ABHD12
entrez
26090
canonical
uniprot
Q8N2K0
canonical
ensembl
ENSG00000100997
resolver
ensp
ENSP00000341408
resolver
ensp
ENSP00000365725
resolver
ensp
ENSP00000459121
resolver
ensp
ENSP00000500106
resolver
ensp
ENSP00000639705
resolver
ensp
ENSP00000727261
resolver
enst
ENST00000672566
resolver
genesymbol
ABHD12
resolver
genesymbol_syn
C20orf22
resolver
hgnc
HGNC:15868
resolver
uniprot
A0A5F9ZH71
resolver
uniprot
A6NED4
resolver
uniprot
A6NJ90
resolver
uniprot
A8K450
resolver
uniprot
B4DE71
resolver
uniprot
Q5T710
resolver
uniprot
Q5T711
resolver
uniprot
Q96CR1
resolver
uniprot
Q9BX05
resolver
uniprot
Q9NPX7
resolver
uniprot
Q9UFV6
resolver
uniprot_entry
A0A5F9ZH71_HUMAN
resolver
uniprot_entry
ABD12_HUMAN
resolver
uniprot_sec
A6NED4
resolver
uniprot_sec
A6NJ90
resolver
uniprot_sec
A8K450
resolver
uniprot_sec
B4DE71
resolver
uniprot_sec
Q5T710
resolver
uniprot_sec
Q5T711
resolver
uniprot_sec
Q96CR1
resolver
uniprot_sec
Q9BX05
resolver
uniprot_sec
Q9NPX7
resolver
uniprot_sec
Q9UFV6
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) (PubMed:30420694, PubMed:30720278). Reversibly inhibited by triterpenoids, but with rather low potency (PubMed:24879289). {ECO:0000269|PubMed:24879289, ECO:0000269|PubMed:30420694, ECO:0000269|PubMed:30720278}.
uniprot
proteins
amino_acid_sequence
MRKRTEPVALEHERCAAAGSSSSGSAAAALDADCRLKQNLRLTGPAAAEPRCAADAGMKRALGRRKGVWLRLRKILFCVLGLYIAIPFLIKLCPGIQAKLIFLNFVRVPYFIDLKKPQDQGLNHTCNYYLQPEEDVTIGVWHTVPAVWWKNAQGKDQMWYEDALASSHPIILYLHGNAGTRGGDHRVELYKVLSSLGYHVVTFDYRGWGDSVGTPSERGMTYDALHVFDWIKARSGDNPVYIWGHSLGTGVATNLVRRLCERETPPDALILESPFTNIREEAKSHPFSVIYRYFPGFDWFFLDPITSSGIKFANDENVKHISCPLLILHAEDDPVVPFQLGRKLYSIAAPARSFRDFKVQFVPFHSDLGYRHKYIYKSPELPRILREFLGKSEPEHQH
uniprot
proteins
disease_involvement
DISEASE: Polyneuropathy, hearing loss, ataxia, retinitis pigmentosa, and cataract (PHARC) [MIM:612674]: A slowly progressive neurologic disorder with a variable phenotype resembling Refsum disease. Clinical features include sensorineural hearing loss, visual problems related to cataracts, retinitis pigmentosa, pes cavus, ataxic and/or spastic gait disturbances with a progressive sensorimotor peripheral neuropathy. Other features include hyporeflexia, hyperreflexia, extensor plantar responses. {ECO:0000269|PubMed:20797687, ECO:0000269|PubMed:22938382, ECO:0000269|PubMed:24027063, ECO:0000269|PubMed:24697911, ECO:0000269|PubMed:25743180, ECO:0000269|PubMed:27890673, ECO:0000269|PubMed:29571850}. Note=The disease is caused by variants affecting the gene represented in this entry.
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:25290914, PubMed:30237167, PubMed:30420694, PubMed:30643283, PubMed:30720278, PubMed:33571455). Represents a major lysophosphatidylserine lipase in the brain, thereby playing a key role in the central nervous system (By similarity). 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:22969151, PubMed:24027063). 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:0000250|UniProtKB:Q99LR1, ECO:0000269|PubMed:22969151, ECO:0000269|PubMed:24027063, ECO:0000269|PubMed:25290914, ECO:0000269|PubMed:30237167, ECO:0000269|PubMed:30420694, ECO:0000269|PubMed:30643283, ECO:0000269|PubMed:30720278, ECO:0000269|PubMed:33571455}.
uniprot
proteins
mass_dalton
45097
uniprot
proteins
mutagenesis
MUTAGEN 246; /note="S->A: Loss of lipase activity."; /evidence="ECO:0000269|PubMed:22969151, ECO:0000269|PubMed:30237167, ECO:0000269|PubMed:30643283"; MUTAGEN 333; /note="D->N: Loss of 2-arachidonoyglycerol hydrolase activity."; /evidence="ECO:0000269|PubMed:22969151"; MUTAGEN 372; /note="H->A: Loss of 2-arachidonoyglycerol hydrolase activity."; /evidence="ECO:0000269|PubMed:22969151
uniprot
proteins
post_translational_modification
PTM: Glycosylated; glycosylation is required for optimal activity. {ECO:0000269|PubMed:30237167}.
uniprot
proteins
protein_family
Serine esterase family
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
20797687
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22938382
uniprot
proteins
pubmed
22969151
uniprot
proteins
pubmed
24027063
uniprot
proteins
pubmed
24697911
uniprot
proteins
pubmed
24879289
uniprot
proteins
pubmed
25290914
uniprot
proteins
pubmed
25743180
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27890673
uniprot
proteins
pubmed
29571850
uniprot
proteins
pubmed
30237167
uniprot
proteins
pubmed
30420694
uniprot
proteins
pubmed
30643283
uniprot
proteins
pubmed
30720278
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}.
uniprot
proteins
transmembrane_region
TRANSMEM 75..95; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q99LR1
uniprot
proteins