SLA2_MACLB
ID SLA2_MACLB Reviewed; 156 AA.
AC B4XSZ2;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Snaclec A2;
DE AltName: Full=C-type lectin A2;
DE Flags: Precursor;
OS Macrovipera lebetina (Levantine viper) (Vipera lebetina).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Macrovipera.
OX NCBI_TaxID=8709;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=19059426; DOI=10.1016/j.toxicon.2008.11.006;
RA Jebali J., Bazaa A., Sarray S., Benhaj K., Karboul A., El Ayeb M.,
RA Marrakchi N., Gargouri A.;
RT "C-type lectin protein isoforms of Macrovipera lebetina: cDNA cloning and
RT genetic diversity.";
RL Toxicon 53:228-237(2009).
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 {ECO:0000250}.
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; EU085454; ABW82664.1; -; mRNA.
DR AlphaFoldDB; B4XSZ2; -.
DR SMR; B4XSZ2; -.
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 2: Evidence at transcript level;
KW Disulfide bond; Hemostasis impairing toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..156
FT /note="Snaclec A2"
FT /id="PRO_0000356318"
FT DOMAIN 34..155
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..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 106
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 129..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 156 AA; 17864 MW; 0D9E58CF00311F0D CRC64;
MGRLISVSFG LLVVFLSLSG TGADQDCLPG WSSHEGHCYK VFNLDKTWED AEKFCTEQAN
SGHLVSIDSK KEANFVAELV SQNIKETRRT DFVWIGLRAE DKRQHCSSEW SDGSSINYQN
WIEAESKKCL GLEKQTRYRK WVNLNCGQPY RFTCEI