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Q01523 (DEF5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. 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:
Defensin-5
Alternative name(s):
Defensin, alpha 5
HD5(20-94)

Cleaved into the following 4 chains:

  1. HD5(23-94)
  2. HD5(29-94)
  3. HD5(56-94)
  4. HD5(63-94)
Gene names
Name:DEFA5
Synonyms:DEF5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length94 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 and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane. All DEFA5 peptides exert antimicrobial activities, but their potency is affected by peptide processing. Ref.5 Ref.6 Ref.7

Subunit structure

Homodimer. Ref.7

Subcellular location

Secreted. Cytoplasmic vesiclesecretory vesicle. Note: Peptides HD5(20-94), HD5(23-94) and HD5(29-94) are found within tissues, HD5(20-94) being the predominant intracellular form. Peptides HD5(56-94) and HD5(63-94) are found in the extracellular milieu, HD5(63-94) being the most abundant form. Ref.5

Tissue specificity

Paneth cells of the small intestine (at protein level). Ref.5

Post-translational modification

Glycosylated. Ref.5

Sequence similarities

Belongs to the alpha-defensin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919
Peptide20 – 9475Defensin-5
PRO_0000006787
Peptide23 – 9472HD5(23-94)
PRO_0000417387
Peptide29 – 9466HD5(29-94)
PRO_0000417388
Peptide56 – 9439HD5(56-94)
PRO_0000417389
Peptide63 – 9432HD5(63-94)
PRO_0000417390

Amino acid modifications

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

Natural variations

Natural variant711R → H.
Corresponds to variant rs7839771 [ dbSNP | Ensembl ].
VAR_059245

Secondary structure

....... 94
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q01523 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 19B5B00B6BAF90DA

FASTA9410,071
        10         20         30         40         50         60 
MRTIAILAAI LLVALQAQAE SLQERADEAT TQKQSGEDNQ DLAISFAGNG LSALRTSGSQ 

        70         80         90 
ARATCYCRTG RCATRESLSG VCEISGRLYR LCCR 

« Hide

References

« Hide 'large scale' references
[1]"Paneth cells of the human small intestine express an antimicrobial peptide gene."
Jones D.E., Bevins C.L.
J. Biol. Chem. 267:23216-23225(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Intestine.
[2]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
[5]"Paneth cell trypsin is the processing enzyme for human defensin-5."
Ghosh D., Porter E., Shen B., Lee S.K., Wilk D., Drazba J., Yadav S.P., Crabb J.W., Ganz T., Bevins C.L.
Nat. Immunol. 3:583-590(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, PEPTIDE CHARACTERIZATION, GLYCOSYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[6]"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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 63-94, FUNCTION, SUBUNIT, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M97925 Genomic DNA. Translation: AAA35754.1.
AF238378 Genomic DNA. Translation: AAT68886.1.
CH471153 Genomic DNA. Translation: EAW80489.1.
BC069690 mRNA. Translation: AAH69690.1.
BC107079 mRNA. Translation: AAI07080.1.
CCDSCCDS5963.1.
PIRA44454.
RefSeqNP_066290.1. NM_021010.1.
UniGeneHs.655233.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZMPX-ray1.65A/B/C/D63-94[»]
2LXZNMR-A63-94[»]
3I5WX-ray1.63A/B63-94[»]
4E82X-ray1.70A/B63-94[»]
4E83X-ray1.90A/B63-94[»]
4E86X-ray2.75A/B/C/D/E/F/G/H/L63-94[»]
ProteinModelPortalQ01523.
SMRQ01523. Positions 63-94.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108034. 1 interaction.
IntActQ01523. 1 interaction.
STRING9606.ENSP00000329890.

Polymorphism databases

DMDM399353.

Proteomic databases

PaxDbQ01523.
PeptideAtlasQ01523.
PRIDEQ01523.

Protocols and materials databases

DNASU1670.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000330590; ENSP00000329890; ENSG00000164816.
GeneID1670.
KEGGhsa:1670.
UCSCuc003wra.1. human.

Organism-specific databases

CTD1670.
GeneCardsGC08M006900.
HGNCHGNC:2764. DEFA5.
HPAHPA015775.
MIM600472. gene.
neXtProtNX_Q01523.
PharmGKBPA27241.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG69207.
HOGENOMHOG000233351.
HOVERGENHBG011703.
InParanoidQ01523.
KOK05230.
OMAQSGEDNQ.
OrthoDBEOG75TMFQ.
PhylomeDBQ01523.
TreeFamTF338414.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

BgeeQ01523.
CleanExHS_DEFA5.
GenevestigatorQ01523.

Family and domain databases

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

ChiTaRSDEFA5. human.
EvolutionaryTraceQ01523.
GeneWikiDEFA5.
GenomeRNAi1670.
NextBio6872.
PMAP-CutDBQ01523.
PROQ01523.
SOURCESearch...

Entry information

Entry nameDEF5_HUMAN
AccessionPrimary (citable) accession number: Q01523
Secondary accession number(s): A0JDY6, Q3KNV2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: July 9, 2014
This is version 118 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

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