P81534 (D103A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-defensin 103

Alternative name(s):
Beta-defensin 3
Short name=BD-3
Short name=DEFB-3
Short name=HBD3
Short name=hBD-3
Defensin, beta 103
Defensin-like protein

Gene names

Name:	DEFB103A
Synonyms:	BD3, DEFB103, DEFB3
AND
Name:	DEFB103B

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	67 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Exhibits antimicrobial activity against Gram-positive bacteria S.aureus and S.pyogenes, Gram-negative bacteria P.aeruginosa and E.coli and the yeast C.albicans. Kills multiresistant S.aureus and vancomycin-resistent E.faecium. No significant hemolytic activity was observed. Ref.1
Subcellular location	Secreted.
Tissue specificity	Highly expressed in skin and tonsils, and to a lesser extent in trachea, uterus, kidney, thymus, adenoid, pharynx and tongue. Low expression in salivary gland, bone marrow, colon, stomach, polyp and larynx. No expression in small intestine. Ref.1
Induction	By bacterial infection and by IFNG/IFN-gamma. Ref.1
Sequence similarities	Belongs to the beta-defensin family.
Mass spectrometry	Molecular mass is 5154.59 Da from positions 23 - 67. Determined by ESI. Ref.1

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Antibiotic Antimicrobial Defensin
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of biosynthetic process of antibacterial peptides active against Gram-positive bacteria Traceable author statement Ref.1. Source: UniProtKB
Cellular component	extracellular region Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Ref.1

Peptide

23 – 67

45

Beta-defensin 103 Ref.1

PRO_0000006971

Amino acid modifications

Disulfide bond

33 ↔ 62

Disulfide bond

40 ↔ 55

Disulfide bond

45 ↔ 63

Experimental info

Sequence conflict

45

1

C → R in AAM62424. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

67

Helix Strand Turn

Details...

Turn

29 – 31

3

Helix

32 – 36

5

Beta strand

39 – 44

6

Beta strand

49 – 53

5

Beta strand

55 – 59

5

Beta strand

61 – 65

5

Sequences

	Sequence		Length	Mass (Da)
	P81534 [UniParc]. Last modified June 1, 2001. Version 2. Checksum: 54266DE1C90D4B65	FASTA	67	7,697
	10 20 30 40 50 60 MRIHYLLFAL LFLFLVPVPG HGGIINTLQK YYCRVRGGRC AVLSCLPKEE QIGKCSTRGR KCCRRKK

References

[1]	"Isolation and characterization of human beta-defensin-3, a novel human inducible peptide antibiotic." Harder J., Bartels J., Christophers E., Schroeder J.-M. J. Biol. Chem. 276:5707-5713(2001) [PubMed: 11085990] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-67, FUNCTION, TISSUE SPECIFICITY, INDUCTION, MASS SPECTROMETRY. Tissue: Keratinocyte, Lung epithelium and Tracheal epithelium.
[2]	"Identification of a novel, multifunctional beta-defensin (human beta-defensin 3) with specific antimicrobial activity. Its interaction with plasma membranes of Xenopus oocytes and the induction of macrophage chemoattraction." Conejo-Garcia J.-R., Jaumann F., Schulz S., Krause A., Rodriguez-Jimenez F.-J., Forssmann U., Adermann K., Kluever E., Vogelmeier C., Becker D., Hedrich R., Forssmann W.-G., Bals R. Cell Tissue Res. 306:257-264(2001) [PubMed: 11702237] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[3]	"Discovery of new human beta-defensins using a genomics-based approach." Jia H.P., Schutte B.C., Schudy A., Linzmeier R., Guthmiller J.M., Johnson G.K., Tack B.F., Mitros J.P., Rosenthal A., Ganz T., McCray P.B. Jr. Gene 263:211-218(2001) [PubMed: 11223260] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	Imai Y. Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"EST and genomic database mining yield novel human and mouse beta-defensins." Adler D.A., Diamond G., Sheppard P., Holloway J., Presnell S., Jaspers S., Whitmore T., Fox B., Gosink J., Rixon M., Gao Z., Haldeman B., O'Hara P. Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"Cloning and expression of Chinese human beta defensin-3." Chen S., He F., Li R. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Tonsil.
[7]	"The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus." Schibli D.J., Hunter H.N., Aseyev V., Starner T.D., Wiencek J.M., McCray P.B. Jr., Tack B.F., Vogel H.J. J. Biol. Chem. 277:8279-8289(2002) [PubMed: 11741980] [Abstract] Cited for: STRUCTURE BY NMR OF 23-67.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ237673 mRNA. Translation: CAC03097.1.
AF295370 mRNA. Translation: AAG02237.1.
AF217245 mRNA. Translation: AAF73853.1.
AB037972 mRNA. Translation: BAB40572.1.
AF301470 mRNA. Translation: AAG22030.1.
AF516673 mRNA. Translation: AAM62424.1.

IPI

IPI00027327.

RefSeq

NP_001075020.1. NM_001081551.2.
NP_061131.1. NM_018661.3.

UniGene

Hs.283082.
Hs.637221.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KJ6	NMR	-	A	23-67	[»]

ProteinModelPortal

P81534.

SMR

P81534. Positions 23-67.

ModBase

Search...

Protein-protein interaction databases

STRING

P81534.

Protein family/group databases

TCDB

1.C.85.1.3. pore-forming beta,-defensin (beta,-Defensin) family.

Proteomic databases

PRIDE

P81534.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000314357; ENSP00000320951; ENSG00000176797.
ENST00000318124; ENSP00000324633; ENSG00000177243.

GeneID

414325.
55894.

KEGG

hsa:414325.
hsa:55894.

UCSC

uc003wrf.1. human.

Organism-specific databases

CTD

414325.
55894.

GeneCards

GC08M007277.
GC08P007739.

HGNC

HGNC:15967. DEFB103A.
HGNC:31702. DEFB103B.

MIM

606611. gene.

neXtProt

NX_P81534.

PharmGKB

PA134933952.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG21678.

HOGENOM

HBG127022.

HOVERGEN

HBG004834.

InParanoid

P81534.

OMA

IRGGRCA.

OrthoDB

EOG4907BQ.

PhylomeDB

P81534.

Gene expression databases

CleanEx

HS_DEFB103A.
HS_DEFB103B.

Genevestigator

P81534.

GermOnline

ENSG00000176797. Homo sapiens.
ENSG00000177243. Homo sapiens.

Family and domain databases

InterPro

IPR001855. Defensin_beta-typ.
[Graphical view]

Pfam

PF00711. Defensin_beta. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

108587.

SOURCE

Search...

Entry information

Entry name

D103A_HUMAN

Accession

Primary (citable) accession number: P81534
Secondary accession number(s): Q8NFG6, Q9NPF6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2001
Last sequence update:	June 1, 2001
Last modified:	January 25, 2012
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.