Abhd17b
entrez
226016
canonical
uniprot
Q7M759
canonical
ensembl
ENSMUSG00000047368
resolver
ensp
ENSMUSP00000056099
resolver
ensp
ENSMUSP00000263359
resolver
enst
ENSMUST00000052556
resolver
genesymbol
Abhd17b
resolver
uniprot
Q58EV9
resolver
uniprot
Q8K275
resolver
uniprot_entry
AB17B_MOUSE
resolver
uniprot_sec
Q58EV9
resolver
uniprot_sec
Q8K275
resolver
amino_acid_sequence
MNNLSFSELCCLFCCPPCPGKIASKLAFLPPDPTYTLMCDESGSRWTLHLSERADWQYSSREKDAIECFMTRTSKGNRIACMFVRCSPNAKYTLLFSHGNAVDLGQMSSFYIGLGSRINCNIFSYDYSGYGASSGKPTEKNLYADVEAAWLALRTRYGIRPENVIIYGQSIGTVPSVDLAARYESAAVILHSPLTSGMRVAFPDTKKTYCFDAFPNIDKISKITSPVLIIHGTEDEVIDFSHGLALFERCQRPVEPLWVEGAGHNDVELYGQYLERLKQFVSQELVNL
uniprot
proteins
ec_number
3.1.2.22
uniprot
proteins
function
FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in proteins (PubMed:27307232). Has depalmitoylating activity towards DLG4/PSD95 (PubMed:27307232). Has depalmitoylating activity towards GAP43 (PubMed:27307232). Has depalmitoylating activity towards MAP6 (PubMed:28521134). Has depalmitoylating activity towards NRAS (By similarity). {ECO:0000250|UniProtKB:Q5VST6, ECO:0000269|PubMed:27307232, ECO:0000305|PubMed:28521134}.
uniprot
proteins
mass_dalton
32201
uniprot
proteins
mutagenesis
MUTAGEN 1..20; /note="MNNLSFSELCCLFCCPPCPG->MGSNKSKPKDASQRRRSLEP: Loss of palmitoylation activity towards LG4/PSD95 and appears more diffused at the plasma membrane."; /evidence="ECO:0000269|PubMed:27307232"; MUTAGEN 10..18; /note="CCLFCCPPC->SSLFSSPPS: Loss of palmitoylation and plasma membrane localization. Loss of LG4/PSD95 depalmitoylation."; /evidence="ECO:0000269|PubMed:27307232"; MUTAGEN 170; /note="S->A: Loss of catalytic activity."; /evidence="ECO:0000269|PubMed:27307232"; MUTAGEN 235; /note="D->A: Loss of catalytic activity. No effect on its localization. Trapping-mutant that stabilizes interaction with LG4/PSD95."; /evidence="ECO:0000269|PubMed:27307232"; MUTAGEN 264; /note="H->A: Loss of catalytic activity."; /evidence="ECO:0000269|PubMed:27307232
uniprot
proteins
post_translational_modification
PTM: Palmitoylated on cysteine residues located in a cysteine cluster at the N-terminus which promotes membrane localization. Palmitoylation is required for post-synaptic localization and for depalmitoylating activity towards DLG4/PSD95. {ECO:0000269|PubMed:27307232}.
uniprot
proteins
protein_family
AB hydrolase superfamily
uniprot
proteins
protein_family
ABHD17 family
uniprot
proteins
pubmed
12838346
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
27307232
uniprot
proteins
pubmed
28521134
uniprot
proteins
sequence_length
288
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27307232}; Lipid-anchor {ECO:0000269|PubMed:27307232}; Cytoplasmic side {ECO:0000269|PubMed:27307232}. Recycling endosome membrane {ECO:0000269|PubMed:27307232}; Lipid-anchor {ECO:0000269|PubMed:27307232}; Cytoplasmic side {ECO:0000269|PubMed:27307232}. Cell projection, dendritic spine {ECO:0000269|PubMed:27307232}. Postsynaptic density membrane {ECO:0000269|PubMed:27307232}.
uniprot
proteins