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Database: UniProt
Entry: A0A094KQC1_ANTCR
LinkDB: A0A094KQC1_ANTCR
Original site: A0A094KQC1_ANTCR 
ID   A0A094KQC1_ANTCR        Unreviewed;       432 AA.
AC   A0A094KQC1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Phospholipase A1 member A {ECO:0000256|ARBA:ARBA00040696};
DE   Flags: Fragment;
GN   ORFNames=N321_13925 {ECO:0000313|EMBL:KFZ59547.1};
OS   Antrostomus carolinensis (Chuck-will's-widow) (Caprimulgus carolinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Caprimulgiformes;
OC   Caprimulgidae; Antrostomus.
OX   NCBI_TaxID=279965 {ECO:0000313|EMBL:KFZ59547.1, ECO:0000313|Proteomes:UP000053620};
RN   [1] {ECO:0000313|EMBL:KFZ59547.1, ECO:0000313|Proteomes:UP000053620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N321 {ECO:0000313|EMBL:KFZ59547.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z)-octadecenoyl-sn-glycero-3-phospho-L-serine + H2O =
CC         (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-
CC         serine + H(+); Xref=Rhea:RHEA:40491, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74905,
CC         ChEBI:CHEBI:77342; Evidence={ECO:0000256|ARBA:ARBA00036960};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40492;
CC         Evidence={ECO:0000256|ARBA:ARBA00036960};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O =
CC         (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine;
CC         Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617;
CC         Evidence={ECO:0000256|ARBA:ARBA00000834};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500;
CC         Evidence={ECO:0000256|ARBA:ARBA00000834};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC         3-phospho-L-serine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC         glycero-3-phospho-L-serine + H(+) + hexadecanoate;
CC         Xref=Rhea:RHEA:41187, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:75032, ChEBI:CHEBI:77830;
CC         Evidence={ECO:0000256|ARBA:ARBA00036542};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41188;
CC         Evidence={ECO:0000256|ARBA:ARBA00036542};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|RuleBase:RU004262}.
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DR   EMBL; KL352027; KFZ59547.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094KQC1; -.
DR   ESTHER; antcr-a0a094kqc1; Phospholipase.
DR   Proteomes; UP000053620; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro.
DR   GO; GO:0016298; F:lipase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd00707; Pancreat_lipase_like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013818; Lipase.
DR   InterPro; IPR016272; Lipase_LIPH.
DR   InterPro; IPR033906; Lipase_N.
DR   InterPro; IPR000734; TAG_lipase.
DR   PANTHER; PTHR11610; LIPASE; 1.
DR   PANTHER; PTHR11610:SF111; PHOSPHOLIPASE A1 MEMBER A; 1.
DR   Pfam; PF00151; Lipase; 1.
DR   PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR   PRINTS; PR00821; TAGLIPASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRSR:PIRSR000865-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000865-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053620};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          9..313
FT                   /note="Lipase"
FT                   /evidence="ECO:0000259|Pfam:PF00151"
FT   ACT_SITE        143
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT   ACT_SITE        167
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT   ACT_SITE        237
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT   BINDING         181
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT   BINDING         183
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT   BINDING         186
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFZ59547.1"
FT   NON_TER         432
FT                   /evidence="ECO:0000313|EMBL:KFZ59547.1"
SQ   SEQUENCE   432 AA;  47051 MW;  C96F823CBE084A5C CRC64;
     AGNTDGSSGH HCTDFQTANF LRGSKLKVHF ILFTSSSPSC GELILPDDGI KNSSFNSSLE
     TKIIIHGFRA LGTKPSWIEG LVHAILHTSQ VNVIAVDWVY GSTAAYPSAV ENVTQLALSI
     SQFISKLLAL GVSGTSIHII GVSLGAHVGG LVGHFHGGQL GRITGLDPAG PKYTRASPEE
     RLDPGDALFV EAIHTDADNF GIRIPVGHID YFVNGGKDQP GCPRFISAGY KYLICDHMRA
     VHLYVSALKH SCPLVAFPCA SHQDFLNGRC LDCGDPFPFS CPRIGLLEQA GVNMRKLSRE
     VKVYLMTSPS APFCVHHSLV EFHLQKKRNT VTSIEITFSS NSTKDTAKIT IPKHQEMGKR
     VLAHRVPLCQ LNHVTLKYLP KNQFWRKDES FIVGKFCTAP LPLDSNRTMS CLPWNLTLPG
     NTDISSKPPT AC
//
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