Reviewed, UniProtKB/Swiss-Prot P22029 (BOTA_BOTJA)

Names and origin

Protein names	Recommended name:     Botrocetin subunit alpha Alternative name(s):     Platelet coagglutinin
Organism	Bothrops jararaca (Jararaca)
Taxonomic identifier	8724 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Bothrops

Protein attributes

Sequence length	133 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Two-chain botrocetin forms an activated complex with vWF, and the complex then binds to platelet GPIb, resulting in platelet agglutination. There are two distinct forms of the von Willebrand factor-dependent platelet coagglutinin. The dimeric form is 34-times more active than the one-chain botrocetin in promoting vWF binding to platelets.
Subunit structure	Heterodimer of subunits alpha and beta; disulfide-linked. Botrocetin and vWF form a soluble complex. Ref.1
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Sequence similarities	Contains 1 C-type lectin domain.

Ontologies

Keywords
Cellular component	Secreted
Ligand	Lectin
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	sugar binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 133

133

Botrocetin subunit alpha

PRO_0000046697

Regions

Domain

9 – 129

121

C-type lectin

Amino acid modifications

Disulfide bond

2 ↔ 13

Ref.1

Disulfide bond

30 ↔ 128

Ref.1

Disulfide bond

80

Interchain (with C-75 in beta chain) Ref.1

Disulfide bond

103 ↔ 120

Ref.1

Secondary structure

1

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133

Helix Strand Turn

Details...

Beta strand

7 – 9

3

Beta strand

12 – 21

10

Helix

23 – 33

11

Helix

48 – 59

12

Beta strand

66 – 73

8

Beta strand

76 – 80

5

Helix

97 – 99

3

Beta strand

103 – 107

5

Turn

108 – 111

4

Beta strand

114 – 118

5

Beta strand

124 – 130

7

Sequences

	Sequence		Length	Mass (Da)
	P22029-1 [UniParc]. Last modified July 1, 1993. Version 2. Checksum: E4CF4502946AC74B	FASTA	133	15,215
	10 20 30 40 50 60 DCPSGWSSYE GNCYKFFQQK MNWADAERFC SEQAKGGHLV SIKIYSKEKD FVGDLVTKNI 70 80 90 100 110 120 QSSDLYAWIG LRVENKEKQC SSEWSDGSSV SYENVVERTV KKCFALEKDL GFVLWINLYC 130 AQKNPFVCKS PPP

References

[1]	"Primary structure of two-chain botrocetin, a von Willebrand factor modulator purified from the venom of Bothrops jararaca." Usami Y., Fujimura Y., Suzuki M., Ozeki Y., Nishio K., Fukui H., Titani K. Proc. Natl. Acad. Sci. U.S.A. 90:928-932(1993) [PubMed: 8430107] [Abstract] Cited for: PROTEIN SEQUENCE, DISULFIDE BONDS. Tissue: Venom.
[2]	"Isolation and chemical characterization of two structurally and functionally distinct forms of botrocetin, the platelet coagglutinin isolated from the venom of Bothrops jararaca." Fujimura Y., Titani K., Usami Y., Suzuki M., Oyama R., Matsui T., Fukui H., Sugimoto M., Ruggeri Z.M. Biochemistry 30:1957-1964(1991) [PubMed: 1993206] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-40. Tissue: Venom.
[3]	"Structural basis of von Willebrand factor activation by the snake toxin botrocetin." Fukuda K., Doggett T.A., Bankston L.A., Cruz M.A., Diacovo T.G., Liddington R.C. Structure 10:943-950(2002) [PubMed: 12121649] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

A47267.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FVU	X-ray	1.80	A/C	1-133	[»]
1IJK	X-ray	2.60	B	1-133	[»]
1U0N	X-ray	2.95	B	1-133	[»]
1U0O	X-ray	2.70	A	1-133	[»]

ModBase

Search...

Phylogenomic databases

HOVERGEN

P22029.

Family and domain databases

InterPro

IPR002353. AntifreezeII.
IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
[Graphical view]

Gene3D

G3DSA:3.10.100.10. C-type_lectin-like. 1 hit.

Pfam

PF00059. Lectin_C. 1 hit.
[Graphical view]

PRINTS

PR00356. ANTIFREEZEII.

SMART

SM00034. CLECT. 1 hit.
[Graphical view]

PROSITE

PS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

BOTA_BOTJA

Accession

Primary (citable) accession number: P22029

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	July 1, 1993
Last modified:	November 24, 2009
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)