ID   A0A5N4DCF7_CAMDR        Unreviewed;       138 AA.
AC   A0A5N4DCF7;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   22-APR-2020, entry version 2.
DE   RecName: Full=Phospholipase A(2) {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=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       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|RuleBase:RU361236};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU361236,
CC       ECO:0000256|SAAS:SAAS00614830}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family.
CC       {ECO:0000256|RuleBase:RU003654, ECO:0000256|SAAS:SAAS00534670}.
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   GeneID; 105088846; -.
DR   Proteomes; UP000299084; Chromosome 13.
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|RuleBase:RU361236};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00331946};
KW   Hydrolase {ECO:0000256|RuleBase:RU361236};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361236};
KW   Secreted {ECO:0000256|RuleBase:RU361236, ECO:0000256|SAAS:SAAS00614840};
KW   Signal {ECO:0000256|RuleBase:RU361236}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|RuleBase:RU361236"
FT   CHAIN           21..138
FT                   /note="Phospholipase A(2)"
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
//