AB17B_CHICK
ID AB17B_CHICK Reviewed; 288 AA.
AC Q5ZJ01;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Alpha/beta hydrolase domain-containing protein 17B {ECO:0000305};
DE Short=Abhydrolase domain-containing protein 17B {ECO:0000250|UniProtKB:Q5VST6};
DE EC=3.1.2.22 {ECO:0000250|UniProtKB:Q5VST6};
GN Name=ABHD17B {ECO:0000250|UniProtKB:Q5VST6}; ORFNames=RCJMB04_22d6;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in
CC proteins. Has depalmitoylating activity towards NRAS.
CC {ECO:0000250|UniProtKB:Q5VST6, ECO:0000250|UniProtKB:Q7M759}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) +
CC hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233,
CC Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:74151; EC=3.1.2.22;
CC Evidence={ECO:0000250|UniProtKB:Q7M759};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q7M759};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q7M759}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q7M759}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q7M759}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q7M759}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q7M759}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:Q7M759}. Postsynaptic density membrane
CC {ECO:0000250|UniProtKB:Q7M759}.
CC -!- PTM: Palmitoylated on cysteine residues located in a cysteine cluster
CC at the N-terminus which promotes membrane localization.
CC {ECO:0000250|UniProtKB:Q7M759}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. ABHD17 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ720633; CAG32292.1; -; mRNA.
DR RefSeq; NP_001026594.1; NM_001031423.1.
DR RefSeq; XP_015135774.1; XM_015280288.1.
DR AlphaFoldDB; Q5ZJ01; -.
DR SMR; Q5ZJ01; -.
DR STRING; 9031.ENSGALP00000042466; -.
DR ESTHER; chick-q5zj01; ABHD17-depalmitoylase.
DR MEROPS; S09.055; -.
DR PaxDb; Q5ZJ01; -.
DR Ensembl; ENSGALT00000024428; ENSGALP00000024382; ENSGALG00000015138.
DR GeneID; 427252; -.
DR KEGG; gga:427252; -.
DR CTD; 51104; -.
DR VEuPathDB; HostDB:geneid_427252; -.
DR eggNOG; KOG1552; Eukaryota.
DR GeneTree; ENSGT00940000153636; -.
DR InParanoid; Q5ZJ01; -.
DR OMA; FMTRTCK; -.
DR OrthoDB; 691954at2759; -.
DR PhylomeDB; Q5ZJ01; -.
DR TreeFam; TF314365; -.
DR PRO; PR:Q5ZJ01; -.
DR Proteomes; UP000000539; Chromosome Z.
DR Bgee; ENSGALG00000015138; Expressed in spermatocyte and 12 other tissues.
DR ExpressionAtlas; Q5ZJ01; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:1902817; P:negative regulation of protein localization to microtubule; IEA:Ensembl.
DR GO; GO:1905668; P:positive regulation of protein localization to endosome; IEA:Ensembl.
DR GO; GO:0002084; P:protein depalmitoylation; IEA:Ensembl.
DR GO; GO:1902950; P:regulation of dendritic spine maintenance; IEA:Ensembl.
DR GO; GO:1902473; P:regulation of protein localization to synapse; IEA:Ensembl.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR022742; Hydrolase_4.
DR Pfam; PF12146; Hydrolase_4; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Endosome; Hydrolase; Lipoprotein; Membrane;
KW Palmitate; Postsynaptic cell membrane; Reference proteome; Synapse.
FT CHAIN 1..288
FT /note="Alpha/beta hydrolase domain-containing protein 17B"
FT /id="PRO_0000281114"
FT ACT_SITE 170
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q96GS6"
FT ACT_SITE 235
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O75608"
FT ACT_SITE 264
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O75608"
SQ SEQUENCE 288 AA; 32201 MW; 376A3F0C34F5D9A0 CRC64;
MNNLSFSELC CLFCCPPCPG KIASKLAFLP PDPTYTLMCD ESGSRWTLHL SERADWQYSS
REKDAIECFM TRTSKGNRIA CMFVRCSPNA KYTLLFSHGN AVDLGQMSSF YIGLGSRINC
NIFSYDYSGY GASSGKPSEK NLYADIDAAW VALRTRYGIR PENVIIYGQS IGTVPSVDLA
ARYESAAVIL HSPLTSGMRV AFPDTKKTYC FDAFPNIDKI SKITSPVLII HGTEDEVIDF
SHGLALFERC QRPVEPLWVE GAGHNDVELY GQYLERLKRF VSQELVNL
