Full text data of AZU1
AZU1
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Azurocidin (Cationic antimicrobial protein CAP37; Heparin-binding protein; HBP; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Azurocidin (Cationic antimicrobial protein CAP37; Heparin-binding protein; HBP; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P20160
ID CAP7_HUMAN Reviewed; 251 AA.
AC P20160; P80014; Q52LG4; Q9UCM1; Q9UCT5;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1993, sequence version 3.
DT 22-JAN-2014, entry version 145.
DE RecName: Full=Azurocidin;
DE AltName: Full=Cationic antimicrobial protein CAP37;
DE AltName: Full=Heparin-binding protein;
DE Short=HBP;
DE Flags: Precursor;
GN Name=AZU1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1919011;
RA Morgan J.G., Sukiennicki T., Pereira H.A., Spitznagel J.K.,
RA Guerra M.E., Larrick J.L.;
RT "Cloning of the cDNA for the serine protease homolog CAP37/azurocidin,
RT a microbicidal and chemotactic protein from human granulocytes.";
RL J. Immunol. 147:3210-3214(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1518849; DOI=10.1073/pnas.89.17.8215;
RA Zimmer M., Medcalf R.L., Fink T.M., Mattmann C., Lichter P.,
RA Jenne D.E.;
RT "Three human elastase-like genes coordinately expressed in the
RT myelomonocyte lineage are organized as a single genetic locus on
RT 19pter.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8215-8219(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-251.
RC TISSUE=Neutrophil;
RX PubMed=2049091; DOI=10.1016/0006-291X(91)91843-2;
RA Almeida R.P., Melchior M., Campanelli D., Nathan C., Gabay J.E.;
RT "Complementary DNA sequence of human neutrophil azurocidin, an
RT antibiotic with extensive homology to serine proteases.";
RL Biochem. Biophys. Res. Commun. 177:688-695(1991).
RN [6]
RP PROTEIN SEQUENCE OF 27-248.
RX PubMed=2226832; DOI=10.1016/0014-5793(90)80484-Z;
RA Pohl J., Pereira H.A., Martin N.M., Spitznagel J.K.;
RT "Amino acid sequence of CAP37, a human neutrophil granule-derived
RT antibacterial and monocyte-specific chemotactic glycoprotein
RT structurally similar to neutrophil elastase.";
RL FEBS Lett. 272:200-204(1990).
RN [7]
RP PROTEIN SEQUENCE OF 27-248.
RC TISSUE=Neutrophil;
RX PubMed=2026172; DOI=10.1111/j.1432-1033.1991.tb15942.x;
RA Flodgaard H., Oestergaard E., Bayne S., Svendsen A., Thomsen J.,
RA Engels M., Wollmer A.;
RT "Covalent structure of two novel neutrophile leucocyte-derived
RT proteins of porcine and human origin. Neutrophile elastase homologues
RT with strong monocyte and fibroblast chemotactic activities.";
RL Eur. J. Biochem. 197:535-547(1991).
RN [8]
RP PROTEIN SEQUENCE OF 27-68.
RC TISSUE=Neutrophil;
RX PubMed=2332502; DOI=10.1172/JCI114593;
RA Pereira H.A., Shafer W.M., Pohl J., Martin L.E., Spitznagel J.K.;
RT "CAP37, a human neutrophil-derived chemotactic factor with monocyte
RT specific activity.";
RL J. Clin. Invest. 85:1468-1476(1990).
RN [9]
RP PROTEIN SEQUENCE OF 27-67.
RC TISSUE=Neutrophil;
RX PubMed=2406527; DOI=10.1016/0024-3205(90)90104-Y;
RA Pereira H.A., Spitznagel J.K., Pohl J., Wilson D.E., Morgan J.,
RA Palings I., Larrick J.W.;
RT "CAP 37, a 37 kD human neutrophil granule cationic protein shares
RT homology with inflammatory proteinases.";
RL Life Sci. 46:189-196(1990).
RN [10]
RP PROTEIN SEQUENCE OF 27-48, AND FUNCTION.
RC TISSUE=Leukocyte;
RX PubMed=1937776;
RA Wasiluk K.R., Skubitz K.M., Gray B.H.;
RT "Comparison of granule proteins from human polymorphonuclear
RT leukocytes which are bactericidal toward Pseudomonas aeruginosa.";
RL Infect. Immun. 59:4193-4200(1991).
RN [11]
RP PROTEIN SEQUENCE OF 27-47.
RX PubMed=1897955; DOI=10.1016/0003-9861(91)90042-H;
RA Green B.G., Weston H., Ashe B.M., Doherty J., Finke P., Hagmann W.,
RA Lark M., Mao J., Maycock A., Moore V., Mumford R., Shah S.,
RA Walakovits L., Knight W.B.;
RT "PMN elastases: a comparison of the specificity of human isozymes and
RT the enzyme from other species toward substrates and inhibitors.";
RL Arch. Biochem. Biophys. 286:284-292(1991).
RN [12]
RP PROTEIN SEQUENCE OF 27-46.
RX PubMed=2501794; DOI=10.1073/pnas.86.14.5610;
RA Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C.,
RA Marra M.N., Seeger M., Nathan C.F.;
RT "Antibiotic proteins of human polymorphonuclear leukocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989).
RN [13]
RP PROTEIN SEQUENCE OF 27-46 AND 194-217.
RX PubMed=2404977;
RA Wilde C.G., Snable J.L., Griffith J.E., Scott R.W.;
RT "Characterization of two azurphil granule proteases with active-site
RT homology to neutrophil elastase.";
RL J. Biol. Chem. 265:2038-2041(1990).
RN [14]
RP PROTEIN SEQUENCE OF 27-46, AND FUNCTION.
RX PubMed=1399008;
RA Miyasaki K.T., Bodeau A.L.;
RT "Human neutrophil azurocidin synergizes with leukocyte elastase and
RT cathepsin G in the killing of Capnocytophaga sputigena.";
RL Infect. Immun. 60:4973-4975(1992).
RN [15]
RP REVIEW.
RX PubMed=1755383;
RA Morgan J.G., Pereira H.A., Sukiennicki T., Spitznagel J.K.,
RA Larrick J.W.;
RT "Human neutrophil granule cationic protein CAP37 is a specific
RT macrophage chemotaxin that shares homology with inflammatory
RT proteinases.";
RL Adv. Exp. Med. Biol. 305:89-96(1991).
RN [16]
RP SYNTHESIS OF 46-70.
RX PubMed=8506327; DOI=10.1073/pnas.90.10.4733;
RA Pereira H.A., Erdem I., Pohl J., Spitznagel J.K.;
RT "Synthetic bactericidal peptide based on CAP37: a 37-kDa human
RT neutrophil granule-associated cationic antimicrobial protein
RT chemotactic for monocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:4733-4737(1993).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126; ASN-140 AND ASN-171,
RP AND MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=9095193; DOI=10.1038/nsb0497-265;
RA Iversen L.F., Kastrup J.S., Bjoern S.E., Rasmussen P.B., Wiberg F.C.,
RA Flodgaard H.J., Larsen I.K.;
RT "Structure of HBP, a multifunctional protein with a serine proteinase
RT fold.";
RL Nat. Struct. Biol. 4:265-268(1997).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS).
RX PubMed=9761855; DOI=10.1107/S0907444997016193;
RA Karlsen S., Iversen L.F., Larsen I.K., Flodgaard H.J., Kastrup J.S.;
RT "Atomic resolution structure of human HBP/CAP37/azurocidin.";
RL Acta Crystallogr. D 54:598-609(1998).
CC -!- FUNCTION: This is a neutrophil granule-derived antibacterial and
CC monocyte- and fibroblast-specific chemotactic glycoprotein. Binds
CC heparin. The cytotoxic action is limited to many species of Gram-
CC negative bacteria; this specificity may be explained by a strong
CC affinity of the very basic N-terminal half for the negatively
CC charged lipopolysaccharides that are unique to the Gram-negative
CC bacterial outer envelope. It may play a role in mediating
CC recruitment of monocytes in the second wave of inflammation. Has
CC antibacterial activity against the Gram-nagative bacterium
CC P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa.
CC Acting alone, it does not have antimicrobial activity against the
CC Gram-negative bacteria A.actinomycetemcomitans ATCC 29532,
CC A.actinomycetemcomitans NCTC 9709, A.actinomycetemcomitans FDC-Y4,
CC H.aphrophilus ATCC 13252, E.corrodens ATCC 23834, C.sputigena ATCC
CC 33123, Capnocytophaga sp ATCC 33124, Capnocytophaga sp ATCC 27872
CC or E.coli ML-35. Has antibacterial activity against C.sputigena
CC ATCC 33123 when acting synergistically with either elastase or
CC cathepsin G.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Cytoplasmic
CC granules of neutrophils.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase
CC subfamily.
CC -!- SIMILARITY: Contains 1 peptidase S1 domain.
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DR EMBL; M96326; AAB59353.1; -; Genomic_DNA.
DR EMBL; AC004799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069495; AAH69495.1; -; mRNA.
DR EMBL; BC093931; AAH93931.1; -; mRNA.
DR EMBL; BC093933; AAH93933.1; -; mRNA.
DR EMBL; X58794; CAA41601.1; -; mRNA.
DR PIR; A46268; TRHUAZ.
DR RefSeq; NP_001691.1; NM_001700.3.
DR UniGene; Hs.72885; -.
DR PDB; 1A7S; X-ray; 1.12 A; A=27-251.
DR PDB; 1AE5; X-ray; 2.30 A; A=27-251.
DR PDB; 1FY1; X-ray; 2.50 A; A=27-251.
DR PDB; 1FY3; X-ray; 1.89 A; A=27-251.
DR PDBsum; 1A7S; -.
DR PDBsum; 1AE5; -.
DR PDBsum; 1FY1; -.
DR PDBsum; 1FY3; -.
DR ProteinModelPortal; P20160; -.
DR SMR; P20160; 27-251.
DR IntAct; P20160; 2.
DR MINT; MINT-4054423; -.
DR STRING; 9606.ENSP00000233997; -.
DR MEROPS; S01.971; -.
DR DMDM; 416746; -.
DR PaxDb; P20160; -.
DR PRIDE; P20160; -.
DR DNASU; 566; -.
DR Ensembl; ENST00000233997; ENSP00000233997; ENSG00000172232.
DR GeneID; 566; -.
DR KEGG; hsa:566; -.
DR UCSC; uc002lpz.1; human.
DR CTD; 566; -.
DR GeneCards; GC19P000825; -.
DR HGNC; HGNC:913; AZU1.
DR MIM; 162815; gene.
DR neXtProt; NX_P20160; -.
DR PharmGKB; PA25206; -.
DR eggNOG; COG5640; -.
DR HOGENOM; HOG000251820; -.
DR HOVERGEN; HBG013304; -.
DR InParanoid; P20160; -.
DR OMA; ALFRDWI; -.
DR OrthoDB; EOG73FQNK; -.
DR PhylomeDB; P20160; -.
DR EvolutionaryTrace; P20160; -.
DR GeneWiki; Azurocidin_1; -.
DR GenomeRNAi; 566; -.
DR NextBio; 2309; -.
DR PRO; PR:P20160; -.
DR Bgee; P20160; -.
DR CleanEx; HS_AZU1; -.
DR Genevestigator; P20160; -.
DR GO; GO:0042582; C:azurophil granule; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; NAS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0015643; F:toxic substance binding; NAS:UniProtKB.
DR GO; GO:0045123; P:cellular extravasation; NAS:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; TAS:UniProtKB.
DR GO; GO:0008347; P:glial cell migration; IDA:UniProtKB.
DR GO; GO:0050930; P:induction of positive chemotaxis; NAS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; NAS:UniProtKB.
DR GO; GO:0048246; P:macrophage chemotaxis; NAS:UniProtKB.
DR GO; GO:0001774; P:microglial cell activation; IEP:UniProtKB.
DR GO; GO:0042117; P:monocyte activation; TAS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; NAS:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IDA:UniProtKB.
DR GO; GO:0050754; P:positive regulation of fractalkine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0050725; P:positive regulation of interleukin-1 beta biosynthetic process; IDA:UniProtKB.
DR GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; IEP:UniProtKB.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IDA:UniProtKB.
DR GO; GO:0042535; P:positive regulation of tumor necrosis factor biosynthetic process; IDA:UniProtKB.
DR GO; GO:0007205; P:protein kinase C-activating G-protein coupled receptor signaling pathway; TAS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0043114; P:regulation of vascular permeability; NAS:UniProtKB.
DR InterPro; IPR001254; Peptidase_S1.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR009003; Trypsin-like_Pept_dom.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; FALSE_NEG.
DR PROSITE; PS00135; TRYPSIN_SER; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Chemotaxis;
KW Complete proteome; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Heparin-binding; Polymorphism; Reference proteome;
KW Serine protease homolog; Signal.
FT SIGNAL 1 26
FT CHAIN 27 248 Azurocidin.
FT /FTId=PRO_0000027705.
FT PROPEP 249 251
FT /FTId=PRO_0000027706.
FT DOMAIN 27 244 Peptidase S1.
FT REGION 46 70 Possesses antibiotic activity.
FT REGION 52 84 Hydrophobic.
FT CARBOHYD 126 126 N-linked (GlcNAc...); partial.
FT CARBOHYD 140 140 N-linked (GlcNAc...).
FT CARBOHYD 171 171 N-linked (GlcNAc...); partial.
FT DISULFID 52 68
FT DISULFID 149 207
FT DISULFID 180 186
FT DISULFID 197 222
FT VARIANT 248 248 Missing (in 50% of the molecules).
FT /FTId=VAR_006496.
FT MUTAGEN 52 52 C->S: Loss of antibiotic activity.
FT MUTAGEN 68 68 C->S: Loss of antibiotic activity.
FT CONFLICT 36 36 R -> H (in Ref. 13; AA sequence).
FT CONFLICT 130 130 S -> N (in Ref. 7; AA sequence).
FT STRAND 41 46
FT STRAND 49 58
FT STRAND 61 64
FT HELIX 66 68
FT STRAND 76 82
FT TURN 91 93
FT STRAND 95 103
FT TURN 109 112
FT STRAND 117 123
FT STRAND 148 154
FT STRAND 157 160
FT STRAND 168 174
FT HELIX 177 179
FT STRAND 184 188
FT STRAND 190 193
FT STRAND 204 207
FT STRAND 210 218
FT STRAND 227 231
FT HELIX 232 235
FT HELIX 236 244
SQ SEQUENCE 251 AA; 26886 MW; 22F80D9EBE87DE60 CRC64;
MTRLTVLALL AGLLASSRAG SSPLLDIVGG RKARPRQFPF LASIQNQGRH FCGGALIHAR
FVMTAASCFQ SQNPGVSTVV LGAYDLRRRE RQSRQTFSIS SMSENGYDPQ QNLNDLMLLQ
LDREANLTSS VTILPLPLQN ATVEAGTRCQ VAGWGSQRSG GRLSRFPRFV NVTVTPEDQC
RPNNVCTGVL TRRGGICNGD GGTPLVCEGL AHGVASFSLG PCGRGPDFFT RVALFRDWID
GVLNNPGPGP A
//
ID CAP7_HUMAN Reviewed; 251 AA.
AC P20160; P80014; Q52LG4; Q9UCM1; Q9UCT5;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1993, sequence version 3.
DT 22-JAN-2014, entry version 145.
DE RecName: Full=Azurocidin;
DE AltName: Full=Cationic antimicrobial protein CAP37;
DE AltName: Full=Heparin-binding protein;
DE Short=HBP;
DE Flags: Precursor;
GN Name=AZU1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1919011;
RA Morgan J.G., Sukiennicki T., Pereira H.A., Spitznagel J.K.,
RA Guerra M.E., Larrick J.L.;
RT "Cloning of the cDNA for the serine protease homolog CAP37/azurocidin,
RT a microbicidal and chemotactic protein from human granulocytes.";
RL J. Immunol. 147:3210-3214(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1518849; DOI=10.1073/pnas.89.17.8215;
RA Zimmer M., Medcalf R.L., Fink T.M., Mattmann C., Lichter P.,
RA Jenne D.E.;
RT "Three human elastase-like genes coordinately expressed in the
RT myelomonocyte lineage are organized as a single genetic locus on
RT 19pter.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8215-8219(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-251.
RC TISSUE=Neutrophil;
RX PubMed=2049091; DOI=10.1016/0006-291X(91)91843-2;
RA Almeida R.P., Melchior M., Campanelli D., Nathan C., Gabay J.E.;
RT "Complementary DNA sequence of human neutrophil azurocidin, an
RT antibiotic with extensive homology to serine proteases.";
RL Biochem. Biophys. Res. Commun. 177:688-695(1991).
RN [6]
RP PROTEIN SEQUENCE OF 27-248.
RX PubMed=2226832; DOI=10.1016/0014-5793(90)80484-Z;
RA Pohl J., Pereira H.A., Martin N.M., Spitznagel J.K.;
RT "Amino acid sequence of CAP37, a human neutrophil granule-derived
RT antibacterial and monocyte-specific chemotactic glycoprotein
RT structurally similar to neutrophil elastase.";
RL FEBS Lett. 272:200-204(1990).
RN [7]
RP PROTEIN SEQUENCE OF 27-248.
RC TISSUE=Neutrophil;
RX PubMed=2026172; DOI=10.1111/j.1432-1033.1991.tb15942.x;
RA Flodgaard H., Oestergaard E., Bayne S., Svendsen A., Thomsen J.,
RA Engels M., Wollmer A.;
RT "Covalent structure of two novel neutrophile leucocyte-derived
RT proteins of porcine and human origin. Neutrophile elastase homologues
RT with strong monocyte and fibroblast chemotactic activities.";
RL Eur. J. Biochem. 197:535-547(1991).
RN [8]
RP PROTEIN SEQUENCE OF 27-68.
RC TISSUE=Neutrophil;
RX PubMed=2332502; DOI=10.1172/JCI114593;
RA Pereira H.A., Shafer W.M., Pohl J., Martin L.E., Spitznagel J.K.;
RT "CAP37, a human neutrophil-derived chemotactic factor with monocyte
RT specific activity.";
RL J. Clin. Invest. 85:1468-1476(1990).
RN [9]
RP PROTEIN SEQUENCE OF 27-67.
RC TISSUE=Neutrophil;
RX PubMed=2406527; DOI=10.1016/0024-3205(90)90104-Y;
RA Pereira H.A., Spitznagel J.K., Pohl J., Wilson D.E., Morgan J.,
RA Palings I., Larrick J.W.;
RT "CAP 37, a 37 kD human neutrophil granule cationic protein shares
RT homology with inflammatory proteinases.";
RL Life Sci. 46:189-196(1990).
RN [10]
RP PROTEIN SEQUENCE OF 27-48, AND FUNCTION.
RC TISSUE=Leukocyte;
RX PubMed=1937776;
RA Wasiluk K.R., Skubitz K.M., Gray B.H.;
RT "Comparison of granule proteins from human polymorphonuclear
RT leukocytes which are bactericidal toward Pseudomonas aeruginosa.";
RL Infect. Immun. 59:4193-4200(1991).
RN [11]
RP PROTEIN SEQUENCE OF 27-47.
RX PubMed=1897955; DOI=10.1016/0003-9861(91)90042-H;
RA Green B.G., Weston H., Ashe B.M., Doherty J., Finke P., Hagmann W.,
RA Lark M., Mao J., Maycock A., Moore V., Mumford R., Shah S.,
RA Walakovits L., Knight W.B.;
RT "PMN elastases: a comparison of the specificity of human isozymes and
RT the enzyme from other species toward substrates and inhibitors.";
RL Arch. Biochem. Biophys. 286:284-292(1991).
RN [12]
RP PROTEIN SEQUENCE OF 27-46.
RX PubMed=2501794; DOI=10.1073/pnas.86.14.5610;
RA Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C.,
RA Marra M.N., Seeger M., Nathan C.F.;
RT "Antibiotic proteins of human polymorphonuclear leukocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989).
RN [13]
RP PROTEIN SEQUENCE OF 27-46 AND 194-217.
RX PubMed=2404977;
RA Wilde C.G., Snable J.L., Griffith J.E., Scott R.W.;
RT "Characterization of two azurphil granule proteases with active-site
RT homology to neutrophil elastase.";
RL J. Biol. Chem. 265:2038-2041(1990).
RN [14]
RP PROTEIN SEQUENCE OF 27-46, AND FUNCTION.
RX PubMed=1399008;
RA Miyasaki K.T., Bodeau A.L.;
RT "Human neutrophil azurocidin synergizes with leukocyte elastase and
RT cathepsin G in the killing of Capnocytophaga sputigena.";
RL Infect. Immun. 60:4973-4975(1992).
RN [15]
RP REVIEW.
RX PubMed=1755383;
RA Morgan J.G., Pereira H.A., Sukiennicki T., Spitznagel J.K.,
RA Larrick J.W.;
RT "Human neutrophil granule cationic protein CAP37 is a specific
RT macrophage chemotaxin that shares homology with inflammatory
RT proteinases.";
RL Adv. Exp. Med. Biol. 305:89-96(1991).
RN [16]
RP SYNTHESIS OF 46-70.
RX PubMed=8506327; DOI=10.1073/pnas.90.10.4733;
RA Pereira H.A., Erdem I., Pohl J., Spitznagel J.K.;
RT "Synthetic bactericidal peptide based on CAP37: a 37-kDa human
RT neutrophil granule-associated cationic antimicrobial protein
RT chemotactic for monocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:4733-4737(1993).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126; ASN-140 AND ASN-171,
RP AND MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=9095193; DOI=10.1038/nsb0497-265;
RA Iversen L.F., Kastrup J.S., Bjoern S.E., Rasmussen P.B., Wiberg F.C.,
RA Flodgaard H.J., Larsen I.K.;
RT "Structure of HBP, a multifunctional protein with a serine proteinase
RT fold.";
RL Nat. Struct. Biol. 4:265-268(1997).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS).
RX PubMed=9761855; DOI=10.1107/S0907444997016193;
RA Karlsen S., Iversen L.F., Larsen I.K., Flodgaard H.J., Kastrup J.S.;
RT "Atomic resolution structure of human HBP/CAP37/azurocidin.";
RL Acta Crystallogr. D 54:598-609(1998).
CC -!- FUNCTION: This is a neutrophil granule-derived antibacterial and
CC monocyte- and fibroblast-specific chemotactic glycoprotein. Binds
CC heparin. The cytotoxic action is limited to many species of Gram-
CC negative bacteria; this specificity may be explained by a strong
CC affinity of the very basic N-terminal half for the negatively
CC charged lipopolysaccharides that are unique to the Gram-negative
CC bacterial outer envelope. It may play a role in mediating
CC recruitment of monocytes in the second wave of inflammation. Has
CC antibacterial activity against the Gram-nagative bacterium
CC P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa.
CC Acting alone, it does not have antimicrobial activity against the
CC Gram-negative bacteria A.actinomycetemcomitans ATCC 29532,
CC A.actinomycetemcomitans NCTC 9709, A.actinomycetemcomitans FDC-Y4,
CC H.aphrophilus ATCC 13252, E.corrodens ATCC 23834, C.sputigena ATCC
CC 33123, Capnocytophaga sp ATCC 33124, Capnocytophaga sp ATCC 27872
CC or E.coli ML-35. Has antibacterial activity against C.sputigena
CC ATCC 33123 when acting synergistically with either elastase or
CC cathepsin G.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Cytoplasmic
CC granules of neutrophils.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase
CC subfamily.
CC -!- SIMILARITY: Contains 1 peptidase S1 domain.
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DR EMBL; M96326; AAB59353.1; -; Genomic_DNA.
DR EMBL; AC004799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069495; AAH69495.1; -; mRNA.
DR EMBL; BC093931; AAH93931.1; -; mRNA.
DR EMBL; BC093933; AAH93933.1; -; mRNA.
DR EMBL; X58794; CAA41601.1; -; mRNA.
DR PIR; A46268; TRHUAZ.
DR RefSeq; NP_001691.1; NM_001700.3.
DR UniGene; Hs.72885; -.
DR PDB; 1A7S; X-ray; 1.12 A; A=27-251.
DR PDB; 1AE5; X-ray; 2.30 A; A=27-251.
DR PDB; 1FY1; X-ray; 2.50 A; A=27-251.
DR PDB; 1FY3; X-ray; 1.89 A; A=27-251.
DR PDBsum; 1A7S; -.
DR PDBsum; 1AE5; -.
DR PDBsum; 1FY1; -.
DR PDBsum; 1FY3; -.
DR ProteinModelPortal; P20160; -.
DR SMR; P20160; 27-251.
DR IntAct; P20160; 2.
DR MINT; MINT-4054423; -.
DR STRING; 9606.ENSP00000233997; -.
DR MEROPS; S01.971; -.
DR DMDM; 416746; -.
DR PaxDb; P20160; -.
DR PRIDE; P20160; -.
DR DNASU; 566; -.
DR Ensembl; ENST00000233997; ENSP00000233997; ENSG00000172232.
DR GeneID; 566; -.
DR KEGG; hsa:566; -.
DR UCSC; uc002lpz.1; human.
DR CTD; 566; -.
DR GeneCards; GC19P000825; -.
DR HGNC; HGNC:913; AZU1.
DR MIM; 162815; gene.
DR neXtProt; NX_P20160; -.
DR PharmGKB; PA25206; -.
DR eggNOG; COG5640; -.
DR HOGENOM; HOG000251820; -.
DR HOVERGEN; HBG013304; -.
DR InParanoid; P20160; -.
DR OMA; ALFRDWI; -.
DR OrthoDB; EOG73FQNK; -.
DR PhylomeDB; P20160; -.
DR EvolutionaryTrace; P20160; -.
DR GeneWiki; Azurocidin_1; -.
DR GenomeRNAi; 566; -.
DR NextBio; 2309; -.
DR PRO; PR:P20160; -.
DR Bgee; P20160; -.
DR CleanEx; HS_AZU1; -.
DR Genevestigator; P20160; -.
DR GO; GO:0042582; C:azurophil granule; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; NAS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0015643; F:toxic substance binding; NAS:UniProtKB.
DR GO; GO:0045123; P:cellular extravasation; NAS:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; TAS:UniProtKB.
DR GO; GO:0008347; P:glial cell migration; IDA:UniProtKB.
DR GO; GO:0050930; P:induction of positive chemotaxis; NAS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; NAS:UniProtKB.
DR GO; GO:0048246; P:macrophage chemotaxis; NAS:UniProtKB.
DR GO; GO:0001774; P:microglial cell activation; IEP:UniProtKB.
DR GO; GO:0042117; P:monocyte activation; TAS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; NAS:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IDA:UniProtKB.
DR GO; GO:0050754; P:positive regulation of fractalkine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0050725; P:positive regulation of interleukin-1 beta biosynthetic process; IDA:UniProtKB.
DR GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; IEP:UniProtKB.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IDA:UniProtKB.
DR GO; GO:0042535; P:positive regulation of tumor necrosis factor biosynthetic process; IDA:UniProtKB.
DR GO; GO:0007205; P:protein kinase C-activating G-protein coupled receptor signaling pathway; TAS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0043114; P:regulation of vascular permeability; NAS:UniProtKB.
DR InterPro; IPR001254; Peptidase_S1.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR009003; Trypsin-like_Pept_dom.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; FALSE_NEG.
DR PROSITE; PS00135; TRYPSIN_SER; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Chemotaxis;
KW Complete proteome; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Heparin-binding; Polymorphism; Reference proteome;
KW Serine protease homolog; Signal.
FT SIGNAL 1 26
FT CHAIN 27 248 Azurocidin.
FT /FTId=PRO_0000027705.
FT PROPEP 249 251
FT /FTId=PRO_0000027706.
FT DOMAIN 27 244 Peptidase S1.
FT REGION 46 70 Possesses antibiotic activity.
FT REGION 52 84 Hydrophobic.
FT CARBOHYD 126 126 N-linked (GlcNAc...); partial.
FT CARBOHYD 140 140 N-linked (GlcNAc...).
FT CARBOHYD 171 171 N-linked (GlcNAc...); partial.
FT DISULFID 52 68
FT DISULFID 149 207
FT DISULFID 180 186
FT DISULFID 197 222
FT VARIANT 248 248 Missing (in 50% of the molecules).
FT /FTId=VAR_006496.
FT MUTAGEN 52 52 C->S: Loss of antibiotic activity.
FT MUTAGEN 68 68 C->S: Loss of antibiotic activity.
FT CONFLICT 36 36 R -> H (in Ref. 13; AA sequence).
FT CONFLICT 130 130 S -> N (in Ref. 7; AA sequence).
FT STRAND 41 46
FT STRAND 49 58
FT STRAND 61 64
FT HELIX 66 68
FT STRAND 76 82
FT TURN 91 93
FT STRAND 95 103
FT TURN 109 112
FT STRAND 117 123
FT STRAND 148 154
FT STRAND 157 160
FT STRAND 168 174
FT HELIX 177 179
FT STRAND 184 188
FT STRAND 190 193
FT STRAND 204 207
FT STRAND 210 218
FT STRAND 227 231
FT HELIX 232 235
FT HELIX 236 244
SQ SEQUENCE 251 AA; 26886 MW; 22F80D9EBE87DE60 CRC64;
MTRLTVLALL AGLLASSRAG SSPLLDIVGG RKARPRQFPF LASIQNQGRH FCGGALIHAR
FVMTAASCFQ SQNPGVSTVV LGAYDLRRRE RQSRQTFSIS SMSENGYDPQ QNLNDLMLLQ
LDREANLTSS VTILPLPLQN ATVEAGTRCQ VAGWGSQRSG GRLSRFPRFV NVTVTPEDQC
RPNNVCTGVL TRRGGICNGD GGTPLVCEGL AHGVASFSLG PCGRGPDFFT RVALFRDWID
GVLNNPGPGP A
//
MIM
162815
*RECORD*
*FIELD* NO
162815
*FIELD* TI
*162815 NEUTROPHIL AZUROCIDIN; NAZC
;;AZUROCIDIN; AZU1;;
CATIONIC ANTIMICROBIAL PROTEIN-37; CAP37
read more*FIELD* TX
Azurophil granules, specialized lysosomes of the neutrophil, contain at
least 10 proteins implicated in the killing of microorganisms. Among
these are 3 serine proteases that are additionally involved in degrading
connective tissues: cathepsin G (116830), neutrophil elastase (130130),
and proteinase 3 (PRTN3; 177020). These 3 proteins have collectively
been termed serprocidins. Campanelli et al. (1990) isolated a 29-kD
azurophil granule antibiotic protein, azurocidin, whose N-terminal
sequence was highly homologous to the serprocidins but which lacked
proteolytic activity. Azurocidin is the same as the 37-kD cationic
antimicrobial protein of human neutrophil granules called CAP37. CAP37
is a specific chemoattractant for monocytes. It lacks the chemotactic
activity for neutrophils and lymphocytes. It is probably responsible for
the wave of monocytes that follows the initial wave of PMNs typical of
the inflammatory response (Pereira et al., 1990). Almeida et al. (1991)
used a monospecific antibody to isolate from human bone marrow a cDNA
encoding the entire azurocidin protein in its mature form, along with an
N-terminal 24-residue hydrophobic peptide. The primary sequence was
highly homologous to elastase, proteinase 3, cathepsin G, T-cell
granzymes, and other serine proteases. However, azurocidin has gly for
ser and ser for his substitutions in the catalytic triad. Southern blot
analysis of human genomic DNA suggested the existence of a single
azurocidin coding sequence.
Zimmer et al. (1992) showed that the genes encoding azurocidin,
neutrophil elastase, and proteinase 3 are in a cluster located at the
tip of the short arm of chromosome 19. Each gene has 5 exons. All 3
genes are expressed coordinately and their protein products are packaged
together into azurophil granules during neutrophil differentiation.
*FIELD* RF
1. Almeida, R. P.; Melchior, M.; Campanelli, D.; Nathan, C.; Gabay,
J. E.: Complementary DNA sequence of human neutrophil azurocidin,
an antibiotic with extensive homology to serine proteases. Biochem.
Biophys. Res. Commun. 177: 688-695, 1991.
2. Campanelli, D.; Detmers, P. A.; Nathan, C. F.; Gabay, J. E.: Azurocidin
and a homologous serine protease from neutrophils: differential antimicrobial
and proteolytic properties. J. Clin. Invest. 85: 904-915, 1990.
3. Pereira, H. A.; Shafer, W. M.; Pohl, J.; Martin, L. E.; Spitznagel,
J. K.: CAP37: a human neutrophil-derived chemotactic factor with
monocyte specific activity. J. Clin. Invest. 85: 1468-1476, 1990.
4. Zimmer, M.; Medcalf, R. L.; Fink, T. M.; Mattmann, C.; Lichter,
P.; Jenne, D. E.: Three human elastase-like genes coordinately expressed
in the myelomonocyte lineage are organized as a single genetic locus
on 19pter. Proc. Nat. Acad. Sci. 89: 8215-8219, 1992.
*FIELD* CN
Alan F. Scott - updated: 8/15/1996
*FIELD* CD
Victor A. McKusick: 8/19/1991
*FIELD* ED
mark: 08/19/1996
terry: 8/15/1996
carol: 11/23/1992
carol: 11/3/1992
carol: 9/29/1992
supermim: 3/16/1992
carol: 10/23/1991
carol: 10/15/1991
*RECORD*
*FIELD* NO
162815
*FIELD* TI
*162815 NEUTROPHIL AZUROCIDIN; NAZC
;;AZUROCIDIN; AZU1;;
CATIONIC ANTIMICROBIAL PROTEIN-37; CAP37
read more*FIELD* TX
Azurophil granules, specialized lysosomes of the neutrophil, contain at
least 10 proteins implicated in the killing of microorganisms. Among
these are 3 serine proteases that are additionally involved in degrading
connective tissues: cathepsin G (116830), neutrophil elastase (130130),
and proteinase 3 (PRTN3; 177020). These 3 proteins have collectively
been termed serprocidins. Campanelli et al. (1990) isolated a 29-kD
azurophil granule antibiotic protein, azurocidin, whose N-terminal
sequence was highly homologous to the serprocidins but which lacked
proteolytic activity. Azurocidin is the same as the 37-kD cationic
antimicrobial protein of human neutrophil granules called CAP37. CAP37
is a specific chemoattractant for monocytes. It lacks the chemotactic
activity for neutrophils and lymphocytes. It is probably responsible for
the wave of monocytes that follows the initial wave of PMNs typical of
the inflammatory response (Pereira et al., 1990). Almeida et al. (1991)
used a monospecific antibody to isolate from human bone marrow a cDNA
encoding the entire azurocidin protein in its mature form, along with an
N-terminal 24-residue hydrophobic peptide. The primary sequence was
highly homologous to elastase, proteinase 3, cathepsin G, T-cell
granzymes, and other serine proteases. However, azurocidin has gly for
ser and ser for his substitutions in the catalytic triad. Southern blot
analysis of human genomic DNA suggested the existence of a single
azurocidin coding sequence.
Zimmer et al. (1992) showed that the genes encoding azurocidin,
neutrophil elastase, and proteinase 3 are in a cluster located at the
tip of the short arm of chromosome 19. Each gene has 5 exons. All 3
genes are expressed coordinately and their protein products are packaged
together into azurophil granules during neutrophil differentiation.
*FIELD* RF
1. Almeida, R. P.; Melchior, M.; Campanelli, D.; Nathan, C.; Gabay,
J. E.: Complementary DNA sequence of human neutrophil azurocidin,
an antibiotic with extensive homology to serine proteases. Biochem.
Biophys. Res. Commun. 177: 688-695, 1991.
2. Campanelli, D.; Detmers, P. A.; Nathan, C. F.; Gabay, J. E.: Azurocidin
and a homologous serine protease from neutrophils: differential antimicrobial
and proteolytic properties. J. Clin. Invest. 85: 904-915, 1990.
3. Pereira, H. A.; Shafer, W. M.; Pohl, J.; Martin, L. E.; Spitznagel,
J. K.: CAP37: a human neutrophil-derived chemotactic factor with
monocyte specific activity. J. Clin. Invest. 85: 1468-1476, 1990.
4. Zimmer, M.; Medcalf, R. L.; Fink, T. M.; Mattmann, C.; Lichter,
P.; Jenne, D. E.: Three human elastase-like genes coordinately expressed
in the myelomonocyte lineage are organized as a single genetic locus
on 19pter. Proc. Nat. Acad. Sci. 89: 8215-8219, 1992.
*FIELD* CN
Alan F. Scott - updated: 8/15/1996
*FIELD* CD
Victor A. McKusick: 8/19/1991
*FIELD* ED
mark: 08/19/1996
terry: 8/15/1996
carol: 11/23/1992
carol: 11/3/1992
carol: 9/29/1992
supermim: 3/16/1992
carol: 10/23/1991
carol: 10/15/1991