P81397 (RHCA_CALRH) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 60.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Rhodocetin subunit alpha |
| Organism | Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma) |
| Taxonomic identifier | 8717 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Calloselasma |
Protein attributes
| Sequence length | 133 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | A potent inhibitor of collagen-induced platelet aggregation. Individually, neither subunit inhibits platelet aggregation. Both subunits are essential. Ref.1 |
| Subunit structure | Heterodimer of subunits alpha and beta; held together by noncovalent interactions rather than by intersubunit disulfide bridges. Ref.1 |
| Subcellular location | |
| Tissue specificity | Expressed by the venom gland. |
| Sequence similarities | Contains 1 C-type lectin domain. |
| Mass spectrometry | Molecular mass is 15955.90±1.44 Da from positions 1 - 133. Determined by ESI. Ref.1 |
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 | Rhodocetin subunit alpha | PRO_0000046706 | ||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||
| Domain | 1 – 129 | 129 | C-type lectin | |||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||
| Disulfide bond | 2 ↔ 13 | Ref.2 | ||||||||||||||||||||||||||||
| Disulfide bond | 30 ↔ 127 | Ref.2 | ||||||||||||||||||||||||||||
| Disulfide bond | 102 ↔ 119 | Ref.2 | ||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||
| Beta strand | 10 – 21 | 12 | ||||||||||||||||||||||||||||
| Helix | 23 – 31 | 9 | ||||||||||||||||||||||||||||
| Beta strand | 33 – 35 | 3 | ||||||||||||||||||||||||||||
| Helix | 45 – 58 | 14 | ||||||||||||||||||||||||||||
| Turn | 59 – 61 | 3 | ||||||||||||||||||||||||||||
| Beta strand | 64 – 73 | 10 | ||||||||||||||||||||||||||||
| Beta strand | 79 – 83 | 5 | ||||||||||||||||||||||||||||
| Beta strand | 94 – 96 | 3 | ||||||||||||||||||||||||||||
| Beta strand | 100 – 111 | 12 | ||||||||||||||||||||||||||||
| Beta strand | 113 – 117 | 5 | ||||||||||||||||||||||||||||
| Beta strand | 123 – 130 | 8 | ||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Rhodocetin, a novel platelet aggregation inhibitor from the venom of Calloselasma rhodostoma (Malayan pit viper): synergistic and noncovalent interaction between its subunits." Wang R., Kini R.M., Chung M.C.M. Biochemistry 38:7584-7593(1999) [PubMed: 10360956] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT, MASS SPECTROMETRY. Tissue: Venom. |
| [2] | "Structure of rhodocetin reveals noncovalently bound heterodimer interface." Paaventhan P., Kong C., Joseph J.S., Chung M.C., Kolatkar P.R. Protein Sci. 14:169-175(2005) [PubMed: 15576563] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH RHCB, DISULFIDE BONDS. |
| + | Additional computationally mapped references. |
Cross-references
3D structure databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||
| ProteinModelPortal | P81397. | ||||||||||||||||||
| SMR | P81397. Positions 1-132. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| HOVERGEN | HBG004151. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR001304. C-type_lectin. IPR016186. C-type_lectin-like. 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] | ||||||||||||||||||
| SMART | SM00034. CLECT. 1 hit. [Graphical view] | ||||||||||||||||||
| SUPFAM | SSF56436. C-type_lectin_fold. 1 hit. | ||||||||||||||||||
| PROSITE | PS00615. C_TYPE_LECTIN_1. False negative. PS50041. C_TYPE_LECTIN_2. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Entry information
| Entry name | RHCA_CALRH | ||||||||
| Accession | Primary (citable) accession number: P81397 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with