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Database: UniProt
Entry: A0A383Z0I3_BALAS
LinkDB: A0A383Z0I3_BALAS
Original site: A0A383Z0I3_BALAS 
ID   A0A383Z0I3_BALAS        Unreviewed;       172 AA.
AC   A0A383Z0I3; A0A383Z198;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 2.
DT   27-MAR-2024, entry version 22.
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};
GN   Name=LYPLA1 {ECO:0000313|RefSeq:XP_007168663.2,
GN   ECO:0000313|RefSeq:XP_007168664.1};
OS   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007168663.2};
RN   [1] {ECO:0000313|RefSeq:XP_007168663.2, ECO:0000313|RefSeq:XP_007168664.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007168663.2,
RC   ECO:0000313|RefSeq:XP_007168664.1};
RG   RefSeq;
RL   Submitted (JAN-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_007168663.2; XM_007168601.2.
DR   RefSeq; XP_007168664.1; XM_007168602.1.
DR   AlphaFoldDB; A0A383Z0I3; -.
DR   STRING; 310752.A0A383Z0I3; -.
DR   KEGG; bacu:103003805; -.
DR   CTD; 10434; -.
DR   InParanoid; A0A383Z0I3; -.
DR   OrthoDB; 4670340at2759; -.
DR   Proteomes; UP000261681; 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:UP000261681}.
FT   DOMAIN          1..167
FT                   /note="Phospholipase/carboxylesterase/thioesterase"
FT                   /evidence="ECO:0000259|Pfam:PF02230"
SQ   SEQUENCE   172 AA;  18712 MW;  86D5BAA98258BF1B CRC64;
     MPVTLNMNMA MPSWFDIIGL SPDSQEDETG IKQAAESVKA LIDQEVKNGI PSNRIILGGF
     SQGGALSLYT ALTTQQKLAG VTALSCWLPL RTSFPQGPIS GVNRDISILQ CHGDLDPLVP
     LMFGSLTAER LKTLVNPTNV TFKTYGGMMH SSCQQEMMDI KQFIDKLLPP ID
//
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