ID   SLB_DABPA               Reviewed;         125 AA.
AC   P0DJL5;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Snaclec VP12 subunit B;
OS   Daboia palaestinae (Palestine viper) (Vipera palaestinae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX   NCBI_TaxID=1170828;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=19502781; DOI=10.4161/cbt.8.15.8999;
RA   Staniszewska I., Walsh E.M., Rothman V.L., Gaathon A., Tuszynski G.P.,
RA   Calvete J.J., Lazarovici P., Marcinkiewicz C.;
RT   "Effect of VP12 and viperistatin on inhibition of collagen-receptor-
RT   dependent melanoma metastasis.";
RL   Cancer Biol. Ther. 8:1507-1516(2009).
CC   -!- FUNCTION: Inhibits integrin alpha-2/beta-1- (ITGA2/ITGB1) dependent
CC       melanoma metastasis. {ECO:0000269|PubMed:19502781}.
CC   -!- SUBUNIT: Heterodimer of subunits alpha and beta; disulfide-linked.
CC       {ECO:0000269|PubMed:19502781}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   AlphaFoldDB; P0DJL5; -.
DR   SMR; P0DJL5; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW   Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT   CHAIN           1..125
FT                   /note="Snaclec VP12 subunit B"
FT                   /id="PRO_0000422554"
FT   DOMAIN          11..122
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        4..15
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        32..121
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        77
FT                   /note="Interchain (with C-85 in subunit beta)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        98..113
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   125 AA;  15157 MW;  7AAB69482C4992A9 CRC64;
     DQDCLPGWSY FEKYCYKVFQ VKKNWEDAEK FCTEEVKDGH LISLHSNEEV EFMTSLAFPI
     LKYDIVWMGL RNFWRDCPWK WSDDAKLDYK AWSDEPNCYG AMTTDYQWLR WNCNDPRYFV
     CKSPA