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Database: UniProt
Entry: A0A2A3ENU8_APICC
LinkDB: A0A2A3ENU8_APICC
Original site: A0A2A3ENU8_APICC 
ID   A0A2A3ENU8_APICC        Unreviewed;       796 AA.
AC   A0A2A3ENU8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=phospholipase A2 {ECO:0000256|ARBA:ARBA00013278};
DE            EC=3.1.1.4 {ECO:0000256|ARBA:ARBA00013278};
GN   ORFNames=APICC_01274 {ECO:0000313|EMBL:PBC33184.1};
OS   Apis cerana cerana (Oriental honeybee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Apis.
OX   NCBI_TaxID=94128 {ECO:0000313|EMBL:PBC33184.1, ECO:0000313|Proteomes:UP000242457};
RN   [1] {ECO:0000313|EMBL:PBC33184.1, ECO:0000313|Proteomes:UP000242457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Pupae without intestine {ECO:0000313|EMBL:PBC33184.1};
RA   Diao Q., Sun L., Zheng H., Zheng H., Xu S., Wang S., Zeng Z., Hu F., Su S.,
RA   Wu J.;
RT   "Genomic and transcriptomic analysis on Apis cerana provide comprehensive
RT   insights into honey bee biology.";
RL   Submitted (JUL-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|ARBA:ARBA00023422};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC         Evidence={ECO:0000256|ARBA:ARBA00023422};
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DR   EMBL; KZ288204; PBC33184.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A3ENU8; -.
DR   STRING; 94128.A0A2A3ENU8; -.
DR   Proteomes; UP000242457; Unassembled WGS sequence.
DR   GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07212; Pat_PNPLA9; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR047148; PLPL9.
DR   InterPro; IPR002641; PNPLA_dom.
DR   PANTHER; PTHR24139:SF34; 85_88 KDA CALCIUM-INDEPENDENT PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR24139; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF01734; Patatin; 1.
DR   SMART; SM00248; ANK; 6.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
DR   PROSITE; PS51635; PNPLA; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242457};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   REPEAT          155..187
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          221..253
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          311..343
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          344..376
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          467..649
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
SQ   SEQUENCE   796 AA;  87885 MW;  D645FCFA2E793136 CRC64;
     MTWLGTIASN VLRMVYTDVP PSIVQEVKPE NYSNRHIECR EDGIVLYGPG EKNEKKYEIV
     LHRPCTETLH QAYSLYRSEE KKETEIHFLV YKDKVPVLVQ ICREMCNVNK IQKLCDTLME
     HPTWTLAHLA AHFALYNAFA HADVNSQLNS GDVETGVSPL QVAVQTNNLR TVQMLIEAKS
     SLEHLDFNAN TVYHYAATST KEIILALGGD LPNSLNSRNS NGHTPMHVAC LNNKPECVKA
     LLLIGADVNI PASEGQPSSP GYVGDFLHSQ PNVLHAEDMR FGGTPLHWSL SREVINALIE
     SNCDIDALNF DGRTALHIMA MRKRLPCVVA LLSHMCSVNI VDKDGNTPLH LAVSEGTAAI
     VQTLIGFGAD IDARNWKSET PRHRINIDNN EGQKILYILD AVGAQRCPPD MINCNLGCKY
     NENFNGIAPQ QPPKAIPRTI LDQMLHVSGM DKMATQENKK IKGGRLLCLD GGGIRGLVLV
     QTLLEIESIL KKPIIECFDW IAGTSTGGIL ALGLAAGKSL RECQALYFRI KEEAFVGMRP
     YNSEGLEKVL KDSLGANTVM SDIEKPKIMI TSVLADKKPV DLYLFRNYDA PSALLEIPEN
     STSASPVPPN EQLLWHAARA TGAAPSYFRA FGKFLDGGLI ANNPTLDAIT EIHEYNLALK
     ASGREQEVIP LSLVVSLGTG LIPTSPLKDI DIFLPESLWS TAKFAMGISV LAVLLVDQAT
     ASDGRIVDRA RNWCSMIGVP YYRFNPQLSQ DINMDEKSDE ILADMIWTTK AFMHANRDQI
     KELAAVINRD VYNDIS
//
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