ID A0A3Q3AVF4_KRYMA Unreviewed; 232 AA.
AC A0A3Q3AVF4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Acyl-protein thioesterase 1 {ECO:0000256|ARBA:ARBA00014923};
DE EC=3.1.2.22 {ECO:0000256|ARBA:ARBA00012423};
DE AltName: Full=Lysophospholipase 1 {ECO:0000256|ARBA:ARBA00042324};
DE AltName: Full=Lysophospholipase I {ECO:0000256|ARBA:ARBA00042319};
DE AltName: Full=Palmitoyl-protein hydrolase {ECO:0000256|ARBA:ARBA00031195};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000020541.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000020541.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000256|ARBA:ARBA00000597};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000256|ARBA:ARBA00000597};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-(9Z-octadecenoyl)-2-acyl-sn-glycero-3-phosphocholine + H2O
CC = (9Z)-octadecenoate + a 2-acyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:41720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57875, ChEBI:CHEBI:78421;
CC Evidence={ECO:0000256|ARBA:ARBA00036969};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41721;
CC Evidence={ECO:0000256|ARBA:ARBA00036969};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Nucleus membrane
CC {ECO:0000256|ARBA:ARBA00004126}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC family. {ECO:0000256|ARBA:ARBA00006499}.
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DR RefSeq; XP_017261775.1; XM_017406286.1.
DR AlphaFoldDB; A0A3Q3AVF4; -.
DR STRING; 37003.ENSKMAP00000020541; -.
DR Ensembl; ENSKMAT00000020810.1; ENSKMAP00000020541.1; ENSKMAG00000015266.1.
DR GeneID; 108230239; -.
DR KEGG; kmr:108230239; -.
DR CTD; 10434; -.
DR GeneTree; ENSGT00940000154185; -.
DR OMA; RARYEWA; -.
DR OrthoDB; 4670340at2759; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003140; PLipase/COase/thioEstase.
DR PANTHER; PTHR10655:SF22; ACYL-PROTEIN THIOESTERASE 1; 1.
DR PANTHER; PTHR10655; LYSOPHOSPHOLIPASE-RELATED; 1.
DR Pfam; PF02230; Abhydrolase_2; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800}.
FT DOMAIN 11..223
FT /note="Phospholipase/carboxylesterase/thioesterase"
FT /evidence="ECO:0000259|Pfam:PF02230"
SQ SEQUENCE 232 AA; 25042 MW; D8F3F1BB7EC38289 CRC64;
MCGNNMSAPL PAIVPAARKA TAAVIFLHGL GDTGHGWAEA FAGIRIPHVK YICPHAPTMP
VSLNMRMSMP SWFDIYGLSP DADEDEAGIK RASENIKALI DQEVKNGIPS HRIILGGFSQ
GGALSLYTAL TSQQKLAGVV ALSCWLPLRK SFPQAAANSA NKDMHVLQCH GDADPLVPFV
FGTQTAEKLK TLTNPANITF KPYRGLPHSA CPEEMVDIKR FVERQLPAIS DE
//
