ID   PA2HS_ECHCO             Reviewed;         121 AA.
AC   P0DMT3;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-2015, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Phospholipase A2 homolog ECO_00035 {ECO:0000303|PubMed:23747272};
DE            Short=svPLA2 homolog;
OS   Echis coloratus (Carpet viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
OX   NCBI_TaxID=64175;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MASS SPECTROMETRY, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=23747272; DOI=10.1016/j.toxicon.2013.05.017;
RA   Conlon J.M., Attoub S., Arafat H., Mechkarska M., Casewell N.R.,
RA   Harrison R.A., Calvete J.J.;
RT   "Cytotoxic activities of [Ser49]phospholipase A(2) from the venom of the
RT   saw-scaled vipers Echis ocellatus, Echis pyramidum leakeyi, Echis carinatus
RT   sochureki, and Echis coloratus.";
RL   Toxicon 71:96-104(2013).
CC   -!- FUNCTION: Snake venom phospholipase A2 homolog that lacks enzymatic
CC       activity (By similarity). Shows high myotoxin activities and displays
CC       edema-inducing activities (By similarity). Has cytotoxic activities
CC       against HUVEC cells (LC(50)=4.9 uL) and human lung adenocarcinoma A549
CC       cells (LC(50)=3.5 uL) (PubMed:23747272). {ECO:0000250|UniProtKB:P48650,
CC       ECO:0000269|PubMed:23747272}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P48650}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23747272}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:23747272}.
CC   -!- MASS SPECTROMETRY: Mass=13692; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:23747272};
CC   -!- MASS SPECTROMETRY: Mass=13720; Method=Electrospray; Note=In variant
CC       Val-18.; Evidence={ECO:0000269|PubMed:23747272};
CC   -!- MISCELLANEOUS: Does not show antimicrobial activity against E.coli and
CC       S.aureus and does not produce appreciable hemolysis on human
CC       erythrocytes. {ECO:0000269|PubMed:23747272}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       S49 sub-subfamily. {ECO:0000305}.
CC   -!- CAUTION: Does not bind calcium as one of the calcium-binding sites is
CC       lost (Asp->Ser in position 47, which corresponds to 'Ser-49' in the
CC       current nomenclature). {ECO:0000305}.
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DR   AlphaFoldDB; P0DMT3; -.
DR   SMR; P0DMT3; -.
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:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Disulfide bond; Myotoxin; Secreted; Toxin.
FT   CHAIN           1..121
FT                   /note="Phospholipase A2 homolog ECO_00035"
FT                   /id="PRO_0000432598"
FT   REGION          104..116
FT                   /note="Important for membrane-damaging activities in
FT                   eukaryotes and bacteria; heparin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        25..114
FT                   /evidence="ECO:0000250|UniProtKB:P48650"
FT   DISULFID        27..43
FT                   /evidence="ECO:0000250|UniProtKB:P48650"
FT   DISULFID        42..94
FT                   /evidence="ECO:0000250|UniProtKB:P48650"
FT   DISULFID        48..121
FT                   /evidence="ECO:0000250|UniProtKB:P48650"
FT   DISULFID        49..87
FT                   /evidence="ECO:0000250|UniProtKB:P48650"
FT   DISULFID        56..80
FT                   /evidence="ECO:0000250|UniProtKB:P48650"
FT   DISULFID        74..85
FT                   /evidence="ECO:0000250|UniProtKB:P48650"
FT   VARIANT         18
FT                   /note="A -> V"
FT                   /evidence="ECO:0000305|PubMed:23747272"
SQ   SEQUENCE   121 AA;  13706 MW;  F85394D3A7925E27 CRC64;
     SVIELGKMIV QLTNKTPASY VSYGCFCGGG DRGKPKDATD RCCFVHSCCY DTLPDCSPKT
     DQYKYKWENG EIICENSTSC KKRICECDKA VAICLRENLK TYNKKYKIYP NILCRGEPDK
     C