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Neutrophil elastase (EC 3.4.21.37) (Bone marrow serine protease) (Elastase-2) (Human leukocyte elastase) (HLE) (Medullasin) (PMN elastase)

 ELNE_HUMAN              Reviewed;         267 AA.
P08246; P09649; Q6B0D9; Q6LDP5;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
25-OCT-2017, entry version 193.
RecName: Full=Neutrophil elastase;
EC=3.4.21.37;
AltName: Full=Bone marrow serine protease;
AltName: Full=Elastase-2;
AltName: Full=Human leukocyte elastase;
Short=HLE;
AltName: Full=Medullasin;
AltName: Full=PMN elastase;
Flags: Precursor;
Name=ELANE; Synonyms=ELA2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3479752; DOI=10.1093/nar/15.22.9601;
Nakamura H., Okano K., Aoki Y., Shimizu H., Naruto M.;
"Nucleotide sequence of human bone marrow serine protease (medullasin)
gene.";
Nucleic Acids Res. 15:9601-9601(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2902087;
Takahashi H., Nukiwa T., Yoshimura K., Quick C.D., States D.J.,
Holmes M.D., Whang-Peng J., Knutsen T., Crystal R.G.;
"Structure of the human neutrophil elastase gene.";
J. Biol. Chem. 263:14739-14747(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2775493;
Farley D., Travis J., Salvesen G.;
"The human neutrophil elastase gene. Analysis of the nucleotide
sequence reveals three distinct classes of repetitive DNA.";
Biol. Chem. Hoppe-Seyler 370:737-744(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2322278; DOI=10.1016/0006-291X(90)90668-D;
Okano K., Aoki Y., Shimizu H., Naruto M.;
"Functional expression of human leukocyte elastase (HLE)/medullasin in
eukaryotic cells.";
Biochem. Biophys. Res. Commun. 167:1326-1332(1990).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-219; LEU-257 AND
LEU-262.
NIEHS SNPs program;
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 30-267.
PubMed=2822677;
Okano K., Aoki Y., Sakurai T., Kajitani M., Kanai S., Shimazu T.,
Shimizu H., Naruto M.;
"Molecular cloning of complementary DNA for human medullasin: an
inflammatory serine protease in bone marrow cells.";
J. Biochem. 102:13-16(1987).
[8]
PROTEIN SEQUENCE OF 30-247.
PubMed=3550808; DOI=10.1073/pnas.84.8.2228;
Sinha S., Watorek W., Karr S., Giles J., Bode W., Travis J.;
"Primary structure of human neutrophil elastase.";
Proc. Natl. Acad. Sci. U.S.A. 84:2228-2232(1987).
[9]
PRELIMINARY PROTEIN SEQUENCE OF 30-103.
Travis J., Giles P.J., Porcelli L., Reilly C.F., Baugh R., Powers J.;
(In) Protein degradation in health and disease,
Ciba Foundation Symposium, pp.75:51-68, Excerpta Medica,
Amsterdam and Oxford (1980).
[10]
PROTEIN SEQUENCE OF 30-49.
PubMed=2501794; DOI=10.1073/pnas.86.14.5610;
Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C.,
Marra M.N., Seeger M., Nathan C.F.;
"Antibiotic proteins of human polymorphonuclear leukocytes.";
Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989).
[11]
PROTEIN SEQUENCE OF 30-49.
TISSUE=Neutrophil;
PubMed=7897245; DOI=10.1016/0022-1759(94)00295-8;
Gaskin G., Kendal H., Coulthart A., Turner N., Pusey C.D.;
"Use of proteinase 3 purified by reverse phase HPLC to detect
autoantibodies in systemic vasculitis.";
J. Immunol. Methods 180:25-33(1995).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 75-267.
PubMed=3422232;
Takahashi H., Nukiwa T., Basset P., Cystal R.G.;
"Myelomonocytic cell lineage expression of the neutrophil elastase
gene.";
J. Biol. Chem. 263:2543-2547(1988).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 123-267.
PubMed=2462434;
Farley D., Salvesen G.S., Travis J.;
"Molecular cloning of human neutrophil elastase.";
Biol. Chem. Hoppe-Seyler 369:3-7(1988).
[14]
PROTEIN SEQUENCE OF 262-267.
PubMed=1859409; DOI=10.1016/0006-291X(91)90135-T;
Aoki Y., Hase T.;
"The primary structure and elastinolytic activity of medullasin (a
serine protease of bone marrow).";
Biochem. Biophys. Res. Commun. 178:501-506(1991).
[15]
FUNCTION.
PubMed=15140022; DOI=10.1111/j.0906-6705.2004.00145.x;
Tralau T., Meyer-Hoffert U., Schroder J.M., Wiedow O.;
"Human leukocyte elastase and cathepsin G are specific inhibitors of
C5a-dependent neutrophil enzyme release and chemotaxis.";
Exp. Dermatol. 13:316-325(2004).
[16]
INTERACTION WITH NOTCH2NL, AND CHARACTERIZATION OF VARIANT CH GLN-220.
PubMed=14673143; DOI=10.1128/MCB.24.1.58-70.2004;
Duan Z., Li F.-Q., Wechsler J., Meade-White K., Williams K.,
Benson K.F., Horwitz M.;
"A novel notch protein, N2N, targeted by neutrophil elastase and
implicated in hereditary neutropenia.";
Mol. Cell. Biol. 24:58-70(2004).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-88 AND ASN-173.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[20]
X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS).
PubMed=2911584; DOI=10.1073/pnas.86.1.7;
Navia M.A., McKeever B.M., Springer J.P., Lin T.-Y., Williams H.R.,
Fluder E.M., Dorn C.P., Hoogsteen K.;
"Structure of human neutrophil elastase in complex with a peptide
chloromethyl ketone inhibitor at 1.84-A resolution.";
Proc. Natl. Acad. Sci. U.S.A. 86:7-11(1989).
[21]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=3391280; DOI=10.1016/0014-5793(88)80118-2;
Wei A.-Z., Mayr I., Bode W.;
"The refined 2.3-A crystal structure of human leukocyte elastase in a
complex with a valine chloromethyl ketone inhibitor.";
FEBS Lett. 234:367-373(1988).
[22]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
PubMed=3640709;
Bode W., Wei A.-Z., Huber R., Meyer E., Travis J., Neumann S.;
"X-ray crystal structure of the complex of human leukocyte elastase
(PMN elastase) and the third domain of the turkey ovomucoid
inhibitor.";
EMBO J. 5:2453-2458(1986).
[23]
VARIANTS CH VAL-61; PHE-206 AND GLN-220.
PubMed=10581030; DOI=10.1038/70544;
Horwitz M., Benson K.F., Person R.E., Aprikyan A.G., Dale D.C.;
"Mutations in ELA2, encoding neutrophil elastase, define a 21-day
biological clock in cyclic haematopoiesis.";
Nat. Genet. 23:433-436(1999).
[24]
VARIANTS SCN1 THR-57; THR-60; SER-71; MET-101; LEU-126; LEU-139;
VAL-210 AND ARG-214, AND VARIANT CH LEU-139.
PubMed=11001877;
Dale D.C., Person R.E., Bolyard A.A., Aprikyan A.G., Bos C.,
Bonilla M.A., Boxer L.A., Kannourakis G., Zeidler C., Welte K.,
Benson K.F., Horwitz M.;
"Mutations in the gene encoding neutrophil elastase in congenital and
cyclic neutropenia.";
Blood 96:2317-2322(2000).
[25]
VARIANTS SCN1 TYR-55; GLU-85; PRO-GLN-LEU-123 INS; LEU-126; SER-151;
190-VAL--PHE-199 DEL AND ARG-205.
PubMed=11675333; DOI=10.1182/blood.V98.9.2645;
Ancliff P.J., Gale R.E., Liesner R., Hann I.M., Linch D.C.;
"Mutations in the ELA2 gene encoding neutrophil elastase are present
in most patients with sporadic severe congenital neutropenia but only
in some patients with the familial form of the disease.";
Blood 98:2645-2650(2001).
[26]
VARIANT SCN1 ARG-71.
PubMed=12091371; DOI=10.1182/blood-2002-01-0060;
Ancliff P.J., Gale R.E., Watts M.J., Liesner R., Hann I.M.,
Strobel S., Linch D.C.;
"Paternal mosaicism proves the pathogenic nature of mutations in
neutrophil elastase in severe congenital neutropenia.";
Blood 100:707-709(2002).
[27]
VARIANTS SCN1 LEU-42; PRO-47; LEU-53; PRO-81; PRO-84; PRO-121;
PRO-127; LEU-139; PRO-152 AND 190-VAL--199-PHE DEL, VARIANTS CH
LEU-43; PHE-46; MET-82; LEU-126; LEU-139; 190-VAL--199-PHE DEL;
ILE-219 AND GLN-220, AND VARIANT LEU-262.
PubMed=14962902; DOI=10.1182/blood-2003-10-3518;
Bellanne-Chantelot C., Clauin S., Leblanc T., Cassinat B.,
Rodrigues-Lima F., Beaufils S., Vaury C., Barkaoui M., Fenneteau O.,
Maier-Redelsperger M., Chomienne C., Donadieu J.;
"Mutations in the ELA2 gene correlate with more severe expression of
neutropenia: a study of 81 patients from the French Neutropenia
Register.";
Blood 103:4119-4125(2004).
[28]
VARIANTS SCN1 LEU-98 AND LEU-101, AND CHARACTERIZATION OF VARIANTS
SCN1 LEU-98 AND LEU-101.
PubMed=17436313; DOI=10.1002/humu.20529;
Salipante S.J., Benson K.F., Luty J., Hadavi V., Kariminejad R.,
Kariminejad M.H., Rezaei N., Horwitz M.S.;
"Double de novo mutations of ELA2 in cyclic and severe congenital
neutropenia.";
Hum. Mutat. 28:874-881(2007).
[29]
VARIANT SCN1 VAL-57.
PubMed=18946670; DOI=10.1007/s00277-008-0629-y;
Lee S.T., Yoon H.S., Kim H.J., Lee J.H., Park J.H., Kim S.H.,
Seo J.J., Im H.J.;
"A novel mutation Ala57Val of the ELA2 gene in a Korean boy with
severe congenital neutropenia.";
Ann. Hematol. 88:593-595(2009).
[30]
VARIANTS SCN1 ARG-44; CYS-46; TYR-53; ARG-85; ARG-203 AND CYS-203.
PubMed=19036076; DOI=10.1111/j.1365-2141.2008.07493.x;
Smith B.N., Ancliff P.J., Pizzey A., Khwaja A., Linch D.C., Gale R.E.;
"Homozygous HAX1 mutations in severe congenital neutropenia patients
with sporadic disease: a novel mutation in two unrelated British
kindreds.";
Br. J. Haematol. 144:762-770(2009).
[31]
VARIANTS SCN1 LEU-42; PRO-81; MET-101 AND LEU-126.
PubMed=19415009; DOI=10.1097/MPH.0b013e3181984dbe;
Shiohara M., Shigemura T., Saito S., Tanaka M., Yanagisawa R.,
Sakashita K., Asada H., Ishii E., Koike K., Chin M., Kobayashi M.,
Koike K.;
"Ela2 mutations and clinical manifestations in familial congenital
neutropenia.";
J. Pediatr. Hematol. Oncol. 31:319-324(2009).
[32]
VARIANTS SCN1 VAL-25 AND THR-166.
PubMed=20220065; DOI=10.3324/haematol.2009.017665;
Germeshausen M., Zeidler C., Stuhrmann M., Lanciotti M., Ballmaier M.,
Welte K.;
"Digenic mutations in severe congenital neutropenia.";
Haematologica 95:1207-1210(2010).
[33]
VARIANTS SCN1 PRO-59 AND GLU-235.
PubMed=19927291; DOI=10.1002/pbc.22350;
Fioredda F., Calvillo M., Lanciotti M., Lanza T., Giunti L.,
Castagnola E., Lorenzi I., Tonelli R., Ghezzi P., Dufour C.;
"Pegfilgrastim in children with severe congenital neutropenia.";
Pediatr. Blood Cancer 54:465-467(2010).
[34]
VARIANT SCN1 SER-57.
PubMed=20803142; DOI=10.1007/s00277-010-1056-4;
van de Vosse E., Verhard E.M., Tool A.J., de Visser A.W.,
Kuijpers T.W., Hiemstra P.S., van Dissel J.T.;
"Severe congenital neutropenia in a multigenerational family with a
novel neutrophil elastase (ELANE) mutation.";
Ann. Hematol. 90:151-158(2011).
[35]
VARIANTS SCN1 THR-131; PRO-152; GLY-235 AND 190-VAL--199-PHE DEL.
PubMed=21425445; DOI=10.1002/pbc.23104;
Kurnikova M., Maschan M., Dinova E., Shagina I., Finogenova N.,
Mamedova E., Polovtseva T., Shagin D., Shcherbina A.;
"Four novel ELANE mutations in patients with congenital neutropenia.";
Pediatr. Blood Cancer 57:332-335(2011).
[36]
VARIANTS SCN1 VAL-25; LEU-42; LEU-43; GLU-45; PHE-46; ARG-47; PRO-49;
SER-55; ARG-56; SER-57; THR-57; VAL-57; PRO-59; 60-ILE-ALA-61 DELINS
ARG; THR-60; VAL-61; VAL-65 DEL; 66-MET--HIS-70 DEL; TRP-67; ARG-71;
PHE-71; TYR-71; GLY-72; GLY-80; PRO-81; MET-82; PRO-84; GLU-85;
LEU-98; MET-98; LEU-101; MET-101; LEU-103; PRO-103; ASN-120; PHE-120;
SER-120; PRO-121; HIS-123; ILE-124; LEU-126; ASP-127; THR-131;
ASP-136; ARG-139; LEU-139; PHE-151; TRP-151; TYR-151; PRO-152;
ASP-153; PRO-153; ARG-156; CYS-156; THR-166; ARG-203; ARG-205;
SER-206; GLY-208; ARG-214; GLU-214; ILE-219; GLN-220; PRO-233; GLU-235
AND GLY-235, VARIANTS CH LEU-45; VAL-61; PRO-81; LEU-97; ASN-104;
PHE-120; LEU-126; LEU-139; HIS-143; 190-VAL--199-PHE DEL; CYS-203;
ILE-209; TRP-210; ILE-219 AND GLN-220, AND VARIANTS VAL-118; ARG-125;
MET-135 AND LEU-257.
PubMed=23463630; DOI=10.1002/humu.22308;
Germeshausen M., Deerberg S., Peter Y., Reimer C., Kratz C.P.,
Ballmaier M.;
"The spectrum of ELANE mutations and their implications in severe
congenital and cyclic neutropenia.";
Hum. Mutat. 34:905-914(2013).
-!- FUNCTION: Modifies the functions of natural killer cells,
monocytes and granulocytes. Inhibits C5a-dependent neutrophil
enzyme release and chemotaxis. {ECO:0000269|PubMed:15140022}.
-!- CATALYTIC ACTIVITY: Hydrolysis of proteins, including elastin.
Preferential cleavage: Val-|-Xaa > Ala-|-Xaa.
-!- SUBUNIT: Interacts with NOTCH2NL. {ECO:0000269|PubMed:14673143}.
-!- INTERACTION:
Q07563:Col17a1 (xeno); NbExp=2; IntAct=EBI-986345, EBI-6251005;
-!- TISSUE SPECIFICITY: Bone marrow cells.
-!- DISEASE: Cyclic haematopoiesis (CH) [MIM:162800]: Autosomal
dominant disease in which blood-cell production from the bone
marrow oscillates with 21-day periodicity. Circulating neutrophils
vary between almost normal numbers and zero. During intervals of
neutropenia, affected individuals are at risk for opportunistic
infection. Monocytes, platelets, lymphocytes and reticulocytes
also cycle with the same frequency. {ECO:0000269|PubMed:10581030,
ECO:0000269|PubMed:11001877, ECO:0000269|PubMed:14673143,
ECO:0000269|PubMed:14962902, ECO:0000269|PubMed:23463630}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Neutropenia, severe congenital 1, autosomal dominant
(SCN1) [MIM:202700]: A disorder of hematopoiesis characterized by
maturation arrest of granulopoiesis at the level of promyelocytes
with peripheral blood absolute neutrophil counts below 0.5 x
10(9)/l and early onset of severe bacterial infections.
{ECO:0000269|PubMed:11001877, ECO:0000269|PubMed:11675333,
ECO:0000269|PubMed:12091371, ECO:0000269|PubMed:14962902,
ECO:0000269|PubMed:17436313, ECO:0000269|PubMed:18946670,
ECO:0000269|PubMed:19036076, ECO:0000269|PubMed:19415009,
ECO:0000269|PubMed:19927291, ECO:0000269|PubMed:20220065,
ECO:0000269|PubMed:20803142, ECO:0000269|PubMed:21425445,
ECO:0000269|PubMed:23463630}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the peptidase S1 family. Elastase
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- SEQUENCE CAUTION:
Sequence=CAA29300.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=CCHMC molecular genetics laboratory mutation
database; Note=ELA2 elastase, neutrophil expressed (ELANE);
URL="http://lovd.nl/ELANE";
-!- WEB RESOURCE: Name=ELA2base; Note=ELA2 mutation db;
URL="http://structure.bmc.lu.se/idbase/ELA2base/";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ela2/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Elastase entry;
URL="https://en.wikipedia.org/wiki/Elastase";
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EMBL; Y00477; CAA68537.1; -; Genomic_DNA.
EMBL; M20203; AAA36359.1; -; Genomic_DNA.
EMBL; M20199; AAA36359.1; JOINED; Genomic_DNA.
EMBL; M20200; AAA36359.1; JOINED; Genomic_DNA.
EMBL; M20201; AAA36359.1; JOINED; Genomic_DNA.
EMBL; M34379; AAA36173.1; -; mRNA.
EMBL; AY596461; AAS89303.1; -; Genomic_DNA.
EMBL; BC074816; AAH74816.1; -; mRNA.
EMBL; BC074817; AAH74817.1; -; mRNA.
EMBL; D00187; BAA00128.1; -; mRNA.
EMBL; X05875; CAA29299.1; -; mRNA.
EMBL; X05875; CAA29300.1; ALT_INIT; mRNA.
EMBL; J03545; AAA52378.1; -; mRNA.
EMBL; M27783; AAA35792.1; -; mRNA.
CCDS; CCDS12045.1; -.
PIR; A31976; ELHUL.
RefSeq; NP_001963.1; NM_001972.3.
RefSeq; XP_011526077.1; XM_011527775.1.
RefSeq; XP_011526078.1; XM_011527776.1.
UniGene; Hs.99863; -.
PDB; 1B0F; X-ray; 3.00 A; A=30-247.
PDB; 1H1B; X-ray; 2.00 A; A/B=30-247.
PDB; 1HNE; X-ray; 1.84 A; E=30-247.
PDB; 1PPF; X-ray; 1.80 A; E=30-247.
PDB; 1PPG; X-ray; 2.30 A; E=30-247.
PDB; 2RG3; X-ray; 1.80 A; A=30-247.
PDB; 2Z7F; X-ray; 1.70 A; E=30-247.
PDB; 3Q76; X-ray; 1.86 A; A/B=30-247.
PDB; 3Q77; X-ray; 2.00 A; A=30-247.
PDB; 4NZL; X-ray; 1.85 A; A=30-247.
PDB; 4WVP; X-ray; 1.63 A; E=30-247.
PDB; 5A09; X-ray; 1.81 A; A=30-247.
PDB; 5A0A; X-ray; 1.78 A; E=30-247.
PDB; 5A0B; X-ray; 2.23 A; A=30-247.
PDB; 5A0C; X-ray; 2.10 A; A/B=30-247.
PDB; 5A8X; X-ray; 2.23 A; A=30-247.
PDB; 5A8Y; X-ray; 1.90 A; A=30-247.
PDB; 5A8Z; X-ray; 2.00 A; A=30-247.
PDB; 5ABW; X-ray; 1.60 A; A=30-247.
PDBsum; 1B0F; -.
PDBsum; 1H1B; -.
PDBsum; 1HNE; -.
PDBsum; 1PPF; -.
PDBsum; 1PPG; -.
PDBsum; 2RG3; -.
PDBsum; 2Z7F; -.
PDBsum; 3Q76; -.
PDBsum; 3Q77; -.
PDBsum; 4NZL; -.
PDBsum; 4WVP; -.
PDBsum; 5A09; -.
PDBsum; 5A0A; -.
PDBsum; 5A0B; -.
PDBsum; 5A0C; -.
PDBsum; 5A8X; -.
PDBsum; 5A8Y; -.
PDBsum; 5A8Z; -.
PDBsum; 5ABW; -.
ProteinModelPortal; P08246; -.
SMR; P08246; -.
BioGrid; 108306; 12.
CORUM; P08246; -.
IntAct; P08246; 5.
MINT; MINT-1505052; -.
STRING; 9606.ENSP00000263621; -.
BindingDB; P08246; -.
ChEMBL; CHEMBL248; -.
DrugBank; DB00058; Alpha-1-proteinase inhibitor.
DrugBank; DB05161; Elafin.
DrugBank; DB00099; Filgrastim.
DrugBank; DB03925; ONO-6818.
DrugBank; DB00019; Pegfilgrastim.
GuidetoPHARMACOLOGY; 2358; -.
MEROPS; S01.131; -.
iPTMnet; P08246; -.
PhosphoSitePlus; P08246; -.
BioMuta; ELANE; -.
DMDM; 119292; -.
PaxDb; P08246; -.
PeptideAtlas; P08246; -.
PRIDE; P08246; -.
Ensembl; ENST00000263621; ENSP00000263621; ENSG00000197561.
Ensembl; ENST00000590230; ENSP00000466090; ENSG00000197561.
Ensembl; ENST00000615489; ENSP00000480128; ENSG00000277571.
Ensembl; ENST00000632488; ENSP00000488075; ENSG00000277571.
GeneID; 1991; -.
KEGG; hsa:1991; -.
UCSC; uc002lqb.4; human.
CTD; 1991; -.
DisGeNET; 1991; -.
EuPathDB; HostDB:ENSG00000197561.6; -.
GeneCards; ELANE; -.
GeneReviews; ELANE; -.
HGNC; HGNC:3309; ELANE.
HPA; CAB015409; -.
HPA; HPA066836; -.
MalaCards; ELANE; -.
MIM; 130130; gene.
MIM; 162800; phenotype.
MIM; 202700; phenotype.
neXtProt; NX_P08246; -.
OpenTargets; ENSG00000197561; -.
Orphanet; 486; Autosomal dominant severe congenital neutropenia.
Orphanet; 2686; Cyclic neutropenia.
PharmGKB; PA27735; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00900000140962; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; P08246; -.
KO; K01327; -.
OMA; NWINSII; -.
OrthoDB; EOG091G0DF7; -.
PhylomeDB; P08246; -.
BRENDA; 3.4.21.37; 2681.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-6803157; Antimicrobial peptides.
Reactome; R-HSA-977606; Regulation of Complement cascade.
SABIO-RK; P08246; -.
SIGNOR; P08246; -.
EvolutionaryTrace; P08246; -.
GeneWiki; Neutrophil_elastase; -.
GenomeRNAi; 1991; -.
PRO; PR:P08246; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000197561; -.
CleanEx; HS_ELA2; -.
Genevisible; P08246; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0030141; C:secretory granule; IDA:MGI.
GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
GO; GO:0017053; C:transcriptional repressor complex; IDA:UniProtKB.
GO; GO:0019955; F:cytokine binding; IPI:UniProtKB.
GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
GO; GO:0008201; F:heparin binding; IDA:MGI.
GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
GO; GO:0001106; F:RNA polymerase II transcription corepressor activity; IMP:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; IBA:GO_Central.
GO; GO:0019730; P:antimicrobial humoral response; TAS:Reactome.
GO; GO:0002812; P:biosynthetic process of antibacterial peptides active against Gram-negative bacteria; IDA:UniProtKB.
GO; GO:0006874; P:cellular calcium ion homeostasis; NAS:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IEA:Ensembl.
GO; GO:0045079; P:negative regulation of chemokine biosynthetic process; IDA:UniProtKB.
GO; GO:0050922; P:negative regulation of chemotaxis; NAS:UniProtKB.
GO; GO:0044130; P:negative regulation of growth of symbiont in host; IEA:Ensembl.
GO; GO:0050728; P:negative regulation of inflammatory response; NAS:UniProtKB.
GO; GO:0045415; P:negative regulation of interleukin-8 biosynthetic process; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0070947; P:neutrophil mediated killing of fungus; IEA:Ensembl.
GO; GO:0070945; P:neutrophil mediated killing of gram-negative bacterium; IDA:UniProtKB.
GO; GO:0006909; P:phagocytosis; IBA:GO_Central.
GO; GO:0050778; P:positive regulation of immune response; IEA:Ensembl.
GO; GO:0045416; P:positive regulation of interleukin-8 biosynthetic process; IDA:UniProtKB.
GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; IEA:Ensembl.
GO; GO:0043406; P:positive regulation of MAP kinase activity; NAS:UniProtKB.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:UniProtKB.
GO; GO:0030163; P:protein catabolic process; NAS:UniProtKB.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0009411; P:response to UV; IDA:UniProtKB.
GO; GO:0001878; P:response to yeast; IEA:Ensembl.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Glycoprotein; Hydrolase;
Polymorphism; Protease; Reference proteome; Serine protease; Signal;
Zymogen.
SIGNAL 1 27 {ECO:0000255}.
PROPEP 28 29 {ECO:0000269|PubMed:2501794,
ECO:0000269|PubMed:3550808,
ECO:0000269|PubMed:7897245}.
/FTId=PRO_0000027703.
CHAIN 30 267 Neutrophil elastase.
/FTId=PRO_0000027704.
DOMAIN 30 247 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 70 70 Charge relay system.
ACT_SITE 117 117 Charge relay system.
ACT_SITE 202 202 Charge relay system.
CARBOHYD 88 88 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 124 124 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:3550808}.
CARBOHYD 173 173 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:3550808}.
DISULFID 55 71 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:3550808}.
DISULFID 151 208 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:3550808}.
DISULFID 181 187 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:3550808}.
DISULFID 198 223 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:3550808}.
VARIANT 25 25 A -> V (in SCN1).
{ECO:0000269|PubMed:20220065,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_064512.
VARIANT 42 42 P -> L (in SCN1).
{ECO:0000269|PubMed:14962902,
ECO:0000269|PubMed:19415009,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_070696.
VARIANT 43 43 F -> L (in SCN1 and CH).
{ECO:0000269|PubMed:14962902,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_070697.
VARIANT 44 44 M -> R (in SCN1).
{ECO:0000269|PubMed:19036076}.
/FTId=VAR_070698.
VARIANT 45 45 V -> E (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070699.
VARIANT 45 45 V -> L (in CH).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070700.
VARIANT 46 46 S -> C (in SCN1).
{ECO:0000269|PubMed:19036076}.
/FTId=VAR_070701.
VARIANT 46 46 S -> F (in CH and SCN1).
{ECO:0000269|PubMed:14962902,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_070702.
VARIANT 47 47 L -> P (in SCN1; dbSNP:rs878855319).
{ECO:0000269|PubMed:14962902}.
/FTId=VAR_070703.
VARIANT 47 47 L -> R (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070704.
VARIANT 49 49 L -> P (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070705.
VARIANT 53 53 H -> L (in SCN1).
{ECO:0000269|PubMed:14962902}.
/FTId=VAR_070706.
VARIANT 53 53 H -> Q (in CH).
/FTId=VAR_070707.
VARIANT 53 53 H -> Y (in SCN1).
{ECO:0000269|PubMed:19036076}.
/FTId=VAR_070708.
VARIANT 55 55 C -> S (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070709.
VARIANT 55 55 C -> Y (in SCN1).
{ECO:0000269|PubMed:11675333}.
/FTId=VAR_038609.
VARIANT 56 56 G -> R (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070710.
VARIANT 57 57 A -> S (in SCN1).
{ECO:0000269|PubMed:20803142,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_070711.
VARIANT 57 57 A -> T (in SCN1).
{ECO:0000269|PubMed:11001877,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_038610.
VARIANT 57 57 A -> V (in SCN1).
{ECO:0000269|PubMed:18946670,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_070712.
VARIANT 59 59 L -> P (in SCN1).
{ECO:0000269|PubMed:19927291,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_070713.
VARIANT 60 61 IA -> R. {ECO:0000269|PubMed:23463630}.
/FTId=VAR_070714.
VARIANT 60 60 I -> T (in SCN1).
{ECO:0000269|PubMed:11001877,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_038611.
VARIANT 61 61 A -> V (in SCN1 and CH;
dbSNP:rs137854447).
{ECO:0000269|PubMed:10581030,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_070715.
VARIANT 65 65 Missing (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070716.
VARIANT 66 70 Missing (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070717.
VARIANT 67 67 S -> W (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070718.
VARIANT 71 71 C -> F (in SCN1; dbSNP:rs878855315).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070719.
VARIANT 71 71 C -> R (in SCN1; dbSNP:rs28931611).
{ECO:0000269|PubMed:12091371,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_038612.
VARIANT 71 71 C -> S (in SCN1).
{ECO:0000269|PubMed:11001877}.
/FTId=VAR_038613.
VARIANT 71 71 C -> Y (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070720.
VARIANT 72 72 V -> G (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070721.
VARIANT 80 80 V -> G (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070722.
VARIANT 81 81 R -> P (in SCN1 and CH).
{ECO:0000269|PubMed:14962902,
ECO:0000269|PubMed:19415009,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_070723.
VARIANT 82 82 V -> M (in SCN1 and CH).
{ECO:0000269|PubMed:14962902,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_070724.
VARIANT 84 84 L -> P (in SCN1).
{ECO:0000269|PubMed:14962902,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_070725.
VARIANT 85 85 G -> E (in SCN1).
{ECO:0000269|PubMed:11675333,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_038614.
VARIANT 85 85 G -> R (in SCN1).
{ECO:0000269|PubMed:19036076}.
/FTId=VAR_070726.
VARIANT 97 97 Q -> L (in CH).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070727.
VARIANT 98 98 V -> L (in SCN1; located on the same
allele as L-101; reduces proteolytic
enzyme activity by slightly less than
half; together with L-101 shows an
additive effect with minimal remaining
enzyme activity; dbSNP:rs267606781).
{ECO:0000269|PubMed:17436313,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_038615.
VARIANT 98 98 V -> M (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070728.
VARIANT 101 101 V -> L (in SCN1; located on the same
allele as L-98; reduces proteolytic
enzyme activity by slightly less than
half; together with L-98 shows an
additive effect with minimal remaining
enzyme activity; dbSNP:rs137854449).
{ECO:0000269|PubMed:17436313,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_038616.
VARIANT 101 101 V -> M (in SCN1; dbSNP:rs28929494).
{ECO:0000269|PubMed:11001877,
ECO:0000269|PubMed:19415009,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_038617.
VARIANT 103 103 R -> L (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070729.
VARIANT 103 103 R -> P (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070730.
VARIANT 104 104 I -> N (in CH).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070731.
VARIANT 118 118 I -> V. {ECO:0000269|PubMed:23463630}.
/FTId=VAR_070732.
VARIANT 120 120 I -> F (in SCN1 and CH).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070733.
VARIANT 120 120 I -> N (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070734.
VARIANT 120 120 I -> S (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070735.
VARIANT 121 121 L -> P (in SCN1).
{ECO:0000269|PubMed:14962902,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_070736.
VARIANT 123 123 L -> H (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070737.
VARIANT 123 123 L -> PQL (in SCN1).
/FTId=VAR_038618.
VARIANT 124 124 N -> I (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070738.
VARIANT 125 125 G -> R (in dbSNP:rs377698556).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070739.
VARIANT 126 126 S -> L (in SCN1 and CH;
dbSNP:rs137854450).
{ECO:0000269|PubMed:11001877,
ECO:0000269|PubMed:11675333,
ECO:0000269|PubMed:14962902,
ECO:0000269|PubMed:19415009,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_038619.
VARIANT 127 127 A -> D (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070740.
VARIANT 127 127 A -> P (in SCN1).
{ECO:0000269|PubMed:14962902}.
/FTId=VAR_070741.
VARIANT 131 131 A -> T (in SCN1; unknown pathological
significance; dbSNP:rs201729066).
{ECO:0000269|PubMed:21425445,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_070742.
VARIANT 135 135 V -> M (in dbSNP:rs774457980).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070743.
VARIANT 136 136 A -> D (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070744.
VARIANT 139 139 P -> L (in SCN1 and CH;
dbSNP:rs28929493).
{ECO:0000269|PubMed:11001877,
ECO:0000269|PubMed:14962902,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_038620.
VARIANT 139 139 P -> R (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070745.
VARIANT 143 143 R -> H (in CH; unknown pathological
significance; dbSNP:rs200993994).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070746.
VARIANT 151 151 C -> F (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070747.
VARIANT 151 151 C -> S (in SCN1).
{ECO:0000269|PubMed:11675333}.
/FTId=VAR_038621.
VARIANT 151 151 C -> W (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070748.
VARIANT 151 151 C -> Y (in SCN1; unknown pathological
significance; dbSNP:rs57246956).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070749.
VARIANT 152 152 L -> P (in SCN1).
{ECO:0000269|PubMed:14962902,
ECO:0000269|PubMed:21425445,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_070750.
VARIANT 153 153 A -> D (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070751.
VARIANT 153 153 A -> P (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070752.
VARIANT 156 156 W -> C (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070753.
VARIANT 156 156 W -> R (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070754.
VARIANT 166 166 A -> T (in SCN1; the patient also carries
mutation Lys-116 in G6PC3;
dbSNP:rs201788817).
{ECO:0000269|PubMed:20220065,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_064513.
VARIANT 190 199 Missing (in SCN1 and CH).
{ECO:0000269|PubMed:11675333}.
/FTId=VAR_038622.
VARIANT 203 203 G -> C (in SCN1 and CH).
{ECO:0000269|PubMed:19036076,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_070755.
VARIANT 203 203 G -> R (in SCN1).
{ECO:0000269|PubMed:19036076,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_070756.
VARIANT 205 205 P -> R (in SCN1).
{ECO:0000269|PubMed:11675333,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_038623.
VARIANT 206 206 L -> F (in CH; dbSNP:rs137854446).
{ECO:0000269|PubMed:10581030}.
/FTId=VAR_070757.
VARIANT 206 206 L -> S (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070758.
VARIANT 208 208 C -> G (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070759.
VARIANT 209 209 N -> I (in CH).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070760.
VARIANT 210 210 G -> V (in SCN1).
{ECO:0000269|PubMed:11001877}.
/FTId=VAR_038624.
VARIANT 210 210 G -> W (in CH).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070761.
VARIANT 214 214 G -> E (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070762.
VARIANT 214 214 G -> R (in SCN1; dbSNP:rs137854451).
{ECO:0000269|PubMed:11001877,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_038625.
VARIANT 219 219 V -> I (in CH and SCN1; unknown
pathological significance;
dbSNP:rs17216656).
{ECO:0000269|PubMed:14962902,
ECO:0000269|PubMed:23463630,
ECO:0000269|Ref.5}.
/FTId=VAR_019237.
VARIANT 220 220 R -> Q (in CH and SCN1; loss of
interaction with NOTCH2NL and loss of
NOTCH2NL and NOTCH2 proteolytic cleavage;
dbSNP:rs137854445).
{ECO:0000269|PubMed:10581030,
ECO:0000269|PubMed:14673143,
ECO:0000269|PubMed:14962902,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_070763.
VARIANT 233 233 A -> P (in SCN1).
{ECO:0000269|PubMed:23463630}.
/FTId=VAR_070764.
VARIANT 235 235 V -> E (in SCN1).
{ECO:0000269|PubMed:19927291,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_070765.
VARIANT 235 235 V -> G (in SCN1).
{ECO:0000269|PubMed:21425445,
ECO:0000269|PubMed:23463630}.
/FTId=VAR_070766.
VARIANT 257 257 P -> L (in dbSNP:rs17216663).
{ECO:0000269|PubMed:23463630,
ECO:0000269|Ref.5}.
/FTId=VAR_019238.
VARIANT 262 262 P -> L (found in patients with severe
congenital or cyclic neutropenia;
dbSNP:rs17216670).
{ECO:0000269|PubMed:14962902,
ECO:0000269|Ref.5}.
/FTId=VAR_019239.
STRAND 44 49 {ECO:0000244|PDB:5ABW}.
STRAND 52 61 {ECO:0000244|PDB:5ABW}.
STRAND 64 67 {ECO:0000244|PDB:5ABW}.
HELIX 69 72 {ECO:0000244|PDB:5ABW}.
HELIX 77 79 {ECO:0000244|PDB:5ABW}.
STRAND 81 85 {ECO:0000244|PDB:5ABW}.
STRAND 97 106 {ECO:0000244|PDB:5ABW}.
TURN 111 114 {ECO:0000244|PDB:5ABW}.
STRAND 119 125 {ECO:0000244|PDB:5ABW}.
STRAND 130 132 {ECO:0000244|PDB:2Z7F}.
STRAND 150 158 {ECO:0000244|PDB:5ABW}.
STRAND 161 163 {ECO:0000244|PDB:4WVP}.
STRAND 170 177 {ECO:0000244|PDB:5ABW}.
STRAND 185 189 {ECO:0000244|PDB:5ABW}.
STRAND 191 193 {ECO:0000244|PDB:5ABW}.
STRAND 205 208 {ECO:0000244|PDB:5ABW}.
STRAND 211 218 {ECO:0000244|PDB:5ABW}.
STRAND 220 222 {ECO:0000244|PDB:5ABW}.
STRAND 226 228 {ECO:0000244|PDB:5ABW}.
STRAND 230 234 {ECO:0000244|PDB:5ABW}.
HELIX 235 238 {ECO:0000244|PDB:5ABW}.
HELIX 239 246 {ECO:0000244|PDB:5ABW}.
SEQUENCE 267 AA; 28518 MW; 3F7610DC33CAA4B9 CRC64;
MTLGRRLACL FLACVLPALL LGGTALASEI VGGRRARPHA WPFMVSLQLR GGHFCGATLI
APNFVMSAAH CVANVNVRAV RVVLGAHNLS RREPTRQVFA VQRIFENGYD PVNLLNDIVI
LQLNGSATIN ANVQVAQLPA QGRRLGNGVQ CLAMGWGLLG RNRGIASVLQ ELNVTVVTSL
CRRSNVCTLV RGRQAGVCFG DSGSPLVCNG LIHGIASFVR GGCASGLYPD AFAPVAQFVN
WIDSIIQRSE DNPCPHPRDP DPASRTH


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Catalog number Product name Quantity
20-272-191518 Elastase 2. prediluted - Mouse monoclonal [SPM205] to Elastase 2. prediluted; EC 3.4.21.37; Elastase-2; Neutrophil elastase; PMN elastase; Bone marrow serine protease; Medullasin; Human leukocyte elas 7 ml
E0181h ELISA kit Bone marrow serine protease,ELA2,ELANE,Elastase-2,HLE,Homo sapiens,Human,Human leukocyte elastase,Medullasin,Neutrophil elastase,PMN elastase 96T
E0181h ELISA Bone marrow serine protease,ELA2,ELANE,Elastase-2,HLE,Homo sapiens,Human,Human leukocyte elastase,Medullasin,Neutrophil elastase,PMN elastase 96T
U0181h CLIA Bone marrow serine protease,ELA2,ELANE,Elastase-2,HLE,Homo sapiens,Human,Human leukocyte elastase,Medullasin,Neutrophil elastase,PMN elastase 96T
E0181m ELISA kit Ela2,Elane,Elastase-2,Leukocyte elastase,Mouse,Mus musculus,Neutrophil elastase 96T
E0181m ELISA Ela2,Elane,Elastase-2,Leukocyte elastase,Mouse,Mus musculus,Neutrophil elastase 96T
U0181m CLIA Ela2,Elane,Elastase-2,Leukocyte elastase,Mouse,Mus musculus,Neutrophil elastase 96T
EIAAB06729 CELA3B,Chymotrypsin-like elastase family member 3B,ELA3B,Elastase IIIB,Elastase-3B,Homo sapiens,Human,Protease E
EIAAB06728 CELA3A,Chymotrypsin-like elastase family member 3A,ELA3,ELA3A,Elastase IIIA,Elastase-3A,Homo sapiens,Human,Protease E
EIAAB06723 Bos taurus,Bovine,CELA2A,Chymotrypsin-like elastase family member 2A,ELA2,ELA2A,Elastase II,Elastase-2,Elastase-2A
E1483b ELISA Bos taurus,Bovine,CELA1,Chymotrypsin-like elastase family member 1,ELA1,Elastase I,Elastase-1 96T
EIAAB06724 Cela2a,Chymotrypsin-like elastase family member 2A,Ela2,Ela-2,Ela2a,Elastase-2,Elastase-2A,Mouse,Mus musculus
EIAAB06726 Cela2a,Chymotrypsin-like elastase family member 2A,Ela2,Ela2a,Elastase-2,Elastase-2A,Rat,Rattus norvegicus
E1483b ELISA kit Bos taurus,Bovine,CELA1,Chymotrypsin-like elastase family member 1,ELA1,Elastase I,Elastase-1 96T
U1483b CLIA Bos taurus,Bovine,CELA1,Chymotrypsin-like elastase family member 1,ELA1,Elastase I,Elastase-1 96T
EIAAB06722 CELA2A,Chymotrypsin-like elastase family member 2A,ELA2,ELA2A,Elastase-2,Elastase-2A,Pig,Sus scrofa
HNE-L ELASTASE Human Neutrophil Elastase, Lyophilized 1.0 mg
HNE-L ELASTASE Human Neutrophil Elastase, Lyophilized 0.5 mg
HNE ELASTASE Human Neutrophil Elastase 1.0 mg
HNE ELASTASE Human Neutrophil Elastase 0.5 mg
orb90360 Human Neutrophil Elastase enzyme Elastase is a purified enzyme. For research use only. 100
4050-0184 NATIVE HUMAN ELASTASE (NEUTROPHIL), Product Type Purified Protein, Specificity ELASTASE, Target Species Human, Host N_A, Format Purified, Isotypes , Applications E, Clone 0.1 mg
SCH-4050-0184 NATIVE HUMAN ELASTASE (NEUTROPHIL), Product Type Purified Protein, Specificity ELASTASE, Target Species Human, Host N_A, Format Purified, Isotypes , Applications E, Clone 0.1 mg
20-321-175215 LEUKOCYTE ELASTASE - MONOCLONAL ANTIBODY TO HUMAN LEUKOCYTE ELASTASE Monoclonal 0.1 mg
EIAAB06727 CELA2B,Chymotrypsin-like elastase family member 2B,ELA2B,Elastase-2B,Homo sapiens,Human


 

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