-94[»]
2PM1X-ray1.60A65-94[»]
3GNYX-ray1.56A/B65-94[»]
3H6CX-ray1.63A/B65-94[»]
3HJ2X-ray1.40A/B65-94[»]
3HJDX-ray1.65A/B65-94[»]
3LO1X-ray1.60A65-94[»]
3LO2X-ray1.56A/B65-94[»]
3LO4X-ray1.75A/B65-94[»]
3LO6X-ray1.56A/B65-94[»]
3LO9X-ray1.56A/B65-94[»]
3LOEX-ray1.56A65-94[»]
3LVXX-ray1.63A/B65-94[»]
4DU0X-ray1.90A/B/C/D65-94[»]
4LB1X-ray2.00A/B/D/E65-94[»]
4LB7X-ray1.90A/B/D/E65-94[»]
4LBBX-ray1.72A/B65-94[»]
4LBFX-ray1.70A/B/C/D/E/F/G/H65-94[»]
ProteinModelPortaliP59665.
SMRiP59665.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108031. 83 interactors.
608786. 3 interactors.
IntActiP59665. 6 interactors.
MINTiMINT-6631351.
STRINGi9606.ENSP00000372136.

Protein family/group databases

TCDBi1.C.19.1.1. the defensin (defensin) family.

PTM databases

iPTMnetiP59665.
PhosphoSitePlusiP59665.

Polymorphism and mutation databases

DMDMi30316322.

Proteomic databases

PaxDbiP59665.
PeptideAtlasiP59665.
PRIDEiP59665.
TopDownProteomicsiP59665.

Protocols and materials databases

DNASUi1667.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000382679; ENSP00000372126; ENSG00000206047.
ENST00000382689; ENSP00000372136; ENSG00000240247.
ENST00000382692; ENSP00000372139; ENSG00000206047.
GeneIDi1667.
728358.
KEGGihsa:1667.
hsa:728358.
UCSCiuc003wqv.2. human.

Organism-specific databases

CTDi1667.
728358.
DisGeNETi1667.
728358.
GeneCardsiDEFA1.
DEFA1B.
HGNCiHGNC:2761. DEFA1.
HGNC:33596. DEFA1B.
HPAiCAB032548.
HPA052517.
MIMi125220. gene.
neXtProtiNX_P59665.
OpenTargetsiENSG00000206047.
ENSG00000240247.
PharmGKBiPA165585475.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410JK0K. Eukaryota.
ENOG41116GP. LUCA.
GeneTreeiENSGT00730000111183.
HOGENOMiHOG000233351.
HOVERGENiHBG011703.
InParanoidiP59665.
KOiK05230.
OMAiRVWAFCC.
OrthoDBiEOG091G12GE.
PhylomeDBiP59665.
TreeFamiTF338414.

Enzyme and pathway databases

ReactomeiR-HSA-1461973. Defensins.
R-HSA-1462054. Alpha-defensins.
R-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiDEFA1. human.
EvolutionaryTraceiP59665.
GeneWikiiDEFA1B.
Defensin,_alpha_1.
PMAP-CutDBP59665.
PROiP59665.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000206047.
CleanExiHS_DEFA1.
GenevisibleiP59665. HS.

Family and domain databases

InterProiIPR006081. Alpha-defensin.
IPR016327. Alpha-defensin_pro.
IPR006080. Defensin_beta/alpha.
IPR002366. Defensin_propep.
[Graphical view]
PANTHERiPTHR11876. PTHR11876. 1 hit.
PfamiPF00323. Defensin_1. 1 hit.
PF00879. Defensin_propep. 1 hit.
[Graphical view]
PIRSFiPIRSF001875. Alpha-defensin. 1 hit.
SMARTiSM00048. DEFSN. 1 hit.
[Graphical view]
PROSITEiPS00269. DEFENSIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDEF1_HUMAN
AccessioniPrimary (citable) accession number: P59665
Secondary accession number(s): P11479, Q14125, Q6EZF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 30, 2003
Last modified: November 30, 2016
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.