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Protein

Crustacyanin-C1 subunit

Gene
N/A
Organism
Homarus gammarus (European lobster) (Homarus vulgaris)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Binds the carotenoid astaxanthin (AXT) which provides the blue coloration to the carapace of the lobster.

GO - Molecular functioni

  1. pigment binding Source: UniProtKB-KW
  2. small molecule binding Source: InterPro

GO - Biological processi

  1. transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Pigment

Names & Taxonomyi

Protein namesi
Recommended name:
Crustacyanin-C1 subunit
OrganismiHomarus gammarus (European lobster) (Homarus vulgaris)
Taxonomic identifieri6707 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaCrustaceaMalacostracaEumalacostracaEucaridaDecapodaPleocyemataAstacideaNephropoideaNephropidaeHomarus

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 181181Crustacyanin-C1 subunitPRO_0000201011Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi12 ↔ 121
Disulfide bondi51 ↔ 173
Disulfide bondi117 ↔ 150

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Found in the carapace.

Interactioni

Subunit structurei

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.

Structurei

Secondary structure

1
181
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 104Combined sources
Helixi17 – 248Combined sources
Helixi25 – 273Combined sources
Helixi28 – 314Combined sources
Beta strandi33 – 419Combined sources
Beta strandi48 – 5811Combined sources
Beta strandi63 – 719Combined sources
Beta strandi76 – 8510Combined sources
Beta strandi91 – 977Combined sources
Beta strandi102 – 1109Combined sources
Beta strandi112 – 12312Combined sources
Beta strandi127 – 14115Combined sources
Helixi144 – 15613Combined sources
Helixi161 – 1633Combined sources
Beta strandi164 – 1663Combined sources
Helixi175 – 1784Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP80029.
SMRiP80029. Positions 1-181.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80029.

Family & Domainsi

Sequence similaritiesi

Belongs to the calycin superfamily. Lipocalin family.Curated

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR003057. Invtbrt_color.
IPR002345. Lipocalin.
IPR022271. Lipocalin_ApoD.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PIRSFiPIRSF036893. Lipocalin_ApoD. 1 hit.
PRINTSiPR01273. INVTBRTCOLOR.
PR00179. LIPOCALIN.
SUPFAMiSSF50814. SSF50814. 1 hit.

Sequencei

Sequence statusi: Complete.

P80029-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
DKIPDFVVPG KCASVDRNKL WAEQTPNRNS YAGVWYQFAL TNNPYQLIEK
60 70 80 90 100
CVRNEYSFDG KQFVIKSTGI AYDGNLLKRN GKLYPNPFGE PHLSIDYENS
110 120 130 140 150
FAAPLVILET DYSNYACLYS CIDYNFGYHS DFSFIFSRSA NLADQYVKKC
160 170 180
EAAFKNINVD TTRFVKTVQG SSCPYDTQKT L
Length:181
Mass (Da):20,667
Last modified:August 1, 1991 - v1
Checksum:i6A05C7CBA3498EE8
GO

Sequence databases

PIRiS19534.

Cross-referencesi

Web resourcesi

Protein Spotlight

Squeeze me - Issue 26 of September 2002

Sequence databases

PIRiS19534.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP80029.
SMRiP80029. Positions 1-181.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP80029.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR003057. Invtbrt_color.
IPR002345. Lipocalin.
IPR022271. Lipocalin_ApoD.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PIRSFiPIRSF036893. Lipocalin_ApoD. 1 hit.
PRINTSiPR01273. INVTBRTCOLOR.
PR00179. LIPOCALIN.
SUPFAMiSSF50814. SSF50814. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiCRC1_HOMGA
AccessioniPrimary (citable) accession number: P80029
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: January 7, 2015
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.