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Protein

Crustacyanin-A2 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-A2 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 – 174174Crustacyanin-A2 subunitPRO_0000201010Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi12 ↔ 1191 Publication
Disulfide bondi46 ↔ 1701 Publication

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 C2.1 Publication

Protein-protein interaction databases

MINTiMINT-242150.

Structurei

Secondary structure

1
174
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 104Combined sources
Turni23 – 264Combined sources
Beta strandi28 – 358Combined sources
Beta strandi45 – 5410Combined sources
Turni55 – 584Combined sources
Beta strandi59 – 679Combined sources
Beta strandi69 – 713Combined sources
Beta strandi73 – 764Combined sources
Beta strandi79 – 813Combined sources
Beta strandi90 – 945Combined sources
Beta strandi96 – 983Combined sources
Beta strandi101 – 1088Combined sources
Beta strandi110 – 12112Combined sources
Beta strandi123 – 13614Combined sources
Beta strandi139 – 1413Combined sources
Helixi142 – 15413Combined sources
Helixi158 – 1603Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GKAX-ray3.23B1-174[»]
SMRiP80007. Positions 1-174.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80007.

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.
IPR022272. Lipocalin_CS.
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.
PROSITEiPS00213. LIPOCALIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P80007-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
DGIPSFVTAG KCASVANQDN FDLRRYAGRW YQTHIIENAY QPVTRCIHSN
60 70 80 90 100
YEYSTNDYGF KVTTAGFNPN DEYLKIDFKV YPTKEFPAAH MLIDAPSVFA
110 120 130 140 150
APYEVIETDY ETYSCVYSCI TTDNYKSEFA FVFSRTPQTS GPAVEKTAAV
160 170
FNKNGVEFSK FVPVSHTAEC VYRA
Length:174
Mass (Da):19,670
Last modified:May 1, 1991 - v1
Checksum:iAC47FAA650C5E44E
GO

Sequence databases

PIRiS15391.

Cross-referencesi

Web resourcesi

Protein Spotlight

Squeeze me - Issue 26 of September 2002

Sequence databases

PIRiS15391.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GKAX-ray3.23B1-174[»]
SMRiP80007. Positions 1-174.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-242150.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP80007.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR003057. Invtbrt_color.
IPR002345. Lipocalin.
IPR022271. Lipocalin_ApoD.
IPR022272. Lipocalin_CS.
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.
PROSITEiPS00213. LIPOCALIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.23 ANGSTROMS) OF HETERODIMER OF A1 AND A3 IN COMPLEX WITH ASTAXANTHIN, DISULFIDE BONDS.

Entry informationi

Entry nameiCRA2_HOMGA
AccessioniPrimary (citable) accession number: P80007
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: April 1, 2015
This is version 90 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.