PA2A6_CROHD
ID PA2A6_CROHD Reviewed; 138 AA.
AC D6MKR0; D6MKQ9;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Acidic phospholipase A2 CH-E6';
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=CH-E6;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
OS Crotalus horridus (Timber rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=35024;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Iowa, and South Carolina; TISSUE=Venom, and Venom gland;
RX PubMed=20347857; DOI=10.1016/j.toxicon.2010.03.015;
RA Wang Y.-M., Parmelee J., Guo Y.-W., Tsai I.-H.;
RT "Absence of phospholipase A(2) in most Crotalus horridus venom due to
RT translation blockage: comparison with Crotalus horridus atricaudatus
RT venom.";
RL Toxicon 56:93-100(2010).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that shows high lipolytic
CC and weak ADP-induced platelet aggregation activities. Also shows weak
CC anticoagulant activity. PLA2 catalyzes the calcium-dependent hydrolysis
CC of the 2-acyl groups in 3-sn-phosphoglycerides (By similarity).
CC {ECO:0000250}.
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:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-
CC ProRule:PRU10036};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: The subspecies C.h.atricaudatus mentioned in
CC PubMed:20347857 is currently considered invalid. However, since
CC different origins of specimens explain sequence variations, the
CC specimen origins are indicated under strain in the reference section
CC (in PubMed:20347857, Iowa also refers to C.horridus and South Carolina
CC to C.h.atricaudatus).
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: A venom protein (not sequenced) was found in the specimen of
CC from South Carolina, whereas no venom protein was found in the specimen
CC from Iowa. {ECO:0000305}.
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DR EMBL; GQ168369; ADD62450.1; -; mRNA.
DR EMBL; GQ168368; ADD62449.1; -; mRNA.
DR AlphaFoldDB; D6MKR0; -.
DR SMR; D6MKR0; -.
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: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:UniProtKB-KW.
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 Blood coagulation cascade inhibiting toxin; Calcium; Disulfide bond;
KW Hemostasis impairing toxin; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Platelet aggregation inhibiting toxin; Secreted; Signal;
KW Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000250"
FT CHAIN 17..138
FT /note="Acidic phospholipase A2 CH-E6'"
FT /id="PRO_0000419284"
FT ACT_SITE 63
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT ACT_SITE 105
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 42..131
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 44..60
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 59..111
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 65..138
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 66..104
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 73..97
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 91..102
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT VARIANT 132
FT /note="Q -> R (in Strain: Iowa) (CH-E6)"
SQ SEQUENCE 138 AA; 15509 MW; 7FA826FA76BD86AC CRC64;
MRTLWIVAVL LLGVEGSLVQ FEMMIMEVAK RSGLLWYSAY GCYCGWGGHG RPQDATDRCC
FVHDCCYGKA TDCNPKRVSY TYSEENGEIV CGGDDPCGTQ ICECDKAAAI CFRDNIPSYD
NKYWLFPPKN CQEEPEPC
