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P80029 (CRC1_HOMGA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Crustacyanin-C1 subunit
OrganismHomarus gammarus (European lobster) (Homarus vulgaris)
Taxonomic identifier6707 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaCrustaceaMalacostracaEumalacostracaEucaridaDecapodaPleocyemataAstacideaNephropoideaNephropidaeHomarus

Protein attributes

Sequence length181 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Secretedextracellular space.

Tissue specificity

Found in the carapace.

Sequence similarities

Belongs to the calycin superfamily. Lipocalin family.

Ontologies

Keywords
   Biological processTransport
   Cellular componentSecreted
   LigandPigment
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processtransport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpigment binding

Inferred from electronic annotation. Source: UniProtKB-KW

small molecule binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 181181Crustacyanin-C1 subunit
PRO_0000201011

Amino acid modifications

Disulfide bond12 ↔ 121
Disulfide bond51 ↔ 173
Disulfide bond117 ↔ 150

Secondary structure

.............................. 181
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P80029 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 6A05C7CBA3498EE8

FASTA18120,667
        10         20         30         40         50         60 
DKIPDFVVPG KCASVDRNKL WAEQTPNRNS YAGVWYQFAL TNNPYQLIEK CVRNEYSFDG 

        70         80         90        100        110        120 
KQFVIKSTGI AYDGNLLKRN GKLYPNPFGE PHLSIDYENS FAAPLVILET DYSNYACLYS 

       130        140        150        160        170        180 
CIDYNFGYHS DFSFIFSRSA NLADQYVKKC EAAFKNINVD TTRFVKTVQG SSCPYDTQKT 


L 

« Hide

References

[1]"Complete sequence and model for the C1 subunit of the carotenoprotein, crustacyanin, and model for the dimer, beta-crustacyanin, formed from the C1 and A2 subunits with astaxanthin."
Keen J.N., Caceres I., Eliopoulos E.E., Zagalsky P.F., Findlay J.B.C.
Eur. J. Biochem. 202:31-40(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[2]"The C1 subunit of alpha-crustacyanin: the de novo phasing of the crystal structure of a 40 kDa homodimeric protein using the anomalous scattering from S atoms combined with direct methods."
Gordon E.J., Leonard G.A., McSweeney S., Zagalsky P.F.
Acta Crystallogr. D 57:1230-1237(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF HOMODIMER.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Squeeze me - Issue 26 of September 2002

Cross-references

Sequence databases

PIRS19534.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H91X-ray1.40A/B2-180[»]
1I4UX-ray1.15A/B1-181[»]
1OBQX-ray1.85A/B1-181[»]
1OBUX-ray2.00A/B1-181[»]
1S2PX-ray1.30A/B1-181[»]
4ALOX-ray2.37A/B1-180[»]
ProteinModelPortalP80029.
SMRP80029. Positions 1-181.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.40.128.20. 1 hit.
InterProIPR012674. Calycin.
IPR011038. Calycin-like.
IPR003057. Invtbrt_color.
IPR002345. Lipocalin.
IPR022271. Lipocalin_ApoD.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PIRSFPIRSF036893. Lipocalin_ApoD. 1 hit.
PRINTSPR01273. INVTBRTCOLOR.
PR00179. LIPOCALIN.
SUPFAMSSF50814. SSF50814. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP80029.

Entry information

Entry nameCRC1_HOMGA
AccessionPrimary (citable) accession number: P80029
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: February 19, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references