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P59665

- DEF1_HUMAN

UniProt

P59665 - DEF1_HUMAN

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Protein

Neutrophil defensin 1

Gene
DEFA1, DEF1, DEFA2, MRS
DEFA1B
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Defensin 1 and defensin 2 have antibacterial, fungicide and antiviral activities. Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane.2 Publications

GO - Biological processi

  1. antibacterial humoral response Source: UniProt
  2. chemotaxis Source: ProtInc
  3. defense response to fungus Source: UniProtKB-KW
  4. defense response to Gram-positive bacterium Source: UniProt
  5. defense response to virus Source: UniProtKB-KW
  6. immune response Source: ProtInc
  7. innate immune response Source: UniProt
  8. innate immune response in mucosa Source: UniProt
  9. intracellular estrogen receptor signaling pathway Source: UniProt
  10. killing of cells of other organism Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Defensin, Fungicide

Keywords - Biological processi

Antiviral defense

Enzyme and pathway databases

ReactomeiREACT_115574. Alpha-defensins.
REACT_115846. Defensins.

Protein family/group databases

TCDBi1.C.19.1.1. the defensin (defensin) family.

Names & Taxonomyi

Organism-specific databases

Protein namesi
Recommended name:
Neutrophil defensin 1
Alternative name(s):
Defensin, alpha 1
HNP-1
Short name:
HP-1
Short name:
HP1
Cleaved into the following 2 chains:
Alternative name(s):
HNP-2
Short name:
HP-2
Short name:
HP2
Gene namesi
Name:DEFA1
Synonyms:DEF1, DEFA2, MRS
AND
Name:DEFA1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8
HGNCiHGNC:2761. DEFA1.
HGNC:33596. DEFA1B.

Subcellular locationi

GO - Cellular componenti

  1. azurophil granule lumen Source: Reactome
  2. extracellular region Source: Reactome
  3. extracellular space Source: UniProt
  4. extracellular vesicular exosome Source: UniProt
  5. Golgi lumen Source: Reactome

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165585475.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Propeptidei20 – 3819PRO_0000006771Add
BLAST
Chaini39 – 9456HP 1-56PRO_0000006772Add
BLAST
Peptidei65 – 9430Neutrophil defensin 11 PublicationPRO_0000006773Add
BLAST
Peptidei66 – 9429Neutrophil defensin 2PRO_0000006774Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi66 ↔ 941 Publication
Disulfide bondi68 ↔ 831 Publication
Disulfide bondi73 ↔ 931 Publication
Modified residuei78 – 781ADP-ribosylarginine; by ART1
Modified residuei85 – 851Phosphotyrosine1 Publication
Modified residuei88 – 881ADP-ribosylarginine; by ART1

Post-translational modificationi

ADP-ribosylation drastically reduces cytotoxic and antibacterial activities, and enhances IL8 production.
Phosphorylation at Tyr-85 has been found in some cancer cell lines, and interferes with ADP-ribosylation.

Keywords - PTMi

ADP-ribosylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP59665.
PeptideAtlasiP59665.
PRIDEiP59665.

PTM databases

PhosphoSiteiP59665.

Miscellaneous databases

PMAP-CutDBP59665.

Expressioni

Gene expression databases

BgeeiP59665.
CleanExiHS_DEFA1.
GenevestigatoriP59665.

Organism-specific databases

HPAiCAB032548.
HPA052517.

Interactioni

Subunit structurei

Dimer.1 Publication

Protein-protein interaction databases

BioGridi108031. 3 interactions.
IntActiP59665. 5 interactions.
MINTiMINT-6631351.
STRINGi9606.ENSP00000372126.

Structurei

Secondary structure

1
94
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi66 – 727
Beta strandi79 – 857
Beta strandi88 – 936

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KHTNMR-A65-94[»]
2PM1X-ray1.60A65-94[»]
3GNYX-ray1.56A/B65-94[»]
3H6CX-ray1.63A/B65-94[»]
3HJ2X-ray1.40A/B65-94[»]
3HJDX-ray1.65A/B65-94[»]
3LO1X-ray1.60A65-94[»]
3LO2X-ray1.56A/B65-94[»]
3LO4X-ray1.75A/B65-94[»]
3LO6X-ray1.56A/B65-94[»]
3LO9X-ray1.56A/B65-94[»]
3LOEX-ray1.56A65-94[»]
3LVXX-ray1.63A/B65-94[»]
4DU0X-ray1.90A/B/C/D65-94[»]
4LB1X-ray2.00A/B/D/E65-94[»]
4LB7X-ray1.90A/B/D/E65-94[»]
4LBBX-ray1.72A/B65-94[»]
4LBFX-ray1.70A/B/C/D/E/F/G/H65-94[»]
ProteinModelPortaliP59665.
SMRiP59665. Positions 65-94.

Miscellaneous databases

EvolutionaryTraceiP59665.

Family & Domainsi

Sequence similaritiesi

Belongs to the alpha-defensin family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG86943.
HOGENOMiHOG000233351.
HOVERGENiHBG011703.
InParanoidiP59665.
KOiK05230.
OMAiRVWAFCC.
OrthoDBiEOG75TMFQ.
PhylomeDBiP59665.
TreeFamiTF338414.

Family and domain databases

InterProiIPR016327. Alpha-defensin.
IPR006080. Defensin_beta/neutrophil.
IPR002366. Defensin_propep.
IPR006081. Mammalian_defensins.
[Graphical view]
PANTHERiPTHR11876. PTHR11876. 1 hit.
PfamiPF00323. Defensin_1. 1 hit.
PF00879. Defensin_propep. 1 hit.
[Graphical view]
PIRSFiPIRSF001875. Alpha-defensin. 1 hit.
SMARTiSM00048. DEFSN. 1 hit.
[Graphical view]
PROSITEiPS00269. DEFENSIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P59665-1 [UniParc]FASTAAdd to Basket

« Hide

MRTLAILAAI LLVALQAQAE PLQARADEVA AAPEQIAADI PEVVVSLAWD   50
ESLAPKHPGS RKNMACYCRI PACIAGERRY GTCIYQGRLW AFCC 94
Length:94
Mass (Da):10,201
Last modified:April 30, 2003 - v1
Checksum:i0E0F8E95737396FA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M21130 mRNA. Translation: AAA52302.1.
M26602 mRNA. Translation: AAA52303.1.
L12690 Genomic DNA. Translation: AAA36382.1.
X52053 mRNA. Translation: CAA36280.1.
AF200455 Genomic DNA. Translation: AAT68875.1.
AF200455 Genomic DNA. Translation: AAT68878.1.
AF200455 Genomic DNA. Translation: AAT68879.1.
AF200455 Genomic DNA. Translation: AAT68880.1.
AF238378 Genomic DNA. Translation: AAT68883.1.
AF238378 Genomic DNA. Translation: AAT68884.1.
BC069423 mRNA. Translation: AAH69423.1.
BC093791 mRNA. Translation: AAH93791.1.
BC112188 mRNA. Translation: AAI12189.1.
CCDSiCCDS34797.1.
CCDS43691.1.
PIRiS32499. A40499.
RefSeqiNP_001035965.1. NM_001042500.1.
NP_004075.1. NM_004084.3.
UniGeneiHs.380781.

Genome annotation databases

EnsembliENST00000382679; ENSP00000372126; ENSG00000206047.
ENST00000382689; ENSP00000372136; ENSG00000240247.
ENST00000382692; ENSP00000372139; ENSG00000206047.
ENST00000535841; ENSP00000443526; ENSG00000240247.
GeneIDi1667.
728358.
KEGGihsa:1667.
hsa:728358.
UCSCiuc003wqv.1. human.

Polymorphism databases

DMDMi30316322.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M21130 mRNA. Translation: AAA52302.1 .
M26602 mRNA. Translation: AAA52303.1 .
L12690 Genomic DNA. Translation: AAA36382.1 .
X52053 mRNA. Translation: CAA36280.1 .
AF200455 Genomic DNA. Translation: AAT68875.1 .
AF200455 Genomic DNA. Translation: AAT68878.1 .
AF200455 Genomic DNA. Translation: AAT68879.1 .
AF200455 Genomic DNA. Translation: AAT68880.1 .
AF238378 Genomic DNA. Translation: AAT68883.1 .
AF238378 Genomic DNA. Translation: AAT68884.1 .
BC069423 mRNA. Translation: AAH69423.1 .
BC093791 mRNA. Translation: AAH93791.1 .
BC112188 mRNA. Translation: AAI12189.1 .
CCDSi CCDS34797.1.
CCDS43691.1.
PIRi S32499. A40499.
RefSeqi NP_001035965.1. NM_001042500.1.
NP_004075.1. NM_004084.3.
UniGenei Hs.380781.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KHT NMR - A 65-94 [» ]
2PM1 X-ray 1.60 A 65-94 [» ]
3GNY X-ray 1.56 A/B 65-94 [» ]
3H6C X-ray 1.63 A/B 65-94 [» ]
3HJ2 X-ray 1.40 A/B 65-94 [» ]
3HJD X-ray 1.65 A/B 65-94 [» ]
3LO1 X-ray 1.60 A 65-94 [» ]
3LO2 X-ray 1.56 A/B 65-94 [» ]
3LO4 X-ray 1.75 A/B 65-94 [» ]
3LO6 X-ray 1.56 A/B 65-94 [» ]
3LO9 X-ray 1.56 A/B 65-94 [» ]
3LOE X-ray 1.56 A 65-94 [» ]
3LVX X-ray 1.63 A/B 65-94 [» ]
4DU0 X-ray 1.90 A/B/C/D 65-94 [» ]
4LB1 X-ray 2.00 A/B/D/E 65-94 [» ]
4LB7 X-ray 1.90 A/B/D/E 65-94 [» ]
4LBB X-ray 1.72 A/B 65-94 [» ]
4LBF X-ray 1.70 A/B/C/D/E/F/G/H 65-94 [» ]
ProteinModelPortali P59665.
SMRi P59665. Positions 65-94.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108031. 3 interactions.
IntActi P59665. 5 interactions.
MINTi MINT-6631351.
STRINGi 9606.ENSP00000372126.

Protein family/group databases

TCDBi 1.C.19.1.1. the defensin (defensin) family.

PTM databases

PhosphoSitei P59665.

Polymorphism databases

DMDMi 30316322.

Proteomic databases

PaxDbi P59665.
PeptideAtlasi P59665.
PRIDEi P59665.

Protocols and materials databases

DNASUi 1667.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000382679 ; ENSP00000372126 ; ENSG00000206047 .
ENST00000382689 ; ENSP00000372136 ; ENSG00000240247 .
ENST00000382692 ; ENSP00000372139 ; ENSG00000206047 .
ENST00000535841 ; ENSP00000443526 ; ENSG00000240247 .
GeneIDi 1667.
728358.
KEGGi hsa:1667.
hsa:728358.
UCSCi uc003wqv.1. human.

Organism-specific databases

CTDi 1667.
728358.
GeneCardsi GC08M006822.
GC08M006843.
HGNCi HGNC:2761. DEFA1.
HGNC:33596. DEFA1B.
HPAi CAB032548.
HPA052517.
MIMi 125220. gene.
neXtProti NX_P59665.
PharmGKBi PA165585475.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG86943.
HOGENOMi HOG000233351.
HOVERGENi HBG011703.
InParanoidi P59665.
KOi K05230.
OMAi RVWAFCC.
OrthoDBi EOG75TMFQ.
PhylomeDBi P59665.
TreeFami TF338414.

Enzyme and pathway databases

Reactomei REACT_115574. Alpha-defensins.
REACT_115846. Defensins.

Miscellaneous databases

ChiTaRSi DEFA1. human.
EvolutionaryTracei P59665.
GeneWikii DEFA1B.
Defensin,_alpha_1.
NextBioi 6860.
PMAP-CutDB P59665.
PROi P59665.
SOURCEi Search...

Gene expression databases

Bgeei P59665.
CleanExi HS_DEFA1.
Genevestigatori P59665.

Family and domain databases

InterProi IPR016327. Alpha-defensin.
IPR006080. Defensin_beta/neutrophil.
IPR002366. Defensin_propep.
IPR006081. Mammalian_defensins.
[Graphical view ]
PANTHERi PTHR11876. PTHR11876. 1 hit.
Pfami PF00323. Defensin_1. 1 hit.
PF00879. Defensin_propep. 1 hit.
[Graphical view ]
PIRSFi PIRSF001875. Alpha-defensin. 1 hit.
SMARTi SM00048. DEFSN. 1 hit.
[Graphical view ]
PROSITEi PS00269. DEFENSIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Isolation and characterization of human defensin cDNA clones."
    Daher K.A., Lehrer R.I., Ganz T., Kronenberg M.
    Proc. Natl. Acad. Sci. U.S.A. 85:7327-7331(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "A myeloid-related sequence that localizes to human chromosome 8q21.1-22."
    Mars W.M., vanTuinen P., Drabkin H.A., White J.W., Saunders G.F.
    Blood 71:1713-1719(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Differentiation stage-specific expression of a gene during granulopoiesis."
    Wiedemann L.M., Francis G.E., Lamb R.F., Burns J.H., Winnie J.N., McKenzie E.D., Birnie G.D.
    Leukemia 3:227-234(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Inheritance of unequal numbers of the genes encoding the human neutrophil defensins HP-1 and HP-3."
    Mars W.M., Patmasiriwat P., Maity T., Huff V., Weil M.M., Saunders G.F.
    J. Biol. Chem. 270:30371-30376(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "The structure of neutrophil defensin genes."
    Linzmeier R., Michaelson D., Liu L., Ganz T.
    FEBS Lett. 321:267-273(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "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.
    , 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].
  7. "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: Liver.
  8. Cited for: PROTEIN SEQUENCE OF 65-94.
  9. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-34.
  10. "Determination of the disulfide array in the human defensin HNP-2. A covalently cyclized peptide."
    Selsted M.E., Harwig S.S.L.
    J. Biol. Chem. 264:4003-4007(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  11. "The isolation and identification of multiple forms of the neutrophil granule peptides from human leukemic cells."
    Bateman A., Singh A., Shustik C., Mars W.M., Solomon S.
    J. Biol. Chem. 266:7524-7530(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.
  12. "Posttranslational processing of defensins in immature human myeloid cells."
    Valore E.V., Ganz T.
    Blood 79:1538-1544(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.
  13. "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.
  14. "Structural and functional consequences induced by post-translational modifications in alpha-Defensins."
    Balducci E., Bonucci A., Picchianti M., Pogni R., Talluri E.
    Int. J. Pept. 2011:594723-594723(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ADP-RIBOSYLATION AT ARG-78 AND ARG-88 BY ART1, PHOSPHORYLATION AT TYR-85.
  15. "NMR studies of defensin antimicrobial peptides. 1. Resonance assignment and secondary structure determination of rabbit NP-2 and human HNP-1."
    Zhang X.-L., Selsted M.E., Pardi A.
    Biochemistry 31:11348-11356(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF DEFENSIN 1.
  16. "NMR studies of defensin antimicrobial peptides. 2. Three-dimensional structures of rabbit NP-2 and human HNP-1."
    Pardi A., Zhang X.-L., Selsted M.E., Skalicky J.J., Yip P.F.
    Biochemistry 31:11357-11364(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF DEFENSIN 1.
  17. "Toward understanding the cationicity of defensins. Arg and Lys versus their noncoded analogs."
    Zou G., de Leeuw E., Li C., Pazgier M., Li C., Zeng P., Lu W.-Y., Lubkowski J., Lu W.
    J. Biol. Chem. 282:19653-19665(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 65-94, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiDEF1_HUMAN
AccessioniPrimary (citable) accession number: P59665
Secondary accession number(s): P11479, Q14125, Q6EZF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 30, 2003
Last modified: September 3, 2014
This is version 123 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, Direct protein sequencing, 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

External Data

Dasty 3

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