PA2HS_ECHCA
ID PA2HS_ECHCA Reviewed; 122 AA.
AC P48650;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Basic phospholipase A2 homolog ecarpholin S {ECO:0000303|PubMed:18586854, ECO:0000303|PubMed:8921006};
DE Short=Ecs-S49 {ECO:0000303|PubMed:8921006};
DE Short=svPLA2 homolog;
OS Echis carinatus (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=40353;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, 3D-STRUCTURE MODELING, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=8921006; DOI=10.1042/bj3190961;
RA Polgar J., Magnenat E.M., Peitsch M.C., Wells T.N.C., Clemetson K.J.;
RT "Asp-49 is not an absolute prerequisite for the enzymic activity of low-
RT M(r) phospholipases A2: purification, characterization and computer
RT modelling of an enzymically active Ser-49 phospholipase A2, ecarpholin S,
RT from the venom of Echis carinatus sochureki (saw-scaled viper).";
RL Biochem. J. 319:961-968(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH SURAMIN AND FATTY
RP ACID, DISULFIDE BONDS, AND FUNCTION.
RX PubMed=18586854; DOI=10.1529/biophysj.107.117747;
RA Zhou X., Tan T.C., Valiyaveettil S., Go M.L., Kini R.M.,
RA Velazquez-Campoy A., Sivaraman J.;
RT "Structural characterization of myotoxic ecarpholin S from Echis carinatus
RT venom.";
RL Biophys. J. 95:3366-3380(2008).
RN [3]
RP DISCUSSION.
RC TISSUE=Venom;
RX PubMed=17927217; DOI=10.1021/bi701304e;
RA Petan T., Krizaj I., Pungercar J.;
RT "Restoration of enzymatic activity in a Ser-49 phospholipase A2 homologue
RT decreases its Ca(2+)-independent membrane-damaging activity and increases
RT its toxicity.";
RL Biochemistry 46:12795-12809(2007).
CC -!- FUNCTION: Snake venom phospholipase A2 homolog that lacks enzymatic
CC activity. Shows high myotoxin activities and displays edema-inducing
CC activities (PubMed:18586854). {ECO:0000269|PubMed:18586854}.
CC -!- ACTIVITY REGULATION: Suramin inhibits the myotoxic activity
CC (PubMed:18586854). {ECO:0000269|PubMed:18586854}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8921006}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:8921006}.
CC -!- MASS SPECTROMETRY: Mass=13805; Mass_error=2.7; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8921006};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC S49 sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: Has been reported as being enzymatically active and calcium-
CC dependently inducing platelet aggregation (PubMed:8921006). This
CC activity appears to be unlikely in light of the lack of activity of
CC both recombinant AtnL (S49) and bothropstoxin-1 (K49), especially
CC keeping in mind the possibility of contamination of the purified
CC protein with catalytically active sPLA2s. The fact that the high level
CC of enzymatic activity reported was determined on PC substrates and that
CC it was in the range of the human group IIA enzyme, which in fact
CC displays a very low activity on PC-rich substrates, casts further doubt
CC on the reported activity of ecarpholin S (PubMed:17927217).
CC {ECO:0000305|PubMed:17927217, ECO:0000305|PubMed:8921006}.
CC -!- CAUTION: Does not bind calcium as one of the calcium-binding sites is
CC lost (Asp->Ser in position 48, which corresponds to 'Ser-49' in the
CC current nomenclature). {ECO:0000305}.
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DR PDB; 2QHD; X-ray; 1.95 A; A/B=1-122.
DR PDB; 2QHE; X-ray; 2.00 A; A=1-122.
DR PDB; 3BJW; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-122.
DR PDBsum; 2QHD; -.
DR PDBsum; 2QHE; -.
DR PDBsum; 3BJW; -.
DR AlphaFoldDB; P48650; -.
DR SMR; P48650; -.
DR EvolutionaryTrace; P48650; -.
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: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 3D-structure; Direct protein sequencing; Disulfide bond; Secreted.
FT CHAIN 1..122
FT /note="Basic phospholipase A2 homolog ecarpholin S"
FT /id="PRO_0000161643"
FT REGION 105..117
FT /note="Important for membrane-damaging activities in
FT eukaryotes and bacteria; heparin-binding"
FT /evidence="ECO:0000250|UniProtKB:P24605"
FT DISULFID 26..115
FT /evidence="ECO:0000269|PubMed:18586854,
FT ECO:0007744|PDB:2QHD, ECO:0007744|PDB:2QHE,
FT ECO:0007744|PDB:3BJW"
FT DISULFID 28..44
FT /evidence="ECO:0000269|PubMed:18586854,
FT ECO:0007744|PDB:2QHD, ECO:0007744|PDB:2QHE,
FT ECO:0007744|PDB:3BJW"
FT DISULFID 43..95
FT /evidence="ECO:0000269|PubMed:18586854,
FT ECO:0007744|PDB:2QHD, ECO:0007744|PDB:2QHE,
FT ECO:0007744|PDB:3BJW"
FT DISULFID 49..122
FT /evidence="ECO:0000269|PubMed:18586854,
FT ECO:0007744|PDB:2QHD, ECO:0007744|PDB:2QHE,
FT ECO:0007744|PDB:3BJW"
FT DISULFID 50..88
FT /evidence="ECO:0000269|PubMed:18586854,
FT ECO:0007744|PDB:2QHD, ECO:0007744|PDB:2QHE,
FT ECO:0007744|PDB:3BJW"
FT DISULFID 57..81
FT /evidence="ECO:0000269|PubMed:18586854,
FT ECO:0007744|PDB:2QHD, ECO:0007744|PDB:2QHE,
FT ECO:0007744|PDB:3BJW"
FT DISULFID 75..86
FT /evidence="ECO:0000269|PubMed:18586854,
FT ECO:0007744|PDB:2QHD, ECO:0007744|PDB:2QHE,
FT ECO:0007744|PDB:3BJW"
FT HELIX 2..13
FT /evidence="ECO:0007829|PDB:2QHD"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:2QHD"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:2QHE"
FT TURN 25..29
FT /evidence="ECO:0007829|PDB:2QHD"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:2QHD"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:2QHD"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:2QHD"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2QHD"
FT HELIX 80..98
FT /evidence="ECO:0007829|PDB:2QHD"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:2QHD"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:2QHD"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:2QHD"
SQ SEQUENCE 122 AA; 13819 MW; 92FA098F1BF3DA45 CRC64;
SVVELGKMII QETGKSPFPS YTSYGCFCGG GERGPPLDAT DRCCLAHSCC YDTLPDCSPK
TDRYKYKREN GEIICENSTS CKKRICECDK AVAVCLRKNL NTYNKKYTYY PNFWCKGDIE
KC
