Abhd12
entrez
76192
canonical
uniprot
Q99LR1
canonical
ensembl
ENSMUSG00000032046
resolver
ensp
ENSMUSP00000053558
resolver
genesymbol
Abhd12
resolver
uniprot
A2ANB4
resolver
uniprot
Q99M06
resolver
uniprot_entry
ABD12_MOUSE
resolver
uniprot_sec
A2ANB4
resolver
uniprot_sec
Q99M06
resolver
activity_regulation
ACTIVITY REGULATION: Selectively inhibited by DO264 (N-3-pyridyl-N'-(1-[3-chloro-4-{2-chloro-4-(trifluoromethoxy)phenoxy}pyridine-2-yl]piperidin-4-yl)thiourea). {ECO:0000269|PubMed:30420694}.
uniprot
proteins
amino_acid_sequence
MRKRTEPVTLEHERCAASGSSSSGSAAAALDADCSLKQNLRLAGKGTAEPHSASDAGMKRALGRRKSLWFRLRKILLCVLGFYIAIPFLVKLCPGIQAKLIFLNFVRVPYFIDLKKPQDQGLNHTCNYYLQPEDDVTIGVWHTIPSVWWKNAQGKDQMWYEDALASNHAIILYLHGNAGTRGGDHRVELYKVLSSLGYHVVTFDYRGWGDSVGTPSERGMTYDALHVFDWIKARSGDNPVYIWGHSLGTGVATNLVRRLCERETPPDALILESPFTNIREEAKSHPFSVIYRYFPGFDWFFLDPITSSGIKFANDENMKHISCPLLILHAEDDPVVPFHLGRKLYNIAAPSRSFRDFKVQFIPFHSDLGYRHKYIYKSPELPRILREFLGKSEPERQH
uniprot
proteins
ec_number
3.1.-.-
uniprot
proteins
ec_number
3.1.1.-
uniprot
proteins
ec_number
3.1.1.23
uniprot
proteins
function
FUNCTION: Lysophosphatidylserine (LPS) lipase that mediates the hydrolysis of lysophosphatidylserine, a class of signaling lipids that regulates immunological and neurological processes (PubMed:23297193, PubMed:25580854, PubMed:30420694, PubMed:33571455). Represents a major lysophosphatidylserine lipase in the brain, thereby playing a key role in the central nervous system (PubMed:23297193). Prefers as substrates lysophosphatidylserines having long and very long chain acyl chains (PubMed:33571455). Also able to hydrolyze oxidized phosphatidylserine; oxidized phosphatidylserine is produced in response to severe inflammatory stress and constitutes a proapoptotic 'eat me' signal (PubMed:30643283). Also has monoacylglycerol (MAG) lipase activity: hydrolyzes 2-arachidonoylglycerol (2-AG), thereby acting as a regulator of endocannabinoid signaling pathways (PubMed:18096503). Has a strong preference for very-long-chain lipid substrates; substrate specificity is likely due to improved catalysis and not improved substrate binding (PubMed:30237167). {ECO:0000269|PubMed:18096503, ECO:0000269|PubMed:23297193, ECO:0000269|PubMed:25580854, ECO:0000269|PubMed:30237167, ECO:0000269|PubMed:30420694, ECO:0000269|PubMed:30643283, ECO:0000269|PubMed:33571455}.
uniprot
proteins
mass_dalton
45270
uniprot
proteins
post_translational_modification
PTM: Glycosylated. {ECO:0000269|PubMed:18096503}.
uniprot
proteins
protein_family
Serine esterase family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18096503
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20657592
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23297193
uniprot
proteins
pubmed
25580854
uniprot
proteins
pubmed
30237167
uniprot
proteins
pubmed
30420694
uniprot
proteins
pubmed
30643283
uniprot
proteins
pubmed
33571455
uniprot
proteins
sequence_length
398
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30237167}; Single-pass membrane protein {ECO:0000255}. Mitochondrion {ECO:0000269|PubMed:20657592}.
uniprot
proteins
transmembrane_region
TRANSMEM 75..95; /note="Helical"; /evidence="ECO:0000269|PubMed:18096503
uniprot
proteins