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Database: UniProt
Entry: A0A1U8DGP5_ALLSI
LinkDB: A0A1U8DGP5_ALLSI
Original site: A0A1U8DGP5_ALLSI 
ID   A0A1U8DGP5_ALLSI        Unreviewed;       838 AA.
AC   A0A1U8DGP5;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 2.
DT   27-MAR-2024, entry version 32.
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};
GN   Name=LOC102386211 {ECO:0000313|RefSeq:XP_014380387.2};
OS   Alligator sinensis (Chinese alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_014380387.2};
RN   [1] {ECO:0000313|RefSeq:XP_014380387.2}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_014380387.2; XM_014524901.2.
DR   AlphaFoldDB; A0A1U8DGP5; -.
DR   STRING; 38654.A0A1U8DGP5; -.
DR   KEGG; asn:102386211; -.
DR   eggNOG; KOG1028; Eukaryota.
DR   eggNOG; KOG1325; Eukaryota.
DR   InParanoid; A0A1U8DGP5; -.
DR   OrthoDB; 4250045at2759; -.
DR   Proteomes; UP000189705; Unplaced.
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:UP000189705}.
FT   DOMAIN          28..148
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          301..838
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
SQ   SEQUENCE   838 AA;  96559 MW;  59E31B7A8EE9CC59 CRC64;
     MESCASSPQD VMGTKTKILE KGEVTQMKMC TEQWISDTKT SLSPCYLLTV RIIRARNIHR
     TDVLSETDCY VSLWLPSASL EKARTKTIKN CKDPVWNETF YYRIQSQVKN VLELAIYDDD
     VVTQDDHLFT VHFDVAKLPF GEPVLMYFKF DTQGKEELEV EFTLDQMLGP LETIVTNGVL
     VSREMCCLEV QVDEKKKRRK PSSRKDLSLS VKGSHEETQD IMFGYDTVFS SSCPTTFHYV
     KYKQPVLDIK LPKKHLPSSF HTYACNTKGG PPHVNLNSLP VGEKITVAED KRFDLHVKAE
     NCPGDLDMRL GFDLCWEEQD FLKKRKKHVA SALKKVLHLE QDLQDYETPV IAIMTTGGGM
     RSLTTTYGSL SGLKKLNLLD CATYITGLSG TTWTMANLYQ DADWSQKDLD EKINEAQKQA
     TKCKLGSFSL ERLKYYKQQL SQRKTEGHRT SFIDLWGLIV EYLLHDGKDN HKLSDQREAV
     NQGQNPLPIY TALNVKDNYS TWDFKEWMEF TPYEVGFLKY GAFIRSEDFG SEFFMGRLIK
     KLPESRICYL EGMWSSIFSL NLIYNWTLSH SSEDFWHRWT QDRVDCIEEE PILPTRPHEL
     KTRLFKPAGP LSQAIRGVMT ERLTVACYHN FLKGLQMHND YLNNDNFCRW KDTVLGDSPN
     QLTETEAYLS LVDTGFFINT STPPLLRPQR KVDVILHLNY SAGSQILPLD QSCKYYSELG
     IPFPKIEVSE EDRKNLKECY LFDGAETPGA PILLFFPLVN DTFQNYKAPG VKRSESEMEE
     GKVDLTSSSS PYSTYSVRYT EKDYDQLVKL CEYNILNNEN LIMKTLSMAV ERKRQRKK
//
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