P80007 (CRA2_HOMGA)
Reviewed,
UniProtKB/Swiss-Prot
Last modified
August 10, 2010.
Version 74.
History...
Names and origin
| Protein names | Recommended name: Crustacyanin-A2 subunit |
| Organism | Homarus gammarus (European lobster) (Homarus vulgaris) |
| Taxonomic identifier | 6707 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Arthropoda › Crustacea › Malacostraca › Eumalacostraca › Eucarida › Decapoda › Pleocyemata › Astacidea › Nephropoidea › Nephropidae › Homarus |
Protein attributes
| Sequence length | 174 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Binds the carotenoid astaxanthin (AXT) which provides the blue coloration to the carapace of the lobster. |
| Subunit structure | Oligomer; Can form dimers (beta-crustacyanin); or complexes of 16 subunits (alpha-crustacyanin). There are five types of subunits: A1, A2, A3, C1 and C2. |
| Subcellular location | |
| Tissue specificity | Found in the carapace. |
| Sequence similarities | Belongs to the calycin superfamily. Lipocalin family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transport |
| Cellular component | Secreted |
| Ligand | Pigment |
| PTM | Disulfide bond |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular component | extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | pigment binding Inferred from electronic annotation. Source: UniProtKB-KW transporter activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 174 | 174 | Crustacyanin-A2 subunit | PRO_0000201010 | ||||||||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 12 ↔ 119 | Ref.2 | ||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 46 ↔ 170 | Ref.2 | ||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 7 – 10 | 4 | ||||||||||||||||||||||||||||||||||||||
| Turn | 23 – 26 | 4 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 28 – 35 | 8 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 45 – 54 | 10 | ||||||||||||||||||||||||||||||||||||||
| Turn | 55 – 58 | 4 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 59 – 67 | 9 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 69 – 71 | 3 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 73 – 76 | 4 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 79 – 81 | 3 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 90 – 94 | 5 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 96 – 98 | 3 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 101 – 108 | 8 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 110 – 121 | 12 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 123 – 136 | 14 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 139 – 141 | 3 | ||||||||||||||||||||||||||||||||||||||
| Helix | 142 – 154 | 13 | ||||||||||||||||||||||||||||||||||||||
| Helix | 158 – 160 | 3 | ||||||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Complete sequence and model for the A2 subunit of the carotenoid pigment complex, crustacyanin." Keen J.N., Caceres I., Eliopoulos E.E., Zagalsky P.F., Findlay J.B.C. Eur. J. Biochem. 197:407-417(1991) [PubMed: 2026162] [Abstract] Cited for: PROTEIN SEQUENCE. |
| [2] | "The molecular basis of the coloration mechanism in lobster shell: beta-crustacyanin at 3.2-A resolution." Cianci M., Rizkallah P.J., Olczak A., Raftery J., Chayen N.E., Zagalsky P.F., Helliwell J.R. Proc. Natl. Acad. Sci. U.S.A. 99:9795-9800(2002) [PubMed: 12119396] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.23 ANGSTROMS) OF HETERODIMER OF A1 AND A3 IN COMPLEX WITH ASTAXANTHIN, DISULFIDE BONDS. |
Web resources
| Protein Spotlight Squeeze me - Issue 26 of September 2002 |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| PIR | S15391. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P80007. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| MINT | MINT-242150. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR012674. Calycin. IPR011038. Calycin-like. IPR003057. Invtbrt_color. IPR002345. Lipocalin. IPR022271. Lipocalin_ApoD. IPR022272. Lipocalin_CS. IPR000566. Lipocln_cytosolic_FA-bd. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:2.40.128.20. Calycin. 1 hit. | ||||||||||||
| Pfam | PF00061. Lipocalin. 1 hit. [Graphical view] | ||||||||||||
| PIRSF | PIRSF036893. Lipocalin_ApoD. 1 hit. | ||||||||||||
| PRINTS | PR01273. INVTBRTCOLOR. PR00179. LIPOCALIN. | ||||||||||||
| SUPFAM | SSF50814. Calycin. 1 hit. | ||||||||||||
| PROSITE | PS00213. LIPOCALIN. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | CRA2_HOMGA | ||||||||
| Accession | Primary (citable) accession number: P80007 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| Protein Spotlight Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


