ID   PA2HB_PROMU             Reviewed;         138 AA.
AC   Q3HLQ4;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Basic phospholipase A2 homolog TM-N49;
DE            Short=svPLA2 homolog;
DE   Flags: Precursor;
OS   Protobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX   NCBI_TaxID=103944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-40, FUNCTION, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=Hunan; TISSUE=Venom, and Venom gland;
RX   PubMed=16413680; DOI=10.1016/j.bbagen.2005.11.022;
RA   Wei J.-F., Wei X.-L., Chen Q.-Y., Huang T., Qiao L.-Y., Wang W.-Y.,
RA   Xiong Y.-L., He S.-H.;
RT   "N49 phospholipase A2, a unique subgroup of snake venom group II
RT   phospholipase A2.";
RL   Biochim. Biophys. Acta 1760:462-471(2006).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that exhibits potent
CC       myotoxic activity causing inflammatory cell infiltration, severe
CC       myoedema, myonecrosis and myolysis in the gastrocnemius muscles of
CC       BALB/c mice. {ECO:0000269|PubMed:16413680}.
CC   -!- SUBUNIT: Homodimer; non-covalently linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=13875; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16413680};
CC   -!- MISCELLANEOUS: Does not possess enzymatic, hemolytic and hemorrhagic
CC       activities. Fails to induce platelet aggregation by itself, and does
CC       not inhibit ADP-induced platelet aggregation (PubMed:16413680).
CC       {ECO:0000305|PubMed:16413680}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       N49 sub-subfamily. {ECO:0000305}.
CC   -!- CAUTION: Does not bind calcium as one of the calcium-binding sites is
CC       lost (Asp->Asn in position 64, which corresponds to 'Asn-49' in the
CC       current nomenclature). {ECO:0000305}.
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DR   EMBL; DQ212913; ABA60780.1; -; mRNA.
DR   AlphaFoldDB; Q3HLQ4; -.
DR   SMR; Q3HLQ4; -.
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; Myotoxin; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:16413680"
FT   CHAIN           17..138
FT                   /note="Basic phospholipase A2 homolog TM-N49"
FT                   /id="PRO_0000419212"
FT   DISULFID        42..131
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..60
FT                   /evidence="ECO:0000250"
FT   DISULFID        59..111
FT                   /evidence="ECO:0000250"
FT   DISULFID        65..138
FT                   /evidence="ECO:0000250"
FT   DISULFID        66..104
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..97
FT                   /evidence="ECO:0000250"
FT   DISULFID        91..102
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   138 AA;  15660 MW;  62F37D5F47866B0E CRC64;
     MRTLWIMAVL LLGVEGNLLQ FRKMIKKMTG KEPILSYATY GCNCGMAGVG QPVDGTDRCC
     FVHNCCYEKV TSCSPKWDQY IYSWENGNIV CGEKNPCKKQ ICECDKAAAM CFRDNVKTYK
     KRNIFYPKSS CTEPTDTC