ID   A0A5N4DCF7_CAMDR        Unreviewed;       138 AA.
AC   A0A5N4DCF7;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   29-MAY-2024, entry version 15.
DE   RecName: Full=Phospholipase A2 {ECO:0000256|ARBA:ARBA00013278, ECO:0000256|RuleBase:RU361236};
DE            EC=3.1.1.4 {ECO:0000256|ARBA:ARBA00013278, ECO:0000256|RuleBase:RU361236};
GN   ORFNames=Cadr_000013352 {ECO:0000313|EMBL:KAB1268750.1};
OS   Camelus dromedarius (Dromedary) (Arabian camel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX   NCBI_TaxID=9838 {ECO:0000313|EMBL:KAB1268750.1, ECO:0000313|Proteomes:UP000299084};
RN   [1] {ECO:0000313|EMBL:KAB1268750.1, ECO:0000313|Proteomes:UP000299084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Drom800 {ECO:0000313|EMBL:KAB1268750.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:KAB1268750.1};
RX   PubMed=30972949; DOI=.1111/1755-0998.13020;
RA   Elbers J.P., Rogers M.F., Perelman P.L., Proskuryakova A.A.,
RA   Serdyukova N.A., Johnson W.E., Horin P., Corander J., Murphy D.,
RA   Burger P.A.;
RT   "Improving Illumina assemblies with Hi-C and long reads: an example with
RT   the North African dromedary.";
RL   Mol. Ecol. Resour. 19:1015-1026(2019).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC         hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC         Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC         Evidence={ECO:0000256|ARBA:ARBA00001479};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC         Evidence={ECO:0000256|ARBA:ARBA00001479};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC         phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-
CC         hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC         Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008;
CC         Evidence={ECO:0000256|ARBA:ARBA00001804};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC         Evidence={ECO:0000256|ARBA:ARBA00001804};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-
CC         sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-
CC         3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:72841, ChEBI:CHEBI:75158;
CC         Evidence={ECO:0000256|ARBA:ARBA00001855};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920;
CC         Evidence={ECO:0000256|ARBA:ARBA00001855};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC         + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC         phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998,
CC         ChEBI:CHEBI:73001; Evidence={ECO:0000256|ARBA:ARBA00001126};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC         Evidence={ECO:0000256|ARBA:ARBA00001126};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC         phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-1-
CC         (9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine;
CC         Xref=Rhea:RHEA:45424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:78097, ChEBI:CHEBI:85217;
CC         Evidence={ECO:0000256|ARBA:ARBA00001129};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425;
CC         Evidence={ECO:0000256|ARBA:ARBA00001129};
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:RU361236};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601211-2};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR601211-2};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC       ECO:0000256|RuleBase:RU361236}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family.
CC       {ECO:0000256|ARBA:ARBA00007056, ECO:0000256|RuleBase:RU003654}.
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:KAB1268750.1}.
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DR   EMBL; JWIN03000013; KAB1268750.1; -; Genomic_DNA.
DR   RefSeq; XP_010978095.1; XM_010979793.1.
DR   AlphaFoldDB; A0A5N4DCF7; -.
DR   GeneID; 105088846; -.
DR   KEGG; cdk:105088846; -.
DR   CTD; 5322; -.
DR   OrthoDB; 638584at2759; -.
DR   Proteomes; UP000299084; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IEA:TreeGrafter.
DR   GO; GO:0005543; F:phospholipid binding; IEA:TreeGrafter.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR   GO; GO:0042130; P:negative regulation of T cell proliferation; IEA:TreeGrafter.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   CDD; cd00125; PLA2c; 1.
DR   Gene3D; 1.20.90.10; Phospholipase A2 domain; 1.
DR   InterPro; IPR001211; PLipase_A2.
DR   InterPro; IPR033112; PLipase_A2_Asp_AS.
DR   InterPro; IPR016090; PLipase_A2_dom.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   InterPro; IPR033113; PLipase_A2_His_AS.
DR   PANTHER; PTHR11716; PHOSPHOLIPASE A2 FAMILY MEMBER; 1.
DR   PANTHER; PTHR11716:SF10; PHOSPHOLIPASE A2 GROUP V; 1.
DR   Pfam; PF00068; Phospholip_A2_1; 1.
DR   PRINTS; PR00389; PHPHLIPASEA2.
DR   SMART; SM00085; PA2c; 1.
DR   SUPFAM; SSF48619; Phospholipase A2, PLA2; 1.
DR   PROSITE; PS00119; PA2_ASP; 1.
DR   PROSITE; PS00118; PA2_HIS; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR601211-2};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR601211-3};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361236};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361236};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601211-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000299084};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU361236};
KW   Signal {ECO:0000256|RuleBase:RU361236}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|RuleBase:RU361236"
FT   CHAIN           21..138
FT                   /note="Phospholipase A2"
FT                   /evidence="ECO:0000256|RuleBase:RU361236"
FT                   /id="PRO_5024501216"
FT   DOMAIN          21..138
FT                   /note="Phospholipase A2"
FT                   /evidence="ECO:0000259|SMART:SM00085"
FT   ACT_SITE        67
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-1"
FT   ACT_SITE        111
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-1"
FT   BINDING         47
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-2"
FT   BINDING         49
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-2"
FT   BINDING         51
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-2"
FT   BINDING         68
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-2"
FT   DISULFID        48..64
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-3"
FT   DISULFID        63..117
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-3"
FT   DISULFID        70..110
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-3"
FT   DISULFID        97..108
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601211-3"
SQ   SEQUENCE   138 AA;  15704 MW;  02A65C50C929C870 CRC64;
     MKGVLILAWF LACSVPAVPG SLLDLSSMIE DVTGKPALES FGFYGCYCGW GGKGTPVDAI
     DWCCWWHDVC YAELERKGYN VLTQSYRYRV RQGLVTCELG SHCQMELCAC DQKLVHCLKR
     NRRSYSSLYQ YFPNFLCI
//