PA2HS_ECHOC
ID PA2HS_ECHOC Reviewed; 138 AA.
AC B5U6Y4;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=Phospholipase A2 homolog;
DE Short=svPLA2 homolog;
DE AltName: Full=PLA2-Eoc15;
DE Flags: Precursor;
OS Echis ocellatus (Ocellated saw-scaled viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
OX NCBI_TaxID=99586;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Wagstaff S.C., Sanz L., Juarez P., Harrison R.A., Calvete J.J.;
RT "Snake venomics and transcriptomics of the ocellated carpet viper, Echis
RT ocellatus.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
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. Shows high myotoxin activities and displays edema-inducing
CC activities (By similarity). Has cytotoxic activities against HUVEC
CC cells (LC(50)=5.0 uL) and human lung adenocarcinoma A549 cells
CC (LC(50)=5.2 uL). {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=13825; Method=Electrospray;
CC 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 (PubMed:23747272). {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 64, which corresponds to 'Ser-49' in the
CC current nomenclature). {ECO:0000305}.
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DR EMBL; FM177946; CAQ72890.1; -; mRNA.
DR AlphaFoldDB; B5U6Y4; -.
DR SMR; B5U6Y4; -.
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; Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:23747272"
FT CHAIN 17..138
FT /note="Phospholipase A2 homolog"
FT /id="PRO_5001339409"
FT REGION 121..133
FT /note="Important for membrane-damaging activities in
FT eukaryotes and bacteria; heparin-binding"
FT /evidence="ECO:0000250|UniProtKB:P24605"
FT DISULFID 42..131
FT /evidence="ECO:0000250|UniProtKB:P48650"
FT DISULFID 44..60
FT /evidence="ECO:0000250|UniProtKB:P48650"
FT DISULFID 59..111
FT /evidence="ECO:0000250|UniProtKB:P48650"
FT DISULFID 65..138
FT /evidence="ECO:0000250|UniProtKB:P48650"
FT DISULFID 66..104
FT /evidence="ECO:0000250|UniProtKB:P48650"
FT DISULFID 73..97
FT /evidence="ECO:0000250|UniProtKB:P48650"
FT DISULFID 91..102
FT /evidence="ECO:0000250|UniProtKB:P48650"
SQ SEQUENCE 138 AA; 15634 MW; 86703E43BB4034C3 CRC64;
MRALWIVAVW LIGVEGSVVE LGKMIIQETG KSPFPSYTSY GCFCGGGEKG TPKDATDRCC
FVHSCCYDKL PDCSPKTDRY KYQRENGEII CENSTSCKKR ICECDKAVAV CLRENLQTYN
KKYTYYPNFL CKGEPEKC
