ID   SLB_PHIOL               Reviewed;         156 AA.
AC   Q09GK0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Snaclec subunit B;
DE   AltName: Full=C-type lectin subunit B;
DE   Flags: Precursor;
OS   Philodryas olfersii (Green snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Dipsadidae; Philodryas.
OX   NCBI_TaxID=120305;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ABI74695.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Venom gland {ECO:0000269|PubMed:16857193};
RX   PubMed=16857193; DOI=10.1016/j.febslet.2006.07.010;
RA   Ching A.T.C., Rocha M.M.T., Paes Leme A.F., Pimenta D.C., Furtado M.F.D.,
RA   Serrano S.M.T., Ho P.L., Junqueira-de-Azevedo I.L.M.;
RT   "Some aspects of the venom proteome of the Colubridae snake Philodryas
RT   olfersii revealed from a Duvernoy's (venom) gland transcriptome.";
RL   FEBS Lett. 580:4417-4422(2006).
RN   [2]
RP   ERRATUM OF PUBMED:16857193.
RA   Ching A.T.C., Rocha M.M.T., Paes Leme A.F., Pimenta D.C., Furtado M.F.D.,
RA   Serrano S.M.T., Ho P.L., Junqueira-de-Azevedo I.L.M.;
RL   FEBS Lett. 580:5122-5123(2006).
CC   -!- FUNCTION: Interferes with one step of hemostasis (modulation of
CC       platelet aggregation, or coagulation cascade, for example).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of subunits A and B; disulfide-linked.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16857193}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:16857193}.
CC   -!- MISCELLANEOUS: Calcium is required for ligand binding.
CC       {ECO:0000250|UniProtKB:P23807}.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   EMBL; DQ912658; ABI74695.1; -; mRNA.
DR   AlphaFoldDB; Q09GK0; -.
DR   SMR; Q09GK0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Disulfide bond; Hemostasis impairing toxin; Lectin; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..156
FT                   /note="Snaclec subunit B"
FT                   /id="PRO_0000315895"
FT   DOMAIN          32..145
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        25..36
FT                   /evidence="ECO:0000250|UniProtKB:P23807,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        53..144
FT                   /evidence="ECO:0000250|UniProtKB:P23807,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        98
FT                   /note="Interchain (with C-102 in subunit A)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        119..136
FT                   /evidence="ECO:0000250|UniProtKB:P23807,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   156 AA;  17768 MW;  89208CADA0417F92 CRC64;
     MGRSIFVNLG LLVVAFSLRG SEADCPSGWS SYDKYCYKVF DERKNWDEAE SFCMEQKTGS
     HLASILSSEE GSYVANLAFK RVKHPSMWIG LSNIWNQCSW QWSDGSSLGY EAWVEGPDCV
     MMRLQPGFID WYSVECKSTL PFTCKFLAKR EDPAPE