ID A0A5N4DCF7_CAMDR Unreviewed; 138 AA. AC A0A5N4DCF7; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 02-JUN-2021, entry version 8. DE RecName: Full=Phospholipase A2 {ECO:0000256|RuleBase:RU361236}; DE EC=3.1.1.4 {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|RuleBase:RU361236}; 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}. 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 EMBL; JWIN03000013; KAB1268750.1; -; Genomic_DNA. DR RefSeq; XP_010978095.1; XM_010979793.1. DR GeneID; 105088846; -. DR KEGG; cdk:105088846; -. DR CTD; 5322; -. DR Proteomes; UP000299084; Chromosome 13. DR GO; GO:0005576; C:extracellular region; 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:0102567; F:phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine); IEA:UniProtKB-EC. DR GO; GO:0102568; F:phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine); IEA:UniProtKB-EC. DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro. DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro. DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro. DR CDD; cd00125; PLA2c; 1. DR Gene3D; 1.20.90.10; -; 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; PTHR11716; 1. DR Pfam; PF00068; Phospholip_A2_1; 1. DR PRINTS; PR00389; PHPHLIPASEA2. DR SMART; SM00085; PA2c; 1. DR SUPFAM; SSF48619; SSF48619; 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|RuleBase:RU361236}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361236}; KW Lipid metabolism {ECO:0000256|RuleBase:RU361236}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; 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="PA2c" FT /evidence="ECO:0000259|SMART:SM00085" SQ SEQUENCE 138 AA; 15704 MW; 02A65C50C929C870 CRC64; MKGVLILAWF LACSVPAVPG SLLDLSSMIE DVTGKPALES FGFYGCYCGW GGKGTPVDAI DWCCWWHDVC YAELERKGYN VLTQSYRYRV RQGLVTCELG SHCQMELCAC DQKLVHCLKR NRRSYSSLYQ YFPNFLCI //