AOAH
entrez
313
canonical
uniprot
P28039
canonical
ensembl
ENSG00000136250
resolver
ensp
ENSP00000479664
resolver
ensp
ENSP00000483783
resolver
ensp
ENSP00000484305
resolver
ensp
ENSP00000530722
resolver
ensp
ENSP00000778823
resolver
ensp
ENSP00000778824
resolver
enst
ENST00000617267
resolver
genesymbol
AOAH
resolver
hgnc
HGNC:548
resolver
uniprot
A0A087WVT3
resolver
uniprot
A4D1Y5
resolver
uniprot
B7Z490
resolver
uniprot
Q53F13
resolver
uniprot_entry
A0A087WVT3_HUMAN
resolver
uniprot_entry
AOAH_HUMAN
resolver
uniprot_sec
A4D1Y5
resolver
uniprot_sec
B7Z490
resolver
uniprot_sec
Q53F13
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:29343645}.
uniprot
proteins
amino_acid_sequence
MQSPWKILTVAPLFLLLSLQSSASPANDDQSRPSLSNGHTCVGCVLVVSVIEQLAQVHNSTVQASMERLCSYLPEKLFLKTTCYLVIDKFGSDIIKLLSADMNADVVCHTLEFCKQNTGQPLCHLYPLPKETWKFTLQKARQIVKKSPILKYSRSGSDICSLPVLAKICQKIKLAMEQSVPFKDVDSDKYSVFPTLRGYHWRGRDCNDSDESVYPGRRPNNWDVHQDSNCNGIWGVDPKDGVPYEKKFCEGSQPRGIILLGDSAGAHFHISPEWITASQMSLNSFINLPTALTNELDWPQLSGATGFLDSTVGIKEKSIYLRLWKRNHCNHRDYQNISRNGASSRNLKKFIESLSRNKVLDYPAIVIYAMIGNDVCSGKSDPVPAMTTPEKLYSNVMQTLKHLNSHLPNGSHVILYGLPDGTFLWDNLHNRYHPLGQLNKDMTYAQLYSFLNCLQVSPCHGWMSSNKTLRTLTSERAEQLSNTLKKIAASEKFTNFNLFYMDFAFHEIIQEWQKRGGQPWQLIEPVDGFHPNEVALLLLADHFWKKVQLQWPQILGKENPFNPQIKQVFGDQGGH
uniprot
proteins
ec_number
3.1.1.77
uniprot
proteins
function
FUNCTION: Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides (PubMed:1883828, PubMed:29343645, PubMed:8089145). By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflammatory responses (By similarity). In peritoneal macrophages, seems to be important for recovery from a state of immune tolerance following infection by Gram-negative bacteria (By similarity). {ECO:0000250|UniProtKB:O35298, ECO:0000269|PubMed:1883828, ECO:0000269|PubMed:29343645, ECO:0000269|PubMed:8089145}.
uniprot
proteins
mass_dalton
65105
uniprot
proteins
mutagenesis
MUTAGEN 61; /note="T->A: Loss of glycosylation. No effect on enzyme activity or localization to cytoplasmic vesicles."; /evidence="ECO:0000269|PubMed:8089145"; MUTAGEN 173; /note="K->E: No effect on enzyme activity."; /evidence="ECO:0000269|PubMed:29343645"; MUTAGEN 263; /note="S->A: Loss of enzyme activity."; /evidence="ECO:0000269|PubMed:29343645"; MUTAGEN 263; /note="S->L: Nearly abolishes catalytic activity."; /evidence="ECO:0000269|PubMed:8089145"; MUTAGEN 345; /note="R->E: No effect on enzyme activity; when associated with E-379."; /evidence="ECO:0000269|PubMed:29343645"; MUTAGEN 372; /note="G->M: Loss of enzyme activity with lipopolysaccharide, due to steric hindrance. No effect on activity with small, synthetic substrate."; /evidence="ECO:0000269|PubMed:29343645"; MUTAGEN 379; /note="K->E: No effect on enzyme activity; when associated with E-345."; /evidence="ECO:0000269|PubMed:29343645"; MUTAGEN 419; /note="P->M: Loss of enzyme activity with lipopolysaccharide, due to steric hindrance. No effect on activity with small, synthetic substrate."; /evidence="ECO:0000269|PubMed:29343645
uniprot
proteins
post_translational_modification
PTM: Cleaved into a large and a small subunit. {ECO:0000269|PubMed:1883828, ECO:0000269|PubMed:29343645, ECO:0000269|PubMed:8089145}.; PTM: The small subunit is N-glycosylated. {ECO:0000269|PubMed:8089145}.
uniprot
proteins
pubmed
12690205
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1883828
uniprot
proteins
pubmed
29343645
uniprot
proteins
pubmed
8089145
uniprot
proteins
sequence_length
575
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8089145, ECO:0000305|PubMed:1883828}. Cytoplasmic vesicle {ECO:0000269|PubMed:8089145}. Note=Detected in urine. {ECO:0000250|UniProtKB:O35298}.
uniprot
proteins