ID   SLA_CROHD               Reviewed;         127 AA.
AC   P81508;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2003, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Snaclec CHH-B subunit alpha;
OS   Crotalus horridus (Timber rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=35024;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Venom;
RX   PubMed=8823201; DOI=10.1021/bi960704e;
RA   Andrews R.K., Kroll M.H., Ward C.M., Rose J.W., Scarborough R.M.,
RA   Smith A.I., Lopez J.A., Berndt M.C.;
RT   "Binding of a novel 50-kilodalton alboaggregin from Trimeresurus albolabris
RT   and related viper venom proteins to the platelet membrane glycoprotein Ib-
RT   IX-V complex. Effect on platelet aggregation and glycoprotein Ib-mediated
RT   platelet activation.";
RL   Biochemistry 35:12629-12639(1996).
CC   -!- FUNCTION: Binds to the subunit GPIbalpha (GP1BA) of the platelet
CC       GPIb/V/IX receptor system. It inhibits ristocetin- and vWF-induced
CC       platelet aggregation in platelet-rich plasma by inhibiting the binding
CC       of vWF to GPIbalpha. {ECO:0000269|PubMed:8823201}.
CC   -!- SUBUNIT: Heterodimer of subunits alpha and beta; disulfide-linked.
CC       {ECO:0000269|PubMed:8823201}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8823201}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:8823201}.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   AlphaFoldDB; P81508; -.
DR   SMR; P81508; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044477; P:envenomation resulting in negative regulation of platelet aggregation in another organism; IDA:UniProtKB.
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   Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT   CHAIN           1..127
FT                   /note="Snaclec CHH-B subunit alpha"
FT                   /id="PRO_0000046699"
FT   DOMAIN          11..121
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..120
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        81
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        95..112
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   127 AA;  15162 MW;  B5DA100D383E3547 CRC64;
     DLECPSGWSS YDRYCYKPFK QEMTWADAER FCSEQAKGRH LLSVETALEA SFVDNVLYAN
     KEYLTRYIWI GLRVQNKGQP CSSIYSENLV DPFDCFMVSR DTRLREWFKV DCEQQHSFIC
     KFTRPRR