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Protein

Azurocidin

Gene

AZU1

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

Functioni

This is a neutrophil granule-derived antibacterial and monocyte- and fibroblast-specific chemotactic glycoprotein. Binds heparin. The cytotoxic action is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. It may play a role in mediating recruitment of monocytes in the second wave of inflammation. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa. Acting alone, it does not have antimicrobial activity against the Gram-negative bacteria A.actinomycetemcomitans ATCC 29532, A.actinomycetemcomitans NCTC 9709, A.actinomycetemcomitans FDC-Y4, H.aphrophilus ATCC 13252, E.corrodens ATCC 23834, C.sputigena ATCC 33123, Capnocytophaga sp ATCC 33124, Capnocytophaga sp ATCC 27872 or E.coli ML-35. Has antibacterial activity against C.sputigena ATCC 33123 when acting synergistically with either elastase or cathepsin G.3 Publications

GO - Molecular functioni

  • heparan sulfate proteoglycan binding Source: UniProtKB
  • heparin binding Source: UniProtKB
  • peptidase activity Source: UniProtKB
  • serine-type endopeptidase activity Source: GO_Central
  • toxic substance binding Source: UniProtKB

GO - Biological processi

  • antimicrobial humoral response Source: UniProtKB
  • calcium-mediated signaling using intracellular calcium source Source: UniProtKB
  • cell chemotaxis Source: UniProtKB
  • cellular extravasation Source: UniProtKB
  • defense response to Gram-negative bacterium Source: UniProtKB
  • defense response to virus Source: UniProtKB
  • glial cell migration Source: UniProtKB
  • induction of positive chemotaxis Source: UniProtKB
  • inflammatory response Source: UniProtKB
  • macrophage chemotaxis Source: UniProtKB
  • microglial cell activation Source: UniProtKB
  • monocyte activation Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • neutrophil mediated killing of bacterium Source: UniProtKB
  • positive regulation of cell adhesion Source: UniProtKB
  • positive regulation of fractalkine biosynthetic process Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of interleukin-1 beta biosynthetic process Source: UniProtKB
  • positive regulation of MHC class II biosynthetic process Source: UniProtKB
  • positive regulation of peptidyl-threonine phosphorylation Source: UniProtKB
  • positive regulation of phagocytosis Source: UniProtKB
  • positive regulation of protein kinase activity Source: UniProtKB
  • positive regulation of tumor necrosis factor biosynthetic process Source: UniProtKB
  • protein kinase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
  • protein kinase C signaling Source: UniProtKB
  • protein processing Source: GO_Central
  • proteolysis Source: UniProtKB
  • regulation of vascular permeability Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Serine protease homolog

Keywords - Biological processi

Chemotaxis

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000172232-MONOMER.
ReactomeiR-HSA-6798695. Neutrophil degranulation.

Protein family/group databases

MEROPSiS01.971.

Names & Taxonomyi

Protein namesi
Recommended name:
Azurocidin1 Publication
Alternative name(s):
Cationic antimicrobial protein CAP371 Publication
Heparin-binding protein1 Publication
Short name:
HBP1 Publication
Short name:
hHBP1 Publication
Gene namesi
Name:AZU1Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:913. AZU1.

Subcellular locationi

GO - Cellular componenti

  • azurophil granule Source: UniProtKB
  • azurophil granule membrane Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
  • extrinsic component of membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi52C → S: Loss of antibiotic activity. 1 Publication1
Mutagenesisi68C → S: Loss of antibiotic activity. 1 Publication1

Organism-specific databases

DisGeNETi566.
OpenTargetsiENSG00000172232.
ENSG00000278624.
PharmGKBiPA25206.

Polymorphism and mutation databases

BioMutaiAZU1.
DMDMi416746.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
PropeptideiPRO_000043537220 – 26Removed in mature form10 Publications7
PropeptideiPRO_000043537325 – 26Dipeptide found in non-mature form1 Publication2
ChainiPRO_000002770527 – 248Azurocidin2 PublicationsAdd BLAST222
PropeptideiPRO_0000027706249 – 251Removed in mature form2 Publications3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi52 ↔ 682 Publications
Glycosylationi126N-linked (GlcNAc...); partial2 Publications1
Glycosylationi140N-linked (GlcNAc...)2 Publications1
Disulfide bondi149 ↔ 2072 Publications
Glycosylationi171N-linked (GlcNAc...); partial2 Publications1
Disulfide bondi180 ↔ 1862 Publications
Disulfide bondi197 ↔ 2222 Publications

Post-translational modificationi

Cleavage of the N-terminal propeptide which is composed of 7 amino acids occurs in two steps. The initial cleavage of 5 amino acids is followed by the cleavage of a dipeptide to produce the mature form.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

EPDiP20160.
PaxDbiP20160.
PeptideAtlasiP20160.
PRIDEiP20160.

Expressioni

Gene expression databases

BgeeiENSG00000172232.
CleanExiHS_AZU1.
ExpressionAtlasiP20160. baseline and differential.
GenevisibleiP20160. HS.

Organism-specific databases

HPAiHPA055851.

Interactioni

Protein-protein interaction databases

BioGridi107043. 14 interactors.
IntActiP20160. 2 interactors.
MINTiMINT-4054423.
STRINGi9606.ENSP00000233997.

Structurei

Secondary structure

1251
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi41 – 46Combined sources6
Beta strandi49 – 58Combined sources10
Beta strandi61 – 64Combined sources4
Helixi66 – 68Combined sources3
Beta strandi76 – 82Combined sources7
Turni91 – 93Combined sources3
Beta strandi95 – 103Combined sources9
Turni109 – 112Combined sources4
Beta strandi117 – 123Combined sources7
Beta strandi148 – 154Combined sources7
Beta strandi157 – 160Combined sources4
Beta strandi168 – 174Combined sources7
Helixi177 – 179Combined sources3
Beta strandi184 – 188Combined sources5
Beta strandi190 – 193Combined sources4
Beta strandi204 – 207Combined sources4
Beta strandi210 – 218Combined sources9
Beta strandi227 – 231Combined sources5
Helixi232 – 235Combined sources4
Helixi236 – 244Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A7SX-ray1.12A27-251[»]
1AE5X-ray2.30A27-251[»]
1FY1X-ray2.50A27-251[»]
1FY3X-ray1.89A27-251[»]
ProteinModelPortaliP20160.
SMRiP20160.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20160.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 244Peptidase S1PROSITE-ProRule annotationAdd BLAST218

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni46 – 70Possesses antibiotic activity1 PublicationAdd BLAST25

Sequence similaritiesi

Belongs to the peptidase S1 family. Elastase subfamily.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118895.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP20160.
OMAiKARPRQF.
OrthoDBiEOG091G0DF7.
PhylomeDBiP20160.
TreeFamiTF335284.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P20160-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRLTVLALL AGLLASSRAG SSPLLDIVGG RKARPRQFPF LASIQNQGRH
60 70 80 90 100
FCGGALIHAR FVMTAASCFQ SQNPGVSTVV LGAYDLRRRE RQSRQTFSIS
110 120 130 140 150
SMSENGYDPQ QNLNDLMLLQ LDREANLTSS VTILPLPLQN ATVEAGTRCQ
160 170 180 190 200
VAGWGSQRSG GRLSRFPRFV NVTVTPEDQC RPNNVCTGVL TRRGGICNGD
210 220 230 240 250
GGTPLVCEGL AHGVASFSLG PCGRGPDFFT RVALFRDWID GVLNNPGPGP

A
Length:251
Mass (Da):26,886
Last modified:October 1, 1993 - v3
Checksum:i22F80D9EBE87DE60
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti36R → H AA sequence (PubMed:2404977).Curated1
Sequence conflicti130S → N AA sequence (PubMed:2026172).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96326 Genomic DNA. Translation: AAB59353.1.
AC004799 Genomic DNA. No translation available.
BC069495 mRNA. Translation: AAH69495.1.
BC093931 mRNA. Translation: AAH93931.1.
BC093933 mRNA. Translation: AAH93933.1.
X58794 mRNA. Translation: CAA41601.1.
CCDSiCCDS12044.1.
PIRiA46268. TRHUAZ.
RefSeqiNP_001691.1. NM_001700.4.
UniGeneiHs.72885.

Genome annotation databases

EnsembliENST00000233997; ENSP00000233997; ENSG00000172232.
ENST00000620695; ENSP00000479183; ENSG00000278624.
GeneIDi566.
KEGGihsa:566.
UCSCiuc002lpz.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96326 Genomic DNA. Translation: AAB59353.1.
AC004799 Genomic DNA. No translation available.
BC069495 mRNA. Translation: AAH69495.1.
BC093931 mRNA. Translation: AAH93931.1.
BC093933 mRNA. Translation: AAH93933.1.
X58794 mRNA. Translation: CAA41601.1.
CCDSiCCDS12044.1.
PIRiA46268. TRHUAZ.
RefSeqiNP_001691.1. NM_001700.4.
UniGeneiHs.72885.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A7SX-ray1.12A27-251[»]
1AE5X-ray2.30A27-251[»]
1FY1X-ray2.50A27-251[»]
1FY3X-ray1.89A27-251[»]
ProteinModelPortaliP20160.
SMRiP20160.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107043. 14 interactors.
IntActiP20160. 2 interactors.
MINTiMINT-4054423.
STRINGi9606.ENSP00000233997.

Protein family/group databases

MEROPSiS01.971.

Polymorphism and mutation databases

BioMutaiAZU1.
DMDMi416746.

Proteomic databases

EPDiP20160.
PaxDbiP20160.
PeptideAtlasiP20160.
PRIDEiP20160.

Protocols and materials databases

DNASUi566.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000233997; ENSP00000233997; ENSG00000172232.
ENST00000620695; ENSP00000479183; ENSG00000278624.
GeneIDi566.
KEGGihsa:566.
UCSCiuc002lpz.2. human.

Organism-specific databases

CTDi566.
DisGeNETi566.
GeneCardsiAZU1.
HGNCiHGNC:913. AZU1.
HPAiHPA055851.
MIMi162815. gene.
neXtProtiNX_P20160.
OpenTargetsiENSG00000172232.
ENSG00000278624.
PharmGKBiPA25206.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118895.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP20160.
OMAiKARPRQF.
OrthoDBiEOG091G0DF7.
PhylomeDBiP20160.
TreeFamiTF335284.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000172232-MONOMER.
ReactomeiR-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

EvolutionaryTraceiP20160.
GeneWikiiAzurocidin_1.
GenomeRNAii566.
PROiP20160.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000172232.
CleanExiHS_AZU1.
ExpressionAtlasiP20160. baseline and differential.
GenevisibleiP20160. HS.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCAP7_HUMAN
AccessioniPrimary (citable) accession number: P20160
Secondary accession number(s): P80014
, Q52LG4, Q9UCM1, Q9UCT5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 1, 1993
Last modified: November 30, 2016
This is version 172 of the entry and version 3 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 19
    Human chromosome 19: 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. Peptidase families
    Classification of peptidase families and list of entries
  5. 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.