ID A0A016UKT9_9BILA Unreviewed; 789 AA.
AC A0A016UKT9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=phospholipase A2 {ECO:0000256|ARBA:ARBA00013278};
DE EC=3.1.1.4 {ECO:0000256|ARBA:ARBA00013278};
GN Name=Acey_s0038.g3630 {ECO:0000313|EMBL:EYC15098.1};
GN ORFNames=Y032_0038g3630 {ECO:0000313|EMBL:EYC15098.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC15098.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYC15098.1}.
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DR EMBL; JARK01001374; EYC15098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016UKT9; -.
DR Proteomes; UP000024635; 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 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; 8.
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:UP000024635};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 40..72
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 108..140
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 209..241
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 242..274
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 390..569
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 327..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 789 AA; 88150 MW; A1257A86654E8A46 CRC64;
MIHIAIACDR LDLFSDANLE YLNGMSTPFQ SLMKMMVQPE GKYPLLLAIE MHRLKIVRRM
LTMGADPLVK DINGNNAIHY ASLASVQMLE LLWEFENCRV LINQPNNEGY VPVMLAIRAG
NPRCFATLLN FGAELSMRVQ GRNPLFEAMQ SKGKNTDIIK AIIEASPDLV KERDSSGNTA
LHAAMYKTPL MGLLLLKCKD VNLNAKNYAG QTPLHIFTHK DEIGLMITLL SYCCDIDAQD
YDGNTALHVA VSKKNIEATR LLLCLGADPN VSNFHEDTPR HLAARLKETA LLESLIKCGA
RTCGPKKLGC VSGCVNEAMV GLLKSSSSSL ESDSPRASSA GLSSQDYPDS VEVDHPIRDF
TQKMFYDGLM ARLEELASRN ERPGNMVNLL SMDGGGIRGL VILQMLMAIE EELNEPIYPY
FDWVAGTSTG ALIATALAQG KTLRECQHIY LRFKDLIFDG WTRPYNASVL EMFMKEAIGE
KSLDDIKYPR LMISTVKADY FPVKLEFMRN YRLPLSDEEN AELGFTDPAE VPTWKALRRT
SAAPMFFSPV DDKYIDGGII ANNPTLDLLA EVQLYNGINT YLPRAKLANI ILRLLFPCSI
WNLGSSIFVQ NFERIEGFVN TSFLDMFNHR KMASQIFSFS NRFSQRAKDK VEIGCVLSLG
TGQIPLSPLD PLHVEIFNPI SSAFTFKNLS LILVDQVTAT EGAPVDRSRS WCNTIGVPFF
RLSAPLHKDI GLGTKDDHDI AHMMWDCVEY THKHRSYIVK LCTLLKRIGK TPTDRRRALP
AMPVLSTES
//
