ABHD5
entrez
51099
canonical
uniprot
Q8WTS1
canonical
ensembl
ENSG00000011198
resolver
ensp
ENSP00000390849
resolver
ensp
ENSP00000412014
resolver
ensp
ENSP00000494478
resolver
ensp
ENSP00000495778
resolver
ensp
ENSP00000497701
resolver
ensp
ENSP00000637578
resolver
enst
ENST00000454293
resolver
enst
ENST00000458276
resolver
enst
ENST00000642351
resolver
enst
ENST00000644371
resolver
enst
ENST00000649763
resolver
enst
ENST00000967519
resolver
genesymbol
ABHD5
resolver
genesymbol_syn
NCIE2
resolver
hgnc
HGNC:21396
resolver
uniprot
A0A0S2Z5D6
resolver
uniprot
A0A2U3TZT9
resolver
uniprot
B2R9K0
resolver
uniprot
C9J1D1
resolver
uniprot
Q9Y369
resolver
uniprot_entry
A0A0S2Z5D6_HUMAN
resolver
uniprot_entry
A0A2U3TZT9_HUMAN
resolver
uniprot_entry
ABHD5_HUMAN
resolver
uniprot_entry
C9J1D1_HUMAN
resolver
uniprot_sec
B2R9K0
resolver
uniprot_sec
Q9Y369
resolver
activity_regulation
ACTIVITY REGULATION: Acyltransferase activity is inhibited by detergents such as Triton X-100 and 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS). Acyltransferase activity is inhibited by the presence of magnesium and calcium. {ECO:0000250|UniProtKB:Q9DBL9}.
uniprot
proteins
amino_acid_sequence
MAAEEEEVDSADTGERSGWLTGWLPTWCPTSISHLKEAEEKMLKCVPCTYKKEPVRISNGNKIWTLKFSHNISNKTPLVLLHGFGGGLGLWALNFGDLCTNRPVYAFDLLGFGRSSRPRFDSDAEEVENQFVESIEEWRCALGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEPWGFPERPDLADQDRPIPVWIRALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMFEDDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQRIGKMHPDIPVSVIFGARSCIDGNSGTSIQSLRPHSYVKTIAILGAGHYVYADQPEEFNQKVKEICDTVD
uniprot
proteins
disease_involvement
DISEASE: Chanarin-Dorfman syndrome (CDS) [MIM:275630]: An autosomal recessive inborn error of lipid metabolism with multisystemic accumulation of triglycerides although plasma concentrations are normal. Clinical characteristics are congenital generalized ichthyosis, vacuolated leukocytes, hepatomegaly, myopathy, cataracts, neurosensory hearing loss and developmental delay. The disorder presents at birth with generalized, fine, white scaling of the skin and a variable degree of erythema resembling non-bullous congenital ichthyosiform erythroderma. {ECO:0000269|PubMed:11590543, ECO:0000269|PubMed:16679289, ECO:0000269|PubMed:17495960, ECO:0000269|PubMed:18606822}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.3.1.51
uniprot
proteins
function
FUNCTION: Coenzyme A-dependent lysophosphatidic acid acyltransferase that catalyzes the transfer of an acyl group on a lysophosphatidic acid (PubMed:18606822). Functions preferentially with 1-oleoyl-lysophosphatidic acid followed by 1-palmitoyl-lysophosphatidic acid, 1-stearoyl-lysophosphatidic acid and 1-arachidonoyl-lysophosphatidic acid as lipid acceptor. Functions preferentially with arachidonoyl-CoA followed by oleoyl-CoA as acyl group donors (By similarity). Functions in phosphatidic acid biosynthesis (PubMed:18606822). May regulate the cellular storage of triacylglycerol through activation of the phospholipase PNPLA2 (PubMed:16679289). Involved in keratinocyte differentiation (PubMed:18832586). Regulates lipid droplet fusion (By similarity). {ECO:0000250|UniProtKB:Q9DBL9, ECO:0000269|PubMed:16679289, ECO:0000269|PubMed:18606822, ECO:0000269|PubMed:18832586}.
uniprot
proteins
mass_dalton
39096
uniprot
proteins
protein_family
ABHD4/ABHD5 subfamily
uniprot
proteins
protein_family
Peptidase S33 family
uniprot
proteins
pubmed
10810093
uniprot
proteins
pubmed
11590543
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15967942
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
16679289
uniprot
proteins
pubmed
17495960
uniprot
proteins
pubmed
18606822
uniprot
proteins
pubmed
18832586
uniprot
proteins
pubmed
22814378
uniprot
proteins
sequence_length
349
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18832586}. Lipid droplet {ECO:0000250|UniProtKB:Q9DBL9}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9DBL9}. Note=Colocalized with PLIN and ADRP on the surface of lipid droplets. The localization is dependent upon the metabolic status of the adipocytes and the activity of PKA (By similarity). {ECO:0000250}.
uniprot
proteins