ID   SL5_BITAR               Reviewed;         152 AA.
AC   Q6X5T3;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Snaclec 5;
DE   AltName: Full=C-type lectin 5;
DE            Short=CTL-5;
DE   Flags: Precursor;
OS   Bitis arietans (African puff adder).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Bitis.
OX   NCBI_TaxID=8692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=14557069; DOI=10.1016/s0378-1119(03)00716-9;
RA   Harrison R.A., Oliver J., Hasson S.S., Bharati K., Theakston R.D.G.;
RT   "Novel sequences encoding venom C-type lectins are conserved in
RT   phylogenetically and geographically distinct Echis and Bitis viper
RT   species.";
RL   Gene 315:95-102(2003).
RN   [2]
RP   PROTEIN SEQUENCE OF 24-39, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=16786436; DOI=10.1007/s00239-005-0268-z;
RA   Juarez P., Wagstaff S.C., Oliver J., Sanz L., Harrison R.A., Calvete J.J.;
RT   "Molecular cloning of disintegrin-like transcript BA-5A from a Bitis
RT   arietans venom gland cDNA library: a putative intermediate in the evolution
RT   of the long-chain disintegrin bitistatin.";
RL   J. Mol. Evol. 63:142-152(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; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Shows greater sequence similarity to the alpha than beta
CC       subunits compared to other heterodimer snaclecs.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   EMBL; AY254327; AAQ01208.1; -; mRNA.
DR   AlphaFoldDB; Q6X5T3; -.
DR   SMR; Q6X5T3; -.
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; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 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   Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:16786436"
FT   CHAIN           24..152
FT                   /note="Snaclec 5"
FT                   /id="PRO_0000355245"
FT   DOMAIN          34..149
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        27..38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        55..148
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        100
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        123..140
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   152 AA;  17255 MW;  78AB99D138108149 CRC64;
     MGRFIFLSSG LLVVFLSLSG TGADFQCPSE WSAYGQHCYR AFKYEKSWAE AEKFCMEQAN
     DGHLVSIQSI KEANFVAKLV SGIIAYIWIG LRDRRKEQQC TSEWNDGSKV TYVNWREGES
     QMCQVLAIWS GFKNWVNTDC ASHNPFVCKS PA