ID   A0A3Q0HMN3_ALLSI        Unreviewed;       844 AA.
AC   A0A3Q0HMN3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=LOC102384971 {ECO:0000313|RefSeq:XP_025071825.1};
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_025071825.1};
RN   [1] {ECO:0000313|RefSeq:XP_025071825.1}
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}.
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   RefSeq; XP_025071825.1; XM_025216040.1.
DR   AlphaFoldDB; A0A3Q0HMN3; -.
DR   STRING; 38654.A0A3Q0HMN3; -.
DR   KEGG; asn:102384971; -.
DR   InParanoid; A0A3Q0HMN3; -.
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   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:UP000189705}.
FT   DOMAIN          24..142
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          304..844
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
SQ   SEQUENCE   844 AA;  96330 MW;  CD793D937779E91A CRC64;
     MFHAVPLHRM SAQMLPLLSA VLFRNEDIWF YGQRHETHPY YNLTVKLLRA RNIRGIDLLS
     KANCYVALKL PAASPFTSRT QVVYNSSHPE WNETFEYRIH SAVKNILEFT FYDKDVVMDS
     HAKSIAFDVG NIKPGQALSH TFVLNPQKKE ELDVEFYLEE STDTPTEVIT NGVLVAHPCL
     CVKGTLNKSK KTQWIIQENC QVHLSVPGAF ENQSSTFCSA DSENRRKIPF LFHVDREIHP
     QLDLELLQTT AVIEEGWTED LKMHTARLGM GSVPVGTLPL GQEAEFSVLL GKEQGVDLTI
     KVEECLQELD VRLSFDLAKG ERDFLDRRKE RASFTLRRLL GLPKKPRKNE VPVVAVVGSG
     GGMRAMTALY GNLLGLQKLN LLDILIYLCG ISGSTWCLSK LYADPYWSHK DLQEAIGIAR
     QLVTSSKVGA FSAERLAYYF HQLFLLEKEG WKVTLTDLWG LIIEYFLHQK EDPSKLSDQQ
     AAVRWGQNPF PVYAAVNVRP HVGSNKFTEW CEFTPHEFGI LKYGAFIHTE DFGSEFFMGL
     LLKKRAEPRI SFLQGIWSSA FAANLDEIWE EVVVSKVGFL ETLRDAIKVA DEAHGYKPVD
     TSELETRMVM PGGAFSNLFQ GFFSSRVSTG ENVNFMHGLH LHKDYLNAKQ FVAWKGLDAF
     PNKLTPQENR LYLIDGVFSI NSPFPLMLQR ERDVDVILSF NYSWEAPFEV LHQAQKYCED
     REIPFPHIAV SEKDRQKPKE CYMFMDAENP KAPIVLHFPL VNNTFQQYKA PGVERETANE
     KSFGNFLVEG ADSPYRSMNF TYKPNEFDRL LELSCYNVLN NKDTILKALA LGMKRRALKK
     ARRQ
//