ID   PA2HH_TRIST             Reviewed;         137 AA.
AC   Q6H3D7;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Basic phospholipase A2 homolog CTs-R6;
DE            Short=svPLA2 homolog;
DE   Flags: Precursor;
OS   Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera
OS   stejnegeri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX   NCBI_TaxID=39682;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-39, FUNCTION, MASS
RP   SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   STRAIN=Chinese; TISSUE=Venom, and Venom gland;
RX   PubMed=12959640; DOI=10.1042/bj20030818;
RA   Tsai I.-H., Wang Y.-M., Chen Y.-H., Tsai T.-S., Tu M.-C.;
RT   "Venom phospholipases A2 of bamboo viper (Trimeresurus stejnegeri):
RT   molecular characterization, geographic variations and evidence of multiple
RT   ancestries.";
RL   Biochem. J. 377:215-223(2004).
CC   -!- FUNCTION: Snake venom phospholipase A2 homolog that induces local edema
CC       a few hours after injection (5-10 ug) in the hind paw, and shows weak
CC       anticoagulant and myotoxic activities. {ECO:0000269|PubMed:12959640}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12959640}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:12959640}.
CC   -!- MASS SPECTROMETRY: Mass=13576; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:12959640};
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; AY211932; AAP48890.1; -; mRNA.
DR   PDB; 4H0S; X-ray; 1.55 A; A/B/C=1-137.
DR   PDBsum; 4H0S; -.
DR   AlphaFoldDB; Q6H3D7; -.
DR   SMR; Q6H3D7; -.
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   3D-structure; Blood coagulation cascade inhibiting toxin;
KW   Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW   Myotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:12959640"
FT   CHAIN           17..137
FT                   /note="Basic phospholipase A2 homolog CTs-R6"
FT                   /evidence="ECO:0000305|PubMed:12959640"
FT                   /id="PRO_0000419081"
FT   DISULFID        42..130
FT                   /evidence="ECO:0007744|PDB:4H0S"
FT   DISULFID        44..60
FT                   /evidence="ECO:0007744|PDB:4H0S"
FT   DISULFID        59..110
FT                   /evidence="ECO:0007744|PDB:4H0S"
FT   DISULFID        65..137
FT                   /evidence="ECO:0007744|PDB:4H0S"
FT   DISULFID        66..103
FT                   /evidence="ECO:0007744|PDB:4H0S"
FT   DISULFID        73..97
FT                   /evidence="ECO:0007744|PDB:4H0S"
FT   DISULFID        91..101
FT                   /evidence="ECO:0007744|PDB:4H0S"
FT   HELIX           18..29
FT                   /evidence="ECO:0007829|PDB:4H0S"
FT   HELIX           33..37
FT                   /evidence="ECO:0007829|PDB:4H0S"
FT   TURN            41..43
FT                   /evidence="ECO:0007829|PDB:4H0S"
FT   HELIX           55..68
FT                   /evidence="ECO:0007829|PDB:4H0S"
FT   TURN            75..77
FT                   /evidence="ECO:0007829|PDB:4H0S"
FT   STRAND          82..85
FT                   /evidence="ECO:0007829|PDB:4H0S"
FT   STRAND          88..91
FT                   /evidence="ECO:0007829|PDB:4H0S"
FT   HELIX           98..113
FT                   /evidence="ECO:0007829|PDB:4H0S"
FT   TURN            114..117
FT                   /evidence="ECO:0007829|PDB:4H0S"
FT   HELIX           120..124
FT                   /evidence="ECO:0007829|PDB:4H0S"
FT   HELIX           127..129
FT                   /evidence="ECO:0007829|PDB:4H0S"
SQ   SEQUENCE   137 AA;  15301 MW;  27C25A9C679332E3 CRC64;
     MRTLLIMAVL LLGVEGSLLQ LRKMIKKMTN KEPILSYSKY GCNCGMAGRG KPVDATDTCC
     SIHNCCYGKV TSCSTKWDSY SYSWENGDIV CDEKHPCKDV CECDKAVATC FRDNLDTYKK
     RNIFHPTSSC VKVSTPC