ID   A0A091TCX9_PHALP        Unreviewed;       745 AA.
AC   A0A091TCX9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Phospholipase A2 {ECO:0000256|RuleBase:RU362102};
DE            EC=3.1.1.4 {ECO:0000256|RuleBase:RU362102};
DE   Flags: Fragment;
GN   ORFNames=N335_14008 {ECO:0000313|EMBL:KFQ71595.1};
OS   Phaethon lepturus (White-tailed tropicbird).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Eurypygimorphae; Phaethontiformes;
OC   Phaethontidae; Phaethon.
OX   NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ71595.1, ECO:0000313|Proteomes:UP000053638};
RN   [1] {ECO:0000313|EMBL:KFQ71595.1, ECO:0000313|Proteomes:UP000053638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ71595.1};
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 {ECO:0000256|ARBA:ARBA00004496}.
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; KK445767; KFQ71595.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091TCX9; -.
DR   PhylomeDB; A0A091TCX9; -.
DR   Proteomes; UP000053638; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; 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; cd07200; cPLA2_Grp-IVA; 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; IPR002642; LysoPLipase_cat_dom.
DR   PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR10728:SF13; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR   Pfam; PF00168; 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:UP000053638}.
FT   DOMAIN          6..124
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          138..740
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   REGION          432..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..446
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         745
FT                   /evidence="ECO:0000313|EMBL:KFQ71595.1"
SQ   SEQUENCE   745 AA;  84657 MW;  D1CC7E3CD6AFD2B8 CRC64;
     MSVIDPYQHI VVEHQYSHIF TVTVKQATNV TKGAIGDMLD TPDPYVELFI PSAPDCRKRT
     KHFNNDVNPV WNETFEFILD PNQENVLEVT LMDANYVMDE TLGTSTFPIS SLKLGEKKEI
     QLTFNDVTEM TLELSLEVCS STDLRFSMAL CDEEKKFRQQ RKDNIMHSMK SFLGEEDSKN
     LTTSRDVPVI AILGSGGGFR AMVGFAGVMK ALYESGILDC ATYIAGLSGS TWYMSTLYSH
     PDFPEKGPKE INQELMNSVS HNPLLLLTPQ KVKRYIEALW NKKSSGQPVT FTDIFGMLIG
     ETLIHNRMDT TLSNMKEKIN NAQCALPLFT CLHVKPDVSE LMFADWVEFS PYEIGMAKYG
     TFMSPDLFGS KFFMGTVVKK YSENPLHFLM GVWGSAFSIL FNRVLGVSNS QNKGPTMEEE
     LENIRLKHLV SNDSSDSEDE SQHPKGTENA EANQEYQNSS QESWVQRMLM ALVGDSALFN
     TREGRAGKVH NFMLGLNLNS CYPLSPLADL LTQESVEEDE LDAAVADPDE FERIYEPLDV
     KSKKIHIVDS GLTFNLPYPL ILRPQRGVDL IISFDFSARP SDSSPPFKEI LLAEKWAKMN
     KLPFPKIDPN VFDREGMKEC YVFKPKDTSS EKDCPTIIHF VLANINFRKY KAPGIPRETQ
     EEKDFADFDI FDDPNTPFST FNFQYPNEAF KRLHDLMEFN TLNNIDVIKQ AMMESIEYRK
     ENPSRCSVSL SSVEARRFFN KNNLN
//