ID   AB17B_XENLA             Reviewed;         288 AA.
AC   Q6DCC5; Q6DDV9;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
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};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo, and Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; BC077395; AAH77395.1; -; mRNA.
DR   EMBL; BC078123; AAH78123.1; -; mRNA.
DR   RefSeq; NP_001086750.1; NM_001093281.1.
DR   RefSeq; NP_001087176.1; NM_001093707.1.
DR   RefSeq; XP_018102696.1; XM_018247207.1.
DR   AlphaFoldDB; Q6DCC5; -.
DR   SMR; Q6DCC5; -.
DR   ESTHER; xenla-q6dcc5; ABHD17-depalmitoylase.
DR   DNASU; 446585; -.
DR   DNASU; 447065; -.
DR   GeneID; 446585; -.
DR   GeneID; 447065; -.
DR   KEGG; xla:446585; -.
DR   KEGG; xla:447065; -.
DR   CTD; 446585; -.
DR   CTD; 447065; -.
DR   Xenbase; XB-GENE-17335073; abhd17b.L.
DR   Xenbase; XB-GENE-962859; abhd17b.S.
DR   OMA; FMTRTCK; -.
DR   OrthoDB; 691954at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 446585; Expressed in blastula and 19 other tissues.
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:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR022742; Hydrolase_4.
DR   InterPro; IPR001375; Peptidase_S9.
DR   Pfam; PF12146; Hydrolase_4; 1.
DR   Pfam; PF00326; Peptidase_S9; 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_0000281115"
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"
FT   CONFLICT        69
FT                   /note="F -> C (in Ref. 1; AAH77395)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        87
FT                   /note="C -> S (in Ref. 1; AAH77395)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        159
FT                   /note="I -> V (in Ref. 1; AAH77395)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        282
FT                   /note="A -> T (in Ref. 1; AAH77395)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   288 AA;  32209 MW;  EDDEADC2216C88E9 CRC64;
     MNNLSFSELC CLFCCPPCPG KIASKLAFLP PDPTYTLICD ESGSRWTLHL SERADWQYSS
     REKDAIECFM TRTSRGNRIA CMFVRCCPSA KYTLLFSHGN AVDLGQMSSF YIGLGSRINC
     NIFSYDYSGY GSSSGKPSEK NLYADIDAAW IALRTRYGIR PEHVIIYGQS IGTVPSVDLA
     ARYESAAVIL HSPLTSGMRV AFPDTKKTYC FDAFPNIDKI SKITSPVLII HGTEDEVIDF
     SHGLALFERC QRPVEPLWVE GAGHNDVELY GQYLERLKQF VAQELVNL