ID   SLOA_PROMU              Reviewed;         158 AA.
AC   Q6TPH0;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Snaclec mucrocetin subunit alpha;
DE   Flags: Precursor;
OS   Protobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX   NCBI_TaxID=103944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-49, X-RAY
RP   CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 24-158, SUBUNIT, AND DISULFIDE BONDS.
RC   STRAIN=Taiwan; TISSUE=Venom, and Venom gland;
RX   PubMed=14613481; DOI=10.1042/bj20031507;
RA   Huang K.-F., Ko T.-P., Hung C.-C., Chu J., Wang A.H.-J., Chiou S.-H.;
RT   "Crystal structure of a platelet-agglutinating factor isolated from the
RT   venom of Taiwan habu (Trimeresurus mucrosquamatus).";
RL   Biochem. J. 378:399-407(2004).
CC   -!- FUNCTION: Platelet-agglutinating factor that acts in a vWF-independent
CC       manner. Binds specifically to platelet GPIbalpha (GP1BA) to a distinct
CC       binding site from that of flavocetin-A.
CC   -!- SUBUNIT: Tetramer of heterodimers of alpha and beta subunits
CC       (alphabeta)(4); disulfide-linked. {ECO:0000269|PubMed:14613481}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY390533; AAQ93686.1; -; mRNA.
DR   PDB; 1V4L; X-ray; 2.80 A; A/C/E=24-158.
DR   PDBsum; 1V4L; -.
DR   AlphaFoldDB; Q6TPH0; -.
DR   SMR; Q6TPH0; -.
DR   EvolutionaryTrace; Q6TPH0; -.
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   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Hemostasis impairing toxin; Platelet aggregation activating toxin;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:14613481"
FT   CHAIN           24..158
FT                   /note="Snaclec mucrocetin subunit alpha"
FT                   /id="PRO_0000355297"
FT   DOMAIN          34..153
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        27..38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:14613481"
FT   DISULFID        55..152
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:14613481"
FT   DISULFID        104
FT                   /note="Interchain (with C-100 in subunit beta of
FT                   heterodimeric partner)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:14613481"
FT   DISULFID        127..144
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:14613481"
FT   DISULFID        158
FT                   /note="Interchain (with C-26 in subunit beta of tetrameric
FT                   partner)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:14613481"
FT   STRAND          32..34
FT                   /evidence="ECO:0007829|PDB:1V4L"
FT   STRAND          37..46
FT                   /evidence="ECO:0007829|PDB:1V4L"
FT   HELIX           48..57
FT                   /evidence="ECO:0007829|PDB:1V4L"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:1V4L"
FT   HELIX           70..81
FT                   /evidence="ECO:0007829|PDB:1V4L"
FT   STRAND          89..97
FT                   /evidence="ECO:0007829|PDB:1V4L"
FT   STRAND          101..104
FT                   /evidence="ECO:0007829|PDB:1V4L"
FT   HELIX           121..123
FT                   /evidence="ECO:0007829|PDB:1V4L"
FT   STRAND          127..131
FT                   /evidence="ECO:0007829|PDB:1V4L"
FT   STRAND          138..142
FT                   /evidence="ECO:0007829|PDB:1V4L"
FT   STRAND          148..154
FT                   /evidence="ECO:0007829|PDB:1V4L"
SQ   SEQUENCE   158 AA;  18129 MW;  419ABE2F0344B9CA CRC64;
     MGRFIFVSFG LLVVFLSLSG TGADFDCIPG WSAYDRYCYQ AFSEPKNWED AESFCEEGVK
     TSHLVSIESS GEGDFVAQLV AEKIKTSFQY VWIGLRIQNK EQQCRSEWSD ASSVNYENLY
     KQSSKKCYAL KKGTELRTWF NVYCGRENPF VCKYTPEC