Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P20160

- CAP7_HUMAN

UniProt

P20160 - CAP7_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Azurocidin

Gene

AZU1

Organism
Homo sapiens (Human)
Status
Reviewed - 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.2 Publications

GO - Molecular functioni

  1. heparin binding Source: UniProtKB
  2. serine-type endopeptidase activity Source: InterPro
  3. toxic substance binding Source: UniProtKB

GO - Biological processi

  1. cellular extravasation Source: UniProtKB
  2. defense response to Gram-negative bacterium Source: UniProtKB
  3. glial cell migration Source: UniProtKB
  4. induction of positive chemotaxis Source: UniProtKB
  5. inflammatory response Source: UniProtKB
  6. macrophage chemotaxis Source: UniProtKB
  7. microglial cell activation Source: UniProtKB
  8. monocyte activation Source: UniProtKB
  9. negative regulation of apoptotic process Source: UniProtKB
  10. positive regulation of cell adhesion Source: UniProtKB
  11. positive regulation of fractalkine biosynthetic process Source: UniProtKB
  12. positive regulation of interleukin-1 beta biosynthetic process Source: UniProtKB
  13. positive regulation of MHC class II biosynthetic process Source: UniProtKB
  14. positive regulation of phagocytosis Source: UniProtKB
  15. positive regulation of tumor necrosis factor biosynthetic process Source: UniProtKB
  16. protein kinase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
  17. 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

Protein family/group databases

MEROPSiS01.971.

Names & Taxonomyi

Protein namesi
Recommended name:
Azurocidin
Alternative name(s):
Cationic antimicrobial protein CAP37
Heparin-binding protein
Short name:
HBP
Gene namesi
Name:AZU1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:913. AZU1.

Subcellular locationi

Cytoplasmic granule
Note: Cytoplasmic granules of neutrophils.

GO - Cellular componenti

  1. azurophil granule Source: UniProtKB
  2. extracellular region Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi52 – 521C → S: Loss of antibiotic activity.
Mutagenesisi68 – 681C → S: Loss of antibiotic activity.

Organism-specific databases

PharmGKBiPA25206.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26269 PublicationsAdd
BLAST
Chaini27 – 248222AzurocidinPRO_0000027705Add
BLAST
Propeptidei249 – 2513PRO_0000027706

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi52 ↔ 681 PublicationPROSITE-ProRule annotation
Glycosylationi126 – 1261N-linked (GlcNAc...); partial2 Publications
Glycosylationi140 – 1401N-linked (GlcNAc...)2 Publications
Disulfide bondi149 ↔ 207
Glycosylationi171 – 1711N-linked (GlcNAc...); partial2 Publications
Disulfide bondi180 ↔ 186
Disulfide bondi197 ↔ 222

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP20160.
PRIDEiP20160.

Expressioni

Gene expression databases

BgeeiP20160.
CleanExiHS_AZU1.
GenevestigatoriP20160.

Organism-specific databases

HPAiHPA055851.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi107043. 13 interactions.
IntActiP20160. 2 interactions.
MINTiMINT-4054423.
STRINGi9606.ENSP00000233997.

Structurei

Secondary structure

1
251
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi41 – 466
Beta strandi49 – 5810
Beta strandi61 – 644
Helixi66 – 683
Beta strandi76 – 827
Turni91 – 933
Beta strandi95 – 1039
Turni109 – 1124
Beta strandi117 – 1237
Beta strandi148 – 1547
Beta strandi157 – 1604
Beta strandi168 – 1747
Helixi177 – 1793
Beta strandi184 – 1885
Beta strandi190 – 1934
Beta strandi204 – 2074
Beta strandi210 – 2189
Beta strandi227 – 2315
Helixi232 – 2354
Helixi236 – 2449

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A7SX-ray1.12A27-251[»]
1AE5X-ray2.30A27-251[»]
1FY1X-ray2.50A27-251[»]
1FY3X-ray1.89A27-251[»]
ProteinModelPortaliP20160.
SMRiP20160. Positions 27-251.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20160.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 244218Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni46 – 7025Possesses antibiotic activityAdd
BLAST
Regioni52 – 8433HydrophobicAdd
BLAST

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

eggNOGiCOG5640.
GeneTreeiENSGT00760000118895.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP20160.
OMAiWIDSVIN.
OrthoDBiEOG73FQNK.
PhylomeDBiP20160.
TreeFamiTF335284.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_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 [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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361R → H AA sequence (PubMed:2404977)Curated
Sequence conflicti130 – 1301S → N AA sequence (PubMed:2026172)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti248 – 2481Missing in 50% of the molecules.
VAR_006496

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_001700.3.
UniGeneiHs.72885.

Genome annotation databases

EnsembliENST00000233997; ENSP00000233997; ENSG00000172232.
GeneIDi566.
KEGGihsa:566.
UCSCiuc002lpz.1. human.

Polymorphism databases

DMDMi416746.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS12044.1.
PIRi A46268. TRHUAZ.
RefSeqi NP_001691.1. NM_001700.3.
UniGenei Hs.72885.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A7S X-ray 1.12 A 27-251 [» ]
1AE5 X-ray 2.30 A 27-251 [» ]
1FY1 X-ray 2.50 A 27-251 [» ]
1FY3 X-ray 1.89 A 27-251 [» ]
ProteinModelPortali P20160.
SMRi P20160. Positions 27-251.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107043. 13 interactions.
IntActi P20160. 2 interactions.
MINTi MINT-4054423.
STRINGi 9606.ENSP00000233997.

Protein family/group databases

MEROPSi S01.971.

Polymorphism databases

DMDMi 416746.

Proteomic databases

PaxDbi P20160.
PRIDEi P20160.

Protocols and materials databases

DNASUi 566.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000233997 ; ENSP00000233997 ; ENSG00000172232 .
GeneIDi 566.
KEGGi hsa:566.
UCSCi uc002lpz.1. human.

Organism-specific databases

CTDi 566.
GeneCardsi GC19P000825.
HGNCi HGNC:913. AZU1.
HPAi HPA055851.
MIMi 162815. gene.
neXtProti NX_P20160.
PharmGKBi PA25206.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5640.
GeneTreei ENSGT00760000118895.
HOGENOMi HOG000251820.
HOVERGENi HBG013304.
InParanoidi P20160.
OMAi WIDSVIN.
OrthoDBi EOG73FQNK.
PhylomeDBi P20160.
TreeFami TF335284.

Miscellaneous databases

EvolutionaryTracei P20160.
GeneWikii Azurocidin_1.
GenomeRNAii 566.
NextBioi 2309.
PROi P20160.
SOURCEi Search...

Gene expression databases

Bgeei P20160.
CleanExi HS_AZU1.
Genevestigatori P20160.

Family and domain databases

InterProi IPR001254. Peptidase_S1.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the cDNA for the serine protease homolog CAP37/azurocidin, a microbicidal and chemotactic protein from human granulocytes."
    Morgan J.G., Sukiennicki T., Pereira H.A., Spitznagel J.K., Guerra M.E., Larrick J.L.
    J. Immunol. 147:3210-3214(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Three human elastase-like genes coordinately expressed in the myelomonocyte lineage are organized as a single genetic locus on 19pter."
    Zimmer M., Medcalf R.L., Fink T.M., Mattmann C., Lichter P., Jenne D.E.
    Proc. Natl. Acad. Sci. U.S.A. 89:8215-8219(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    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. "Complementary DNA sequence of human neutrophil azurocidin, an antibiotic with extensive homology to serine proteases."
    Almeida R.P., Melchior M., Campanelli D., Nathan C., Gabay J.E.
    Biochem. Biophys. Res. Commun. 177:688-695(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-251.
    Tissue: Neutrophil.
  6. "Amino acid sequence of CAP37, a human neutrophil granule-derived antibacterial and monocyte-specific chemotactic glycoprotein structurally similar to neutrophil elastase."
    Pohl J., Pereira H.A., Martin N.M., Spitznagel J.K.
    FEBS Lett. 272:200-204(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-248.
  7. "Covalent structure of two novel neutrophile leucocyte-derived proteins of porcine and human origin. Neutrophile elastase homologues with strong monocyte and fibroblast chemotactic activities."
    Flodgaard H., Oestergaard E., Bayne S., Svendsen A., Thomsen J., Engels M., Wollmer A.
    Eur. J. Biochem. 197:535-547(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-248.
    Tissue: Neutrophil.
  8. "CAP37, a human neutrophil-derived chemotactic factor with monocyte specific activity."
    Pereira H.A., Shafer W.M., Pohl J., Martin L.E., Spitznagel J.K.
    J. Clin. Invest. 85:1468-1476(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-68.
    Tissue: Neutrophil.
  9. "CAP 37, a 37 kD human neutrophil granule cationic protein shares homology with inflammatory proteinases."
    Pereira H.A., Spitznagel J.K., Pohl J., Wilson D.E., Morgan J., Palings I., Larrick J.W.
    Life Sci. 46:189-196(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-67.
    Tissue: Neutrophil.
  10. "Comparison of granule proteins from human polymorphonuclear leukocytes which are bactericidal toward Pseudomonas aeruginosa."
    Wasiluk K.R., Skubitz K.M., Gray B.H.
    Infect. Immun. 59:4193-4200(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-48, FUNCTION.
    Tissue: Leukocyte.
  11. "PMN elastases: a comparison of the specificity of human isozymes and the enzyme from other species toward substrates and inhibitors."
    Green B.G., Weston H., Ashe B.M., Doherty J., Finke P., Hagmann W., Lark M., Mao J., Maycock A., Moore V., Mumford R., Shah S., Walakovits L., Knight W.B.
    Arch. Biochem. Biophys. 286:284-292(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-47.
  12. Cited for: PROTEIN SEQUENCE OF 27-46.
  13. "Characterization of two azurphil granule proteases with active-site homology to neutrophil elastase."
    Wilde C.G., Snable J.L., Griffith J.E., Scott R.W.
    J. Biol. Chem. 265:2038-2041(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-46 AND 194-217.
  14. "Human neutrophil azurocidin synergizes with leukocyte elastase and cathepsin G in the killing of Capnocytophaga sputigena."
    Miyasaki K.T., Bodeau A.L.
    Infect. Immun. 60:4973-4975(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-46, FUNCTION.
  15. "Human neutrophil granule cationic protein CAP37 is a specific macrophage chemotaxin that shares homology with inflammatory proteinases."
    Morgan J.G., Pereira H.A., Sukiennicki T., Spitznagel J.K., Larrick J.W.
    Adv. Exp. Med. Biol. 305:89-96(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  16. "Synthetic bactericidal peptide based on CAP37: a 37-kDa human neutrophil granule-associated cationic antimicrobial protein chemotactic for monocytes."
    Pereira H.A., Erdem I., Pohl J., Spitznagel J.K.
    Proc. Natl. Acad. Sci. U.S.A. 90:4733-4737(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SYNTHESIS OF 46-70.
  17. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126; ASN-140 AND ASN-171.
    Tissue: Liver.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Structure of HBP, a multifunctional protein with a serine proteinase fold."
    Iversen L.F., Kastrup J.S., Bjoern S.E., Rasmussen P.B., Wiberg F.C., Flodgaard H.J., Larsen I.K.
    Nat. Struct. Biol. 4:265-268(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  20. Cited for: X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS).

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: October 29, 2014
This is version 152 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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3