Beta-defensin 1 precursor - Homo sapiens (Human)

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P60022 (DEFB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 102. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Beta-defensin 1
Short name=BD-1
Short name=hBD-1

Alternative name(s):
Defensin, beta 1

Gene names

Name:	DEFB1
Synonyms:	BD1, HBD1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	68 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	Has bactericidal activity By similarity.
Subcellular location	Secreted.
Tissue specificity	Plasma.
Sequence similarities	Belongs to the beta-defensin family.
Mass spectrometry	Molecular mass is 3928±0.5 Da from positions 33 - 68. Determined by ESI. Ref.5

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
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	G-protein coupled receptor signaling pathway Traceable author statement PubMed 10521347. Source: ProtInc acute inflammatory response Inferred from electronic annotation. Source: Compara chemotaxis Traceable author statement PubMed 10521347. Source: ProtInc defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Inferred from sequence or structural similarity. Source: UniProtKB response to bacterium Inferred from direct assay PubMed 12054642. Source: UniProtKB response to testosterone stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi lumen Traceable author statement. Source: Reactome extracellular region Traceable author statement. Source: Reactome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

Potential

Propeptide

22 – 32

PRO_0000006899

Peptide

33 – 68

Beta-defensin 1 Ref.5

PRO_0000006900

Amino acid modifications

Disulfide bond

37 ↔ 66

Disulfide bond

44 ↔ 59

Disulfide bond

49 ↔ 67

Natural variations

Natural variant

V → I.
Corresponds to variant rs2738047 [ dbSNP | Ensembl ].

VAR_018405

Natural variant

A → V.
Corresponds to variant rs1800967 [ dbSNP | Ensembl ].

VAR_014925

Natural variant

C → S.
Corresponds to variant rs1800968 [ dbSNP | Ensembl ].

VAR_014926

Secondary structure

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P60022 [UniParc].

Last modified November 21, 2003. Version 1.
Checksum: B0AB76DEC3B14F94
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FASTA

7,420

        10         20         30         40         50         60 
MRTSYLLLFT LCLLLSEMAS GGNFLTGLGH RSDHYNCVSS GGQCLYSACP IFTKIQGTCY 


RGKAKCCK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human beta-defensin-1 and alpha-defensins are encoded by adjacent genes: two peptide families with differing disulfide topology share a common ancestry." Liu L., Zhao C., Heng H.H.Q., Ganz T. Genomics 43:316-320(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]	Zhao C. Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[3]	"Human airway epithelia express a beta-defensin." McCray P.B. Jr., Bentley L. Am. J. Respir. Cell Mol. Biol. 16:343-349(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[4]	"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: Colon and Skin.
[5]	"hBD-1: a novel beta-defensin from human plasma." Bensch K.W., Raida M., Maegert H.-J., Schulz-Knappe P., Forssmann W.-G. FEBS Lett. 368:331-335(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-68, PROTEIN SEQUENCE OF 33-68, MASS SPECTROMETRY. Tissue: Kidney, Plasma and Vagina.
[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 33-68.
[7]	"The structure of human beta-defensin-1: new insights into structural properties of beta-defensins." Hoover D.M., Chertov O., Lubkowski J. J. Biol. Chem. 276:39021-39026(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 33-68.
[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 33-68.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U50931, U50930 Genomic DNA. Translation: AAC51728.1.
X92744 mRNA. Translation: CAA63405.1.
U73945 mRNA. Translation: AAB49758.1.
BC033298 mRNA. Translation: AAH33298.1.
BC047677 mRNA. Translation: AAH47677.1.
Z50788 mRNA. Translation: CAA90650.1.

IPI

IPI00022290.

PIR

S66282.

RefSeq

NP_005209.1. NM_005218.3.

UniGene

Hs.32949.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E4S	NMR	-	A	33-68	[»]
1IJU	X-ray	1.40	A/B/C/D	33-68	[»]
1IJV	X-ray	1.20	A/B	33-68	[»]
1KJ5	NMR	-	A	33-68	[»]
2NLB	X-ray	1.85	A/B/C/D	33-68	[»]
2NLC	X-ray	1.65	A/B/C/D	33-68	[»]
2NLD	X-ray	1.49	A/B	33-68	[»]
2NLE	X-ray	1.35	A/B	33-68	[»]
2NLF	X-ray	1.45	A/B	33-68	[»]
2NLG	X-ray	1.65	A/B/C/D	33-68	[»]
2NLH	X-ray	1.85	A/B/C/D	33-68	[»]
2NLP	X-ray	1.85	A/B/C/D	33-68	[»]
2NLQ	X-ray	1.80	A/B/C/D	33-68	[»]
2NLS	X-ray	0.98	A	33-68	[»]
2PLZ	X-ray	1.36	A	33-67	[»]

ProteinModelPortal

P60022.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-5306206.

STRING

9606.ENSP00000297439.

Protein family/group databases

TCDB

1.C.85.1.1. pore-forming beta,-defensin (beta,-Defensin) family.

Polymorphism databases

DMDM

38503374.

Proteomic databases

PaxDb

P60022.

PeptideAtlas

P60022.

PRIDE

P60022.

Protocols and materials databases

DNASU

1672.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000297439; ENSP00000297439; ENSG00000164825.

GeneID

1672.

KEGG

hsa:1672.

UCSC

uc003wqs.2. human.

Organism-specific databases

CTD

1672.

GeneCards

GC08M006715.

HGNC

HGNC:2766. DEFB1.

MIM

602056. gene.

neXtProt

NX_P60022.

PharmGKB

PA27243.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG78795.

HOGENOM

HOG000112188.

HOVERGEN

HBG084156.

InParanoid

P60022.

OMA

GKAKCCK.

OrthoDB

EOG4B8JFR.

PhylomeDB

P60022.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

Bgee

P60022.

CleanEx

HS_DEFB1.

Genevestigator

P60022.

GermOnline

ENSG00000164825. Homo sapiens.

Family and domain databases

InterPro

IPR001855. Defensin_beta-typ.
[Graphical view]

Pfam

PF00711. Defensin_beta. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P60022.

GenomeRNAi

1672.

NextBio

6880.

PMAP-CutDB

P60022.

SOURCE

Search...

Entry information

Entry name

DEFB1_HUMAN

Accession

Primary (citable) accession number: P60022
Secondary accession number(s): Q09753

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 21, 2003
Last sequence update:	November 21, 2003
Last modified:	May 1, 2013
This is version 102 of the entry and version 1 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.

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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Natural variations

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents