PA2HA_VIPRE
ID PA2HA_VIPRE Reviewed; 23 AA.
AC P0DKL7;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 25-MAY-2022, entry version 11.
DE RecName: Full=Basic phospholipase A2 homolog Vur-S49 analog;
DE Short=svPLA2 homolog;
DE Flags: Fragment;
OS Vipera renardi (Steppe viper) (Vipera ursinii renardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX NCBI_TaxID=927686;
RN [1]
RP PROTEIN SEQUENCE, MASS SPECTROMETRY, CIRCULAR DICHROISM, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Venom;
RX PubMed=21185324; DOI=10.1016/j.toxicon.2010.12.012;
RA Tsai I.-H., Wang Y.M., Cheng A.C., Starkov V., Osipov A., Nikitin I.,
RA Makarova Y., Ziganshin R., Utkin Y.;
RT "cDNA cloning, structural, and functional analyses of venom phospholipases
RT A and a Kunitz-type protease inhibitor from steppe viper Vipera ursinii
RT renardi.";
RL Toxicon 57:332-341(2011).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21185324}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:21185324}.
CC -!- PTM: Contains 7 disulfide bonds. {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=13946; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21185324};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC {ECO:0000305}.
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DR AlphaFoldDB; P0DKL7; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Secreted; Toxin.
FT CHAIN 1..>23
FT /note="Basic phospholipase A2 homolog Vur-S49 analog"
FT /id="PRO_0000419642"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 23
SQ SEQUENCE 23 AA; 2610 MW; 939E1FE80043B561 CRC64;
SVLEIGLMLQ EETEKNPKTS YSI