PA2HA_CROSS
ID PA2HA_CROSS Reviewed; 138 AA.
AC P18998; Q90395;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Phospholipase A2 homolog mojave toxin acidic chain;
DE Short=Mtx-a;
DE Contains:
DE RecName: Full=Mojave toxin acidic chain A {ECO:0000303|PubMed:2310754};
DE Contains:
DE RecName: Full=Mojave toxin acidic chain B {ECO:0000303|PubMed:2310754};
DE Contains:
DE RecName: Full=Mojave toxin acidic chain C {ECO:0000303|PubMed:2310754};
DE Flags: Precursor;
OS Crotalus scutulatus scutulatus (Mojave rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8738;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=8112610; DOI=10.1016/0378-1119(94)90761-7;
RA John T.R., Smith L.A., Kaiser I.I.;
RT "Genomic sequences encoding the acidic and basic subunits of Mojave toxin:
RT unusually high sequence identity of non-coding regions.";
RL Gene 139:229-234(1994).
RN [2]
RP PROTEIN SEQUENCE OF 41-80; 84-119 AND 127-138, SUBCELLULAR LOCATION, AND
RP PYROGLUTAMATE FORMATION AT GLN-84.
RC TISSUE=Venom;
RX PubMed=2310754; DOI=10.1016/0167-4838(90)90045-h;
RA Bieber A.L., Becker R.R., McParland R., Hunt D.F., Shabanowitz J.,
RA Yates J.R. III, Martino P.A., Johnson G.R.;
RT "The complete sequence of the acidic subunit from Mojave toxin determined
RT by Edman degradation and mass spectrometry.";
RL Biochim. Biophys. Acta 1037:413-421(1990).
RN [3]
RP PRELIMINARY PROTEIN SEQUENCE OF 41-80; 84-119 AND 127-138.
RC TISSUE=Venom;
RA Bieber A.L., Becker R.R., McParland R., Hunt D.F., Shabanowitz J.,
RA Yates J.R. III, Johnson G.R.;
RT "Studies of the sequence of Mojave toxin: the acidic subunit.";
RL Toxicon 27:31-31(1989).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits
CC neuromuscular transmission by blocking acetylcholine release from the
CC nerve termini.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- SUBUNIT: Heterodimer of an acidic and a basic chain. The acidic subunit
CC is non-toxic, without enzymatic activity and comprises 3 peptides that
CC are cross-linked by 5 disulfide bridges. The basic subunit is toxic,
CC has phospholipase A2 activity and is composed of a single chain.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2310754}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:2310754}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; U01026; AAC59673.1; -; Genomic_DNA.
DR PIR; I51380; I51380.
DR AlphaFoldDB; P18998; -.
DR SMR; P18998; -.
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 Direct protein sequencing; Disulfide bond; Neurotoxin;
KW Presynaptic neurotoxin; Pyrrolidone carboxylic acid; Secreted; Signal;
KW Toxin.
FT SIGNAL 1..40
FT /evidence="ECO:0000305|PubMed:2310754"
FT CHAIN 41..80
FT /note="Mojave toxin acidic chain A"
FT /evidence="ECO:0000269|PubMed:2310754, ECO:0000269|Ref.3"
FT /id="PRO_0000022863"
FT PROPEP 81..83
FT /evidence="ECO:0000305|PubMed:2310754"
FT /id="PRO_0000022864"
FT CHAIN 84..119
FT /note="Mojave toxin acidic chain B"
FT /evidence="ECO:0000269|PubMed:2310754, ECO:0000269|Ref.3"
FT /id="PRO_0000022865"
FT PROPEP 120..126
FT /evidence="ECO:0000305|PubMed:2310754"
FT /id="PRO_0000022866"
FT CHAIN 127..138
FT /note="Mojave toxin acidic chain C"
FT /evidence="ECO:0000269|PubMed:2310754, ECO:0000269|Ref.3"
FT /id="PRO_0000022867"
FT MOD_RES 84
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:2310754"
FT DISULFID 42..131
FT /evidence="ECO:0000305"
FT DISULFID 44..60
FT /evidence="ECO:0000305"
FT DISULFID 59..111
FT /evidence="ECO:0000305"
FT DISULFID 65..138
FT /evidence="ECO:0000305"
FT DISULFID 66..104
FT /evidence="ECO:0000305"
FT DISULFID 73..97
FT /evidence="ECO:0000305"
FT DISULFID 91..102
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="Q -> E (in Ref. 2; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 138 AA; 15211 MW; 8164C7C8D27D6EBE CRC64;
MRALWIVAVL LVGVEGSLVE FETLIMKIAG RSGISYYSSY GCYCGAGGQG WPQDASDRCC
FEHDCCYAKL TGCDPTTDVY TYRQEDGEIV CGGDDPCGTQ ICECDKAAAI CFRDSMNTYD
YKYLRFSPEN CQGESQPC
