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P12838 (DEF4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 4
Alternative name(s):
Defensin, alpha 4
HNP-4
Short name=HP-4
Gene names
Name:DEFA4
Synonyms:DEF4
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length97 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has antimicrobial activity against Gram-negative bacteria, and to a lesser extent also against Gram-positive bacteria and fungi. Protects blood cells against infection with HIV-1 (in vitro). Inhibits corticotropin (ACTH)-stimulated corticosterone production. Ref.5 Ref.6

Subunit structure

Homodimer. Ref.7

Subcellular location

Secreted.

Sequence similarities

Belongs to the alpha-defensin family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Propeptide20 – 6344
PRO_0000006781
Peptide64 – 9633Neutrophil defensin 4 Ref.2 Ref.3
PRO_0000006782
Propeptide971
PRO_0000006783

Amino acid modifications

Disulfide bond65 ↔ 93 Ref.7
Disulfide bond67 ↔ 82 Ref.7
Disulfide bond72 ↔ 92 Ref.7

Natural variations

Natural variant81A → P.
Corresponds to variant rs28661751 [ dbSNP | Ensembl ].
VAR_048861
Natural variant81A → V.
Corresponds to variant rs28488529 [ dbSNP | Ensembl ].
VAR_061132
Natural variant741R → Q in a colorectal cancer sample; somatic mutation. Ref.8
VAR_036315

Secondary structure

....... 97
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12838 [UniParc].

Last modified July 1, 1993. Version 2.
Checksum: FE14334631EC2FD3

FASTA9710,504
        10         20         30         40         50         60 
MRIIALLAAI LLVALQVRAG PLQARGDEAP GQEQRGPEDQ DISISFAWDK SSALQVSGST 

        70         80         90 
RGMVCSCRLV FCRRTELRVG NCLIGGVSFT YCCTRVD 

« Hide

References

« Hide 'large scale' references
[1]"The gene encoding the human corticostatin HP-4 precursor contains a recent 86-base duplication and is located on chromosome 8."
Palfree R.G.E., Sadro L.C., Solomon S.
Mol. Endocrinol. 7:199-205(1993) [PubMed: 8469233] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Bone marrow.
[2]"Structure of a novel human granulocyte peptide with anti-ACTH activity."
Singh A., Bateman A., Zhu Q., Shimasaki S., Esch F., Solomon S.
Biochem. Biophys. Res. Commun. 155:524-529(1988) [PubMed: 2843187] [Abstract]
Cited for: PROTEIN SEQUENCE OF 64-96.
[3]"Purification and characterization of human neutrophil peptide 4, a novel member of the defensin family."
Wilde C.G., Griffith J.E., Marra M.N., Snable J.L., Scott R.W.
J. Biol. Chem. 264:11200-11203(1989) [PubMed: 2500436] [Abstract]
Cited for: PROTEIN SEQUENCE OF 64-96.
[4]"Antibiotic proteins of human polymorphonuclear leukocytes."
Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C., Marra M.N., Seeger M., Nathan C.F.
Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989) [PubMed: 2501794] [Abstract]
Cited for: PROTEIN SEQUENCE OF 64-83.
[5]"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.
[6]"Human neutrophil alpha-defensin 4 inhibits HIV-1 infection in vitro."
Wu Z., Cocchi F., Gentles D., Ericksen B., Lubkowski J., Devico A., Lehrer R.I., Lu W.
FEBS Lett. 579:162-166(2005) [PubMed: 15620707] [Abstract]
Cited for: FUNCTION.
[7]"Crystal structures of human alpha-defensins HNP4, HD5, and HD6."
Szyk A., Wu Z., Tucker K., Yang D., Lu W., Lubkowski J.
Protein Sci. 15:2749-2760(2006) [PubMed: 17088326] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 64-96, SUBUNIT, DISULFIDE BONDS.
[8]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-74.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U18745 Genomic DNA. Translation: AAA64488.1.
X65977 mRNA. Translation: CAA46792.1.
IPIIPI00025866.
PIRA47365.
RefSeqNP_001916.1. NM_001925.1.
UniGeneHs.591391.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZMMX-ray1.60A/B/C/D64-96[»]
ProteinModelPortalP12838.
SMRP12838. Positions 64-96.
ModBaseSearch...

Protein-protein interaction databases

STRINGP12838.

Polymorphism databases

DMDM399352.

Proteomic databases

PRIDEP12838.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000297435; ENSP00000297435; ENSG00000164821.
GeneID1669.
KEGGhsa:1669.
UCSCuc003wqu.1. human.

Organism-specific databases

CTD1669.
GeneCardsGC08M006780.
H-InvDBHIX0034376.
HGNCHGNC:2763. DEFA4.
MIM601157. gene.
neXtProtNX_P12838.
PharmGKBPA27240.
GenAtlasSearch...

Phylogenomic databases

eggNOGmaNOG24475.
HOGENOMHBG283450.
HOVERGENHBG011703.
InParanoidP12838.
OMAAWDKSSA.
OrthoDBEOG4GF3GT.
PhylomeDBP12838.

Gene expression databases

ArrayExpressP12838.
BgeeP12838.
CleanExHS_DEFA4.
GenevestigatorP12838.
GermOnlineENSG00000164821. Homo sapiens.

Family and domain databases

InterProIPR016327. Alpha-defensin.
IPR006080. Defensin_beta/neutrophil.
IPR002366. Defensin_propep.
IPR006081. Mammalian_defensins.
[Graphical view]
KOK05230.
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

NextBio6868.
SOURCESearch...

Entry information

Entry nameDEF4_HUMAN
AccessionPrimary (citable) accession number: P12838
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 1, 1993
Last modified: January 25, 2012
This is version 101 of the entry and version 2 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

Human chromosome 8

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

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