ID A0A1U8BT34_MESAU Unreviewed; 288 AA.
AC A0A1U8BT34;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Alpha/beta hydrolase domain-containing protein 17B {ECO:0000256|ARBA:ARBA00039755};
DE EC=3.1.2.22 {ECO:0000256|ARBA:ARBA00012423};
GN Name=Abhd17b {ECO:0000313|RefSeq:XP_012970422.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_012970422.1};
RN [1] {ECO:0000313|RefSeq:XP_012970422.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=28071753;
RA McCann K.E., Sinkiewicz D.M., Norvelle A., Huhman K.L.;
RT "De novo assembly, annotation, and characterization of the whole brain
RT transcriptome of male and female Syrian hamsters.";
RL Sci. Rep. 7:40472-40472(2017).
RN [2] {ECO:0000313|RefSeq:XP_012970422.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000072};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004342};
CC Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004342}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. ABHD17 family.
CC {ECO:0000256|ARBA:ARBA00038397}.
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DR RefSeq; XP_012970422.1; XM_013114968.2.
DR AlphaFoldDB; A0A1U8BT34; -.
DR SMR; A0A1U8BT34; -.
DR STRING; 10036.ENSMAUP00000007751; -.
DR eggNOG; KOG1552; Eukaryota.
DR OrthoDB; 2879561at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:Ensembl.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IEA:Ensembl.
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: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; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR022742; Hydrolase_4.
DR PANTHER; PTHR12277; ALPHA/BETA HYDROLASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR12277:SF48; ALPHA_BETA HYDROLASE DOMAIN-CONTAINING PROTEIN 17B; 1.
DR Pfam; PF12146; Hydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706}.
FT DOMAIN 90..196
FT /note="Serine aminopeptidase S33"
FT /evidence="ECO:0000259|Pfam:PF12146"
SQ SEQUENCE 288 AA; 32201 MW; 4A797F710C99EC72 CRC64;
MNNLSFSELC CLFCCPPCPG KIASKLAFLP PDPTYTLMCD ESGSRWTLHL SERADWQYSS
REKDAIECFM TRTSKGNRIA CMFVRCSPNA KYTLLFSHGN AVDLGQMSSF YIGLGSRINC
NIFSYDYSGY GASSGKPTEK NLYADVEAAW LALRTRYGIR PENVIIYGQS IGTVPSVDLA
ARYESAAVIL HSPLTSGMRV AFPDTKKTYC FDAFPNIDKI SKITSPVLII HGTEDEVIDF
SHGLALFERC QRPVEPLWVE GAGHNDVELY GQYLERLKQF VSQELVNL
//
