ID   A0A091H0J8_BUCRH        Unreviewed;       797 AA.
AC   A0A091H0J8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
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=N320_09628 {ECO:0000313|EMBL:KFO88205.1};
OS   Buceros rhinoceros silvestris.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Bucerotiformes; Bucerotidae; Buceros.
OX   NCBI_TaxID=175836 {ECO:0000313|EMBL:KFO88205.1, ECO:0000313|Proteomes:UP000054064};
RN   [1] {ECO:0000313|EMBL:KFO88205.1, ECO:0000313|Proteomes:UP000054064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N320 {ECO:0000313|EMBL:KFO88205.1};
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}.
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DR   EMBL; KL516570; KFO88205.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091H0J8; -.
DR   Proteomes; UP000054064; 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   CDD; cd07201; cPLA2_Grp-IVB-IVD-IVE-IVF; 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:SF54; PLA2C DOMAIN-CONTAINING PROTEIN-RELATED; 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:UP000054064}.
FT   DOMAIN          1..107
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          259..797
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO88205.1"
FT   NON_TER         797
FT                   /evidence="ECO:0000313|EMBL:KFO88205.1"
SQ   SEQUENCE   797 AA;  91377 MW;  785765F731899591 CRC64;
     SSPCSLLTVR VIRARNLHQT DVLSQSDCYV SLWLPTASTN KFQTKTIKNC KDPVWNETFY
     FRIQSQVKNV LELALYDKDV VTQDDHLFTV YFDTAKLSLG EQVFMHFKRD SQRQEELDVV
     FALDNISGPP ETIITNGVLV SRKICCLEVQ VVEKKKKKEK KSLSKKEFSF KVQGSYEGTQ
     EIMLGSDLAF SSSPARFHYA RYRQPTLDVT LPGKKQPPFS HSPVHDTSSS NMELHSLPSG
     KNMLLAEVSA SSSVREVEKP DPDHLDVRLG FDLCAQEQDF LCKRKKYVAP ALKKVLQLEQ
     DLLDHETPVV AIMTTGGGMR SLTALYGSLR GLKKLEVLDC AAYLTGLSGT TWTMSNLYRD
     ADWSQKDLDK QISEAQKHMT KCKINSLSLE YLKYYKKQLS QRKREGRKTS FIDLWGLVLE
     SLLHDGKDNH KLSDQQRAID GGQNPLPIYT AVNVKNNYST LDFKEWVEFT PYEVGLQKYG
     AFVRSEDFGS EFFMGRLMKK VPESRICFLE GMWSSLFSLN VLYIWNSSHS SEDFWHRWTR
     DQVDNIEEEP HLPQKPHELR TRLFTPPGPL GSTLRSALTD RLSIAQEHNF LKGFQMHNDY
     LENKHFCRWK GTVLDTFPNQ LTQSEEFLSL VDTGFFINTS VMPLLKPERK VDIILHLNYS
     AGSQTKALDQ TCKYCSEQGI LFPRVDLSEE DRRNLKECYL FDGAETPGAP VLLFFPLVND
     TFQKYKAPGQ KRSESEMEDG KVDLYGCCSP YSTYSIQYTE KAYDCLVQLG EYNILNNKDL
     IMQALHTAVA RKRQKKK
//