ID   A0A094KG36_ANTCR        Unreviewed;       788 AA.
AC   A0A094KG36;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Phospholipase A2 {ECO:0000256|ARBA:ARBA00013278, ECO:0000256|RuleBase:RU362102};
DE            EC=3.1.1.4 {ECO:0000256|ARBA:ARBA00013278, ECO:0000256|RuleBase:RU362102};
DE   Flags: Fragment;
GN   ORFNames=N321_14222 {ECO:0000313|EMBL:KFZ58323.1};
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:KFZ58323.1, ECO:0000313|Proteomes:UP000053620};
RN   [1] {ECO:0000313|EMBL:KFZ58323.1, ECO:0000313|Proteomes:UP000053620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N321 {ECO:0000313|EMBL:KFZ58323.1};
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=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC         glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC         Evidence={ECO:0000256|RuleBase:RU362102};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- DOMAIN: The N-terminal C2 domain associates with lipid membranes upon
CC       calcium binding. {ECO:0000256|RuleBase:RU362102}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KL350042; KFZ58323.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094KG36; -.
DR   Proteomes; UP000053620; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR   CDD; cd04036; C2_cPLA2; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR041847; C2_cPLA2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR040723; cPLA2_C2.
DR   InterPro; IPR002642; LysoPLipase_cat_dom.
DR   PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR10728:SF22; CYTOSOLIC PHOSPHOLIPASE A2 ZETA; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF18695; cPLA2_C2; 1.
DR   Pfam; PF01735; PLA2_B; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00022; PLAc; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS51210; PLA2C; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU362102};
KW   Cytoplasm {ECO:0000256|RuleBase:RU362102};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362102};
KW   Lipid degradation {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362102};
KW   Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362102};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362102};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053620}.
FT   DOMAIN          1..93
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          254..788
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFZ58323.1"
FT   NON_TER         788
FT                   /evidence="ECO:0000313|EMBL:KFZ58323.1"
SQ   SEQUENCE   788 AA;  89751 MW;  EDEDC7C18C1DF0F7 CRC64;
     ARNIKGTDLL SKADCYVELK LPTASPIISR TQVVDNSDNP EWNETFRYRI HSAVKNILEL
     TLYDKDVLVS DELTSIVFDV GGMKLGQPLL RTFRLNSEAN KELDVEFYLE KCSDTPTEIL
     TNGVLVVHPC LSLQGTVNKE EKTKEKQHGS CEVKLSVPGA YQKQLCIPWR PDNEEDYGTS
     FVFHVDKEMC PELQVELEQT VSVLQDGMNP DIEKHTTVLG LGTVPVNSLP IGQKVNRTVS
     LGEGQSLDMT LKTEESTWDL DIRLGFDLCK DEREFLDKRK KIVSEALRKT LHLKESPPKD
     EVPVIAVLGS GGGIRALTSF YGSLAGLQQL GLLDATIYLC GISGSTWCLS TLYQDPHWSQ
     KDLQDAIRRA QGAVSSSKAG AFSPERLKYY FQELNAMENS GRKVSFTDLW GLIVEYFLQQ
     KEDPSKLSDQ QEAVKWAQNP YPIYAAVNVR PSISSDDFAE WCEFTPYEIG FRKYGAFVRT
     EDFDSEFFMG RLVQKHPEPR ICFLQGMWGS AFAASLDDIC LKVVGKGLGF LDSFKDVIKV
     VDDCRRFHFR DPTRLKTRLV IPGGPLLQIF QDLFKSRVTC GEAFNFMQGL YLHKDYVNIK
     KFVAWRGTHL DAFPNQLTPM EESLYLVDGG FSINSPFPVV LQPERDVDVI LSFNFSWEAP
     FEVLELTQKY CEEQEIPFPK IKLSEEDEKK PKECYMFVDE NNPKAPVVLH FPLVNDTFQK
     YKAPGVKRES EEEKSFGDFI IETKDSPYRT LNFTFEPYDF SRLVEVNRYN VLNSKDTLFK
     TLNLALQR
//