SLOB_PROMU
ID SLOB_PROMU Reviewed; 148 AA.
AC Q6TPG9;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Snaclec mucrocetin subunit beta;
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 24-43, X-RAY
RP CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 24-148, 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}.
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DR EMBL; AY390534; AAQ93687.1; -; mRNA.
DR PDB; 1V4L; X-ray; 2.80 A; B/D/F=24-148.
DR PDBsum; 1V4L; -.
DR AlphaFoldDB; Q6TPG9; -.
DR SMR; Q6TPG9; -.
DR EvolutionaryTrace; Q6TPG9; -.
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:0000255"
FT CHAIN 24..148
FT /note="Snaclec mucrocetin subunit beta"
FT /id="PRO_0000355298"
FT DOMAIN 34..145
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 26
FT /note="Interchain (with C-158 in subunit alpha of
FT tetrameric partner)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:14613481"
FT DISULFID 27..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:14613481"
FT DISULFID 55..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:14613481"
FT DISULFID 100
FT /note="Interchain (with C-104 in subunit alpha of
FT heterodimeric partner)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:14613481"
FT DISULFID 121..136
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..58
FT /evidence="ECO:0007829|PDB:1V4L"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1V4L"
FT HELIX 70..80
FT /evidence="ECO:0007829|PDB:1V4L"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:1V4L"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1V4L"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1V4L"
FT STRAND 120..129
FT /evidence="ECO:0007829|PDB:1V4L"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:1V4L"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:1V4L"
SQ SEQUENCE 148 AA; 16997 MW; 749A8C88F199561E CRC64;
MGRFIFVSFG LLVVFLSLSG TEAGFCCPLG WSSYDEHCYQ VFQQKINWED AEKFCTQQHR
GSHLVSFHSS EEVDFVVSKT SPILKHDFVW MGLSNVWNEC AKEWSDGTKL DYKAWSGQSD
CITSKTTDNQ WLSMDCSSKR YVVCKFQA