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AB17C_XENLA
ID   AB17C_XENLA             Reviewed;         311 AA.
AC   Q6DD70;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Alpha/beta hydrolase domain-containing protein 17C {ECO:0000305};
DE            Short=Abhydrolase domain-containing protein 17C {ECO:0000250|UniProtKB:Q6PCB6};
DE            EC=3.1.2.22 {ECO:0000250|UniProtKB:Q8VCV1};
GN   Name=abhd17c {ECO:0000250|UniProtKB:Q6PCB6};
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=Lung;
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:Q6PCB6}.
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:Q6PCB6};
CC   -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC       {ECO:0000250|UniProtKB:B5DFK7}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:B5DFK7}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:B5DFK7}. Cell projection, dendritic spine
CC       {ECO:0000250|UniProtKB:B5DFK7}. Postsynaptic density membrane
CC       {ECO:0000250|UniProtKB:B5DFK7}.
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; BC077755; AAH77755.1; -; mRNA.
DR   RefSeq; NP_001086920.1; NM_001093451.1.
DR   AlphaFoldDB; Q6DD70; -.
DR   SMR; Q6DD70; -.
DR   ESTHER; xenla-q6dd70; ABHD17-depalmitoylase.
DR   DNASU; 446755; -.
DR   GeneID; 446755; -.
DR   KEGG; xla:446755; -.
DR   CTD; 446755; -.
DR   Xenbase; XB-GENE-6040950; abhd17c.S.
DR   OMA; IMHVSIL; -.
DR   OrthoDB; 629316at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 446755; Expressed in egg cell 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   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
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..311
FT                   /note="Alpha/beta hydrolase domain-containing protein 17C"
FT                   /id="PRO_0000297517"
FT   REGION          48..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        193
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GS6"
FT   ACT_SITE        258
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:O75608"
FT   ACT_SITE        287
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:O75608"
SQ   SEQUENCE   311 AA;  34747 MW;  9552A78710F015F9 CRC64;
     MPEQGPRMNG FSLGELCWLF CCPPCPSRIA AKLAFLPPEP TYTVREMEAP ASTAQQPPRE
     EGSGEPAACS LHLSERADWQ YSQRELDAVE VFRWRTERGS FLGCMFVRCS PGSRYTLLFS
     HGNAVDLGQM CSFYIGLGTR INCNIFSYDY SGYGVSSGKP SEKNLYADIE AAWHALRTRY
     GVTPENIILY GQSIGTVPTV DLASRYECAA VILHSPLMSG LRVAFPDTRK TYCFDAFPSI
     DKISKVTSPV LIIHGTEDEV IDFSHGLAMY ERCPRAVEPL WVEGAGHNDI ELYAQYLERL
     KQFISHELPN S
 
 
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