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UniProtKB/Swiss-Prot entry P12838


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DEF4_HUMAN
Primary accession number P12838
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1989
Sequence was last modified on July 1, 1993 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 80)
Name and origin of the protein
Protein name Neutrophil defensin 4 [Precursor]
Synonyms HNP-4
HP-4
Defensin, alpha 4
Gene name
Name: DEFA4
Synonyms: DEF4
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Bone marrow;
DOI=10.1210/me.7.2.199; PubMed=8469233 [NCBI, ExPASy, EBI, Israel, Japan]
Palfree R.G.E., Sadro L.C., Solomon S.;
"The gene encoding the human corticostatin HP-4 precursor contains a recent 86-base duplication and is located on chromosome 8.";
Mol. Endocrinol. 7:199-205(1993).
[2]
PROTEIN SEQUENCE OF 64-96.
DOI=10.1016/S0006-291X(88)81118-5; PubMed=2843187 [NCBI, ExPASy, EBI, Israel, Japan]
Singh A., Bateman A., Zhu Q., Shimasaki S., Esch F., Solomon S.;
"Structure of a novel human granulocyte peptide with anti-ACTH activity.";
Biochem. Biophys. Res. Commun. 155:524-529(1988).
[3]
PROTEIN SEQUENCE OF 64-96.
PubMed=2500436 [NCBI, ExPASy, EBI, Israel, Japan]
Wilde C.G., Griffith J.E., Marra M.N., Snable J.L., Scott R.W.;
"Purification and characterization of human neutrophil peptide 4, a novel member of the defensin family.";
J. Biol. Chem. 264:11200-11203(1989).
[4]
PROTEIN SEQUENCE OF 64-83.
DOI=10.1073/pnas.86.14.5610; PubMed=2501794 [NCBI, ExPASy, EBI, Israel, Japan]
Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C., Marra M.N., Seeger M., Nathan C.F.;
"Antibiotic proteins of human polymorphonuclear leukocytes.";
Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989).
[5]
FUNCTION.
DOI=10.1128/AAC.49.1.269-275.2005; PubMed=15616305 [NCBI, ExPASy, EBI, Israel, Japan]
Ericksen B., Wu Z., Lu W., Lehrer R.I.;
"Antibacterial activity and specificity of the six human alpha-defensins.";
Antimicrob. Agents Chemother. 49:269-275(2005).
[6]
FUNCTION.
DOI=10.1016/j.febslet.2004.11.062; PubMed=15620707 [NCBI, ExPASy, EBI, Israel, Japan]
Wu Z., Cocchi F., Gentles D., Ericksen B., Lubkowski J., Devico A., Lehrer R.I., Lu W.;
"Human neutrophil alpha-defensin 4 inhibits HIV-1 infection in vitro.";
FEBS Lett. 579:162-166(2005).
[7]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 64-96, SUBUNIT, AND DISULFIDE BONDS.
DOI=10.1110/ps.062336606; PubMed=17088326 [NCBI, ExPASy, EBI, Israel, Japan]
Szyk A., Wu Z., Tucker K., Yang D., Lu W., Lubkowski J.;
"Crystal structures of human alpha-defensins HNP4, HD5, and HD6.";
Protein Sci. 15:2749-2760(2006).
[8]
VARIANT [LARGE SCALE ANALYSIS] GLN-74.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
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.
  • SUBUNIT: Homodimer.
  • SUBCELLULAR LOCATION: Secreted.
  • SIMILARITY: Belongs to the alpha-defensin family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U18745; AAA64488.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X65977; CAA46792.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00025866; -.
PIR A47365; A47365.
RefSeq NP_001916.1; -.
UniGene Hs.591391
3D structure databases
PDB
1ZMM; X-ray; 1.60 A; A/B/C/D=64-96.[ExPASy / RCSB / EBI]
PDBsum 1ZMM; -.
ModBase P12838.
Organism-specific databases
GeneCards GC08M006780; -.
H-InvDB HIX0034376; -.
HGNC HGNC:2763; DEFA4.
GenAtlas DEFA4.
MIM 601157; gene. [NCBI / EBI]
PharmGKB PA27240; -.
Gene expression databases
ArrayExpress P12838; -.
Bgee P12838; -.
CleanEx HS_DEFA4; -.
GermOnline ENSG00000164821; Homo sapiens.
Ontologies
GO
GO:0005615; Cellular component: extracellular space (inferred from electronic annotation from InterPro).
GO:0042742; Biological process: defense response to bacterium (inferred from electronic annotation from UniProtKB-KW).
GO:0050832; Biological process: defense response to fungus (inferred from electronic annotation from UniProtKB-KW).
GO:0006805; Biological process: xenobiotic metabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR016327; Alpha-defensin.
IPR006081; Defensin_alpha.
IPR006080; Defensin_mammal.
IPR002366; Defensin_propep.
Graphical view of domain structure.
Pfam PF00323; Defensin_1; 1.
PF00879; Defensin_propep; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001875; Alpha-defensin; 1.
SMART SM00048; DEFSN; 1.
SMART graphical view of domain structure.
PROSITE PS00269; DEFENSIN; 1.
Proteomic databases
PRIDE P12838; -.
Genome annotation databases
Ensembl ENSG00000164821; Homo sapiens. [Contig view]
GeneID 1669; -.
KEGG hsa:1669; -.
Phylogenomic databases
HOGENOM P12838; -.
HOVERGEN P12838; -.
OMA P12838; DKSSALQ.
Other
NextBio 6868; -.
SOURCE DEFA4; Homo sapiens.
ProtoNet P12838.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Antibiotic; Antimicrobial; Defensin; Direct protein sequencing; Disulfide bond; Fungicide; Polymorphism; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom  To Length Description FTId
SIGNAL   1   19  19     Potential. 
PROPEP   20   63  44      PRO_0000006781
PEPTIDE   64   96  33     Neutrophil defensin 4. PRO_0000006782
PROPEP   97   97  1      PRO_0000006783
DISULFID   65   93         
DISULFID   67   82         
DISULFID   72   92         
VARIANT   8    8  1     A -> P (in dbSNP:rs28661751 [NCBI]). VAR_048861 
VARIANT   74   74  1     R -> Q (in a colorectal cancer sample; somatic mutation). VAR_036315 [3D]
STRAND   65   70  6      
STRAND   77   84  8      
STRAND   87   93  7      
Sequence information
Length: 97 AA [This is the length of the unprocessed precursor] Molecular weight: 10504 Da [This is the MW of the unprocessed precursor] CRC64: FE14334631EC2FD3 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRIIALLAAI LLVALQVRAG PLQARGDEAP GQEQRGPEDQ DISISFAWDK SSALQVSGST 

        70         80         90 
RGMVCSCRLV FCRRTELRVG NCLIGGVSFT YCCTRVD 

P12838 in FASTA format

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