P80029 (CRC1_HOMGA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Crustacyanin-C1 subunit
Organism	Homarus gammarus (European lobster) (Homarus vulgaris)
Taxonomic identifier	6707 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Crustacea › Malacostraca › Eumalacostraca › Eucarida › Decapoda › Pleocyemata › Astacidea › Nephropoidea › Nephropidae › Homarus

Protein attributes

Sequence length	181 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	Secreted › extracellular space.
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)
Biological_process	transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	pigment binding Inferred from electronic annotation. Source: UniProtKB-KW small molecule binding Inferred 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 – 181

181

Crustacyanin-C1 subunit

PRO_0000201011

Amino acid modifications

Disulfide bond

12 ↔ 121

Disulfide bond

51 ↔ 173

Disulfide bond

117 ↔ 150

Secondary structure

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181

Helix Strand Turn

Details...

Beta strand

7 – 10

4

Helix

17 – 24

8

Helix

25 – 27

3

Helix

28 – 31

4

Beta strand

33 – 41

9

Beta strand

48 – 58

11

Beta strand

63 – 71

9

Beta strand

76 – 85

10

Beta strand

91 – 97

7

Beta strand

102 – 110

9

Beta strand

112 – 123

12

Beta strand

127 – 141

15

Helix

144 – 156

13

Helix

161 – 163

3

Beta strand

164 – 166

3

Helix

175 – 178

4

Sequences

	Sequence		Length	Mass (Da)
	P80029 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: 6A05C7CBA3498EE8	FASTA	181	20,667
	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

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

PIR

S19534.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H91	X-ray	1.40	A/B	2-180	[»]
1I4U	X-ray	1.15	A/B	1-181	[»]
1OBQ	X-ray	1.85	A/B	1-181	[»]
1OBU	X-ray	2.00	A/B	1-181	[»]
1S2P	X-ray	1.30	A/B	1-181	[»]
4ALO	X-ray	2.37	A/B	1-180	[»]

ProteinModelPortal

P80029.

SMR

P80029. Positions 1-181.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

2.40.128.20. 1 hit.

InterPro

IPR012674. Calycin.
IPR011038. Calycin-like.
IPR003057. Invtbrt_color.
IPR002345. Lipocalin.
IPR022271. Lipocalin_ApoD.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]

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. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P80029.

Entry information

Entry name

CRC1_HOMGA

Accession

Primary (citable) accession number: P80029

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	April 3, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)