ELANE
entrez
1991
canonical
uniprot
P08246
canonical
ensembl
ENSG00000197561
resolver
ensembl
ENSG00000277571
resolver
ensp
ENSP00000263621
resolver
ensp
ENSP00000466090
resolver
ensp
ENSP00000480128
resolver
ensp
ENSP00000488075
resolver
enst
ENST00000263621
resolver
enst
ENST00000590230
resolver
enst
ENST00000615489
resolver
enst
ENST00000632488
resolver
genesymbol
ELANE
resolver
genesymbol_syn
ELA2
resolver
hgnc
HGNC:3309
resolver
uniprot
P09649
resolver
uniprot
Q6B0D9
resolver
uniprot
Q6LDP5
resolver
uniprot_entry
ELNE_HUMAN
resolver
uniprot_sec
P09649
resolver
uniprot_sec
Q6B0D9
resolver
uniprot_sec
Q6LDP5
resolver
amino_acid_sequence
MTLGRRLACLFLACVLPALLLGGTALASEIVGGRRARPHAWPFMVSLQLRGGHFCGATLIAPNFVMSAAHCVANVNVRAVRVVLGAHNLSRREPTRQVFAVQRIFENGYDPVNLLNDIVILQLNGSATINANVQVAQLPAQGRRLGNGVQCLAMGWGLLGRNRGIASVLQELNVTVVTSLCRRSNVCTLVRGRQAGVCFGDSGSPLVCNGLIHGIASFVRGGCASGLYPDAFAPVAQFVNWIDSIIQRSEDNPCPHPRDPDPASRTH
uniprot
proteins
disease_involvement
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 variants 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 variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.21.37
uniprot
proteins
function
FUNCTION: Serine protease that modifies the functions of natural killer cells, monocytes and granulocytes (PubMed:15140022). Shows microbicidal activity in neutrophils by mediating cleavage and degradation of bacterial proteins (PubMed:10947984, PubMed:25161283). Capable of killing E.coli but not S.aureus in vitro; digests outer membrane protein A (ompA) in E.coli and K.pneumoniae (PubMed:10947984). Involved for the formation of neutrophil extracellular traps (NETs): translocates into the nucleus downstream of MPO and mediates degadation of histone H4, thereby participating to chromatin decondensation (PubMed:20974816, PubMed:25066128, PubMed:28574339). NETs are mainly composed of DNA fibers and are released by neutrophils to trap pathogens during inflammation (PubMed:20974816, PubMed:25066128, PubMed:28574339). Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (PubMed:15140022). Promotes cleavage of GSDMB, thereby inhibiting pyroptosis (PubMed:36899106). Promotes blood coagulation (PubMed:20676107). Through the activation of the platelet fibrinogen receptor integrin alpha-IIb/beta-3, potentiates platelet aggregation induced by a threshold concentration of cathepsin G (CTSG) (PubMed:25211214, PubMed:9111081). Cleaves and thus inactivates tissue factor pathway inhibitor (TFPI) (PubMed:20676107, PubMed:25211214). {ECO:0000269|PubMed:10947984, ECO:0000269|PubMed:15140022, ECO:0000269|PubMed:20676107, ECO:0000269|PubMed:20974816, ECO:0000269|PubMed:25066128, ECO:0000269|PubMed:25161283, ECO:0000269|PubMed:25211214, ECO:0000269|PubMed:28574339, ECO:0000269|PubMed:36899106, ECO:0000269|PubMed:9111081}.; FUNCTION: (Microbial infection) Inhibited reversibly by S.aureus serine protease inhibitors Eap, EapH1 and EapH2, impairing microbicidal activity in neutrophils. {ECO:0000269|PubMed:25161283, ECO:0000269|PubMed:36736422, ECO:0000269|PubMed:37269950, ECO:0000269|PubMed:39098536}.
uniprot
proteins
mass_dalton
28518
uniprot
proteins
protein_family
Elastase subfamily
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
pubmed
10581030
uniprot
proteins
pubmed
10947984
uniprot
proteins
pubmed
11001877
uniprot
proteins
pubmed
11675333
uniprot
proteins
pubmed
12091371
uniprot
proteins
pubmed
14673143
uniprot
proteins
pubmed
14962902
uniprot
proteins
pubmed
15140022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17436313
uniprot
proteins
pubmed
1859409
uniprot
proteins
pubmed
18946670
uniprot
proteins
pubmed
19036076
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19415009
uniprot
proteins
pubmed
19927291
uniprot
proteins
pubmed
20220065
uniprot
proteins
pubmed
20676107
uniprot
proteins
pubmed
20803142
uniprot
proteins
pubmed
20974816
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21425445
uniprot
proteins
pubmed
2322278
uniprot
proteins
pubmed
23463630
uniprot
proteins
pubmed
2462434
uniprot
proteins
pubmed
2501794
uniprot
proteins
pubmed
25066128
uniprot
proteins
pubmed
25161283
uniprot
proteins
pubmed
25211214
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26274980
uniprot
proteins
pubmed
2775493
uniprot
proteins
pubmed
2822677
uniprot
proteins
pubmed
28574339
uniprot
proteins
pubmed
2902087
uniprot
proteins
pubmed
2911584
uniprot
proteins
pubmed
32434865
uniprot
proteins
pubmed
3391280
uniprot
proteins
pubmed
3422232
uniprot
proteins
pubmed
3479752
uniprot
proteins
pubmed
3550808
uniprot
proteins
pubmed
3640709
uniprot
proteins
pubmed
36736422
uniprot
proteins
pubmed
36899106
uniprot
proteins
pubmed
37269950
uniprot
proteins
pubmed
39098536
uniprot
proteins
pubmed
7897245
uniprot
proteins
pubmed
9111081
uniprot
proteins
sequence_length
267
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:10947984}. Lysosome {ECO:0000269|PubMed:25066128}. Cytolytic granule {ECO:0000269|PubMed:20974816, ECO:0000269|PubMed:25066128}. Nucleus {ECO:0000269|PubMed:20974816, ECO:0000269|PubMed:25066128}. Note=Localizes to azurophil granules, a type of primary lysosome found in neutrophils and monocytes that contains antimicrobial proteins (PubMed:20974816, PubMed:25066128). Translocates from azurophil granules to the nucleus downstream of MPO during formation of neutrophil extracellular traps (NETs), and is present in released NETs (PubMed:20974816, PubMed:25066128, PubMed:32434865). Localized in phagolysosomes following ingestion of E.coli by neutrophils (PubMed:10947984). {ECO:0000269|PubMed:10947984, ECO:0000269|PubMed:20974816, ECO:0000269|PubMed:25066128, ECO:0000269|PubMed:32434865}.
uniprot
proteins