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Reviewed, UniProtKB/Swiss-Prot P59665 (DEF1_HUMAN)

Last modified June 16, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Neutrophil defensin 1
Alternative name(s):
    HNP-1
      Short name=HP-1
      Short name=HP1
    Defensin, alpha 1
Cleaved into the following 2 chains:
    1- Recommended name:
            HP 1-56
    2- Recommended name:
            Neutrophil defensin 2
        Alternative name(s):
            HNP-2
              Short name=HP-2
              Short name=HP2
Gene names
Name: DEFA1
Synonyms: DEF1, DEFA2, MRS
OrganismHomo sapiens (Human)
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 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. Ref.13 Ref.17

Subunit structure

Dimer. Ref.17

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 Ref.9
Propeptide20 – 3819
PRO_0000006771
Chain39 – 9456HP 1-56
PRO_0000006772
Peptide65 – 9430Neutrophil defensin 1
PRO_0000006773
Peptide66 – 9429Neutrophil defensin 2
PRO_0000006774

Amino acid modifications

Modified residue851Phosphotyrosine Ref.14
Disulfide bond66 ↔ 94 Ref.10
Disulfide bond68 ↔ 83 Ref.10
Disulfide bond73 ↔ 93 Ref.10

Secondary structure

..... 94
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P59665-1 [UniParc].

Last modified April 30, 2003. Version 1.
Checksum: 0E0F8E95737396FA

FASTA9410,201
        10         20         30         40         50         60 
MRTLAILAAI LLVALQAQAE PLQARADEVA AAPEQIAADI PEVVVSLAWD ESLAPKHPGS 

        70         80         90 
RKNMACYCRI 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: 3174637] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"A myeloid-related sequence that localizes to human chromosome 8q21.1-22."
Mars W.M., vanTuinen P., Drabkin H.A., White J.W., Saunders G.F.
Blood 71:1713-1719(1988) [PubMed: 3370315] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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: 2918759] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Inheritance of unequal numbers of the genes encoding the human neutrophil defensins HP-1 and HP-3."
Mars W.M., Patmasiriwat P., Maity T., Huff V., Weil M.M., Saunders G.F.
J. Biol. Chem. 270:30371-30376(1995) [PubMed: 8530462] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"The structure of neutrophil defensin genes."
Linzmeier R., Michaelson D., Liu L., Ganz T.
FEBS Lett. 321:267-273(1993) [PubMed: 8477861] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]Erratum
Linzmeier R., Michaelson D., Liu L., Ganz T.
FEBS Lett. 326:299-300(1993) [PubMed: 8325384] [Abstract]
[7]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]"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: 4056036] [Abstract]
Cited for: PROTEIN SEQUENCE OF 65-94.
[9]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed: 15340161] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-34.
[10]"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: 2917986] [Abstract]
Cited for: DISULFIDE BONDS.
[11]"The isolation and identification of multiple forms of the neutrophil granule peptides from human leukemic cells."
Bateman A., Singh A., Shustik C., Mars W.M., Solomon S.
J. Biol. Chem. 266:7524-7530(1991) [PubMed: 2019582] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[12]"Posttranslational processing of defensins in immature human myeloid cells."
Valore E.V., Ganz T.
Blood 79:1538-1544(1992) [PubMed: 1339298] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[13]"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: 15616305] [Abstract]
Cited for: FUNCTION.
[14]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-85, MASS SPECTROMETRY.
Tissue: Lung.
[15]"NMR studies of defensin antimicrobial peptides. 1. Resonance assignment and secondary structure determination of rabbit NP-2 and human HNP-1."
Zhang X.-L., Selsted M.E., Pardi A.
Biochemistry 31:11348-11356(1992) [PubMed: 1445872] [Abstract]
Cited for: STRUCTURE BY NMR OF DEFENSIN 1.
[16]"NMR studies of defensin antimicrobial peptides. 2. Three-dimensional structures of rabbit NP-2 and human HNP-1."
Pardi A., Zhang X.-L., Selsted M.E., Skalicky J.J., Yip P.F.
Biochemistry 31:11357-11364(1992) [PubMed: 1445873] [Abstract]
Cited for: STRUCTURE BY NMR OF DEFENSIN 1.
[17]"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: 17452329] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 65-94, FUNCTION, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

M21130 mRNA. Translation: AAA52302.1.
M26602 mRNA. Translation: AAA52303.1.
L12690 Genomic DNA. Translation: AAA36382.1.
X52053 mRNA. Translation: CAA36280.1.
BC069423 mRNA. Translation: AAH69423.1.
IPIIPI00005721.
PIRA40499. S32499.
RefSeqNP_001035965.1.
NP_004075.1.
UniGeneHs.380781

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2PM1X-ray1.60A65-94[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP59665. 1 interaction.

Protein family/group databases

TCDB1.C.19.1.1. defensin family.

PTM databases

PhosphoSiteP59665.

Proteomic databases

PeptideAtlasP59665.
PRIDEP59665.

Genome annotation databases

EnsemblENSG00000206047. Homo sapiens. [Contig view]
ENSG00000215377. Homo sapiens. [Contig view]
GeneID1667.
728358.
KEGGhsa:1667.
hsa:728358.

Organism-specific databases

GeneCardsGC08M006822.
GC08M006842.
H-InvDBHIX0034280.
HIX0034351.
HGNCHGNC:2761. DEFA1.
MIM125220. gene.
PharmGKBPA27238.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP59665.
HOVERGENP59665.
OMAP59665. MACYCRI.

Enzyme and pathway databases

Pathway_Interaction_DBanthraxpathway. Cellular roles of Anthrax toxin.

Gene expression databases

BgeeP59665.
CleanExHS_DEFA1.
GermOnlineENSG00000206047. Homo sapiens.

Family and domain databases

InterProIPR016327. Alpha-defensin.
IPR006081. Defensin_alpha.
IPR006080. Defensin_mammal.
IPR002366. Defensin_propep.
[Graphical view]
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 Resources

NextBio6860.
PMAP-CutDBP59665.
SOURCESearch...

Entry information

Entry nameDEF1_HUMAN
AccessionPrimary (citable) accession number: P59665
Secondary accession number(s): P11479, Q14125
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 30, 2003
Last modified: June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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 and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents