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Protein

Beta-defensin 4A

Gene

DEFB4A

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

Functioni

Has antibacterial activity.Curated

GO - Biological processi

  • chemotaxis Source: ProtInc
  • defense response to bacterium Source: UniProtKB-KW
  • G-protein coupled receptor signaling pathway Source: ProtInc
  • immune response Source: ProtInc
  • innate immune response Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Defensin

Enzyme and pathway databases

ReactomeiR-HSA-1461957. Beta defensins.
R-HSA-1461973. Defensins.

Protein family/group databases

TCDBi1.C.85.1.2. the pore-forming -defensin (-defensin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-defensin 4A
Alternative name(s):
Beta-defensin 2
Short name:
BD-2
Short name:
hBD-2
Defensin, beta 2
Skin-antimicrobial peptide 1
Short name:
SAP1
Gene namesi
Name:DEFB4A
Synonyms:DEFB102, DEFB2, DEFB4
AND
Name:DEFB4B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:2767. DEFB4A.
HGNC:30193. DEFB4B.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27249.

Polymorphism and mutation databases

BioMutaiDEFB4A.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Peptidei24 – 6441Beta-defensin 4APRO_0000006968Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 60
Disulfide bondi38 ↔ 53
Disulfide bondi43 ↔ 61

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiO15263.
PRIDEiO15263.

Expressioni

Tissue specificityi

Expressed in the skin and respiratory tract.

Inductioni

By inflammation.

Gene expression databases

CleanExiHS_DEFB4.
GenevisibleiO15263. HS.

Interactioni

Protein-protein interaction databases

BioGridi108037. 2 interactions.
STRINGi9606.ENSP00000424598.

Structurei

Secondary structure

1
64
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 273Combined sources
Helixi28 – 336Combined sources
Beta strandi37 – 415Combined sources
Beta strandi48 – 525Combined sources
Beta strandi53 – 553Combined sources
Beta strandi59 – 624Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E4QNMR-A28-64[»]
1FD3X-ray1.35A/B/C/D24-64[»]
1FD4X-ray1.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P24-64[»]
1FQQNMR-A24-64[»]
ProteinModelPortaliO15263.
SMRiO15263. Positions 24-64.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15263.

Family & Domainsi

Sequence similaritiesi

Belongs to the beta-defensin family. LAP/TAP subfamily.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410JJAE. Eukaryota.
ENOG411147G. LUCA.
GeneTreeiENSGT00730000111909.
HOGENOMiHOG000015465.
HOVERGENiHBG004834.
InParanoidiO15263.
OMAiSGAICHP.
OrthoDBiEOG757D1S.
PhylomeDBiO15263.

Family and domain databases

InterProiIPR001855. Defensin_beta-typ.
IPR006080. Defensin_beta/alpha.
[Graphical view]
PfamiPF00711. Defensin_beta. 1 hit.
[Graphical view]
SMARTiSM00048. DEFSN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O15263-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVLYLLFSF LFIFLMPLPG VFGGIGDPVT CLKSGAICHP VFCPRRYKQI
60
GTCGLPGTKC CKKP
Length:64
Mass (Da):7,038
Last modified:January 1, 1998 - v1
Checksum:i05D6454CE7ACD10E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71389 mRNA. Translation: CAA95992.1.
AF040153 Genomic DNA. Translation: AAC33549.1.
AF071216 Genomic DNA. Translation: AAC69554.1.
AJ000152 Genomic DNA. Translation: CAB65126.1.
BC069285 mRNA. Translation: AAH69285.1.
BC093983 mRNA. Translation: AAH93983.1.
BC093985 mRNA. Translation: AAH93985.1.
CCDSiCCDS5971.1.
RefSeqiNP_001192195.1. NM_001205266.1.
NP_004933.1. NM_004942.3.
UniGeneiHs.105924.
Hs.740237.

Genome annotation databases

EnsembliENST00000302247; ENSP00000303532; ENSG00000171711.
ENST00000318157; ENSP00000424598; ENSG00000177257.
ENST00000617136; ENSP00000479138; ENSG00000275444.
GeneIDi100289462.
1673.
KEGGihsa:100289462.
hsa:1673.
UCSCiuc003wsd.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71389 mRNA. Translation: CAA95992.1.
AF040153 Genomic DNA. Translation: AAC33549.1.
AF071216 Genomic DNA. Translation: AAC69554.1.
AJ000152 Genomic DNA. Translation: CAB65126.1.
BC069285 mRNA. Translation: AAH69285.1.
BC093983 mRNA. Translation: AAH93983.1.
BC093985 mRNA. Translation: AAH93985.1.
CCDSiCCDS5971.1.
RefSeqiNP_001192195.1. NM_001205266.1.
NP_004933.1. NM_004942.3.
UniGeneiHs.105924.
Hs.740237.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E4QNMR-A28-64[»]
1FD3X-ray1.35A/B/C/D24-64[»]
1FD4X-ray1.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P24-64[»]
1FQQNMR-A24-64[»]
ProteinModelPortaliO15263.
SMRiO15263. Positions 24-64.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108037. 2 interactions.
STRINGi9606.ENSP00000424598.

Protein family/group databases

TCDBi1.C.85.1.2. the pore-forming -defensin (-defensin) family.

Polymorphism and mutation databases

BioMutaiDEFB4A.

Proteomic databases

PaxDbiO15263.
PRIDEiO15263.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302247; ENSP00000303532; ENSG00000171711.
ENST00000318157; ENSP00000424598; ENSG00000177257.
ENST00000617136; ENSP00000479138; ENSG00000275444.
GeneIDi100289462.
1673.
KEGGihsa:100289462.
hsa:1673.
UCSCiuc003wsd.4. human.

Organism-specific databases

CTDi100289462.
1673.
GeneCardsiDEFB4A.
DEFB4B.
HGNCiHGNC:2767. DEFB4A.
HGNC:30193. DEFB4B.
MIMi602215. gene.
neXtProtiNX_O15263.
PharmGKBiPA27249.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410JJAE. Eukaryota.
ENOG411147G. LUCA.
GeneTreeiENSGT00730000111909.
HOGENOMiHOG000015465.
HOVERGENiHBG004834.
InParanoidiO15263.
OMAiSGAICHP.
OrthoDBiEOG757D1S.
PhylomeDBiO15263.

Enzyme and pathway databases

ReactomeiR-HSA-1461957. Beta defensins.
R-HSA-1461973. Defensins.

Miscellaneous databases

EvolutionaryTraceiO15263.
GeneWikiiBeta-defensin_2.
NextBioi20779203.
PROiO15263.
SOURCEiSearch...

Gene expression databases

CleanExiHS_DEFB4.
GenevisibleiO15263. HS.

Family and domain databases

InterProiIPR001855. Defensin_beta-typ.
IPR006080. Defensin_beta/alpha.
[Graphical view]
PfamiPF00711. Defensin_beta. 1 hit.
[Graphical view]
SMARTiSM00048. DEFSN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skin.
  2. "Structure and mapping of the human beta-defensin HBD-2 gene and its expression at sites of inflammation."
    Liu L., Wang L., Jia H.P., Zhao C., Heng H.H.Q., Schutte B.C., McCray P.B. Jr., Ganz T.
    Gene 222:237-244(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  3. "Transcriptional regulation of beta-defensin gene expression in tracheal epithelial cells."
    Diamond G., Kaiser V., Rhodes J., Russell J.P., Bevins C.L.
    Infect. Immun. 68:113-119(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Mucoid Pseudomonas aeruginosa, TNF-alpha, and IL-1beta, but not IL-6, induce human beta-defensin-2 in respiratory epithelia."
    Harder J., Meyer-Hoffert U., Teran L.M., Schwichtenberg L., Bartels J., Maune S., Schroeder J.-M.
    Am. J. Respir. Cell Mol. Biol. 22:714-721(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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: Brain.
  6. "Chemical synthesis of beta-defensins and LEAP-1/hepcidin."
    Kluever E., Schulz A., Forssmann W.-G., Adermann K.
    J. Pept. Res. 59:241-248(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SYNTHESIS OF 24-64.
  7. "The structure of human beta-defensin-2 shows evidence of higher order oligomerization."
    Hoover D.M., Rajashankar K.R., Blumenthal R., Puri A., Oppenheim J.J., Chertov O., Lubkowski J.
    J. Biol. Chem. 275:32911-32918(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
  8. "Structure determination of human and murine beta-defensins reveals structural conservation in the absence of significant sequence similarity."
    Bauer F., Schweimer K., Kluever E., Conejo-Garcia J.-R., Forssmann W.-G., Roesch P., Adermann K., Sticht H.
    Protein Sci. 10:2470-2479(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 28-64.

Entry informationi

Entry nameiDFB4A_HUMAN
AccessioniPrimary (citable) accession number: O15263
Secondary accession number(s): Q52LC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: May 11, 2016
This is version 153 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, 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.