P09464 (BBP_PIEBR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Bilin-binding protein Short name=BBP
Organism	Pieris brassicae (White butterfly) (Large white butterfly)
Taxonomic identifier	7116 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Lepidoptera › Glossata › Ditrysia › Papilionoidea › Pieridae › Pierinae › Pieris

Protein attributes

Sequence length	189 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This protein binds the blue pigments bilins. Ref.2
Subunit structure	Homotetramer. Ref.3
Subcellular location	Secreted Ref.2.
Tissue specificity	Hemolymph.
Sequence similarities	Belongs to the calycin superfamily. Lipocalin family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Bile pigment Chromophore Pigment
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	protein-chromophore linkage Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	pigment binding Inferred from electronic annotation. Source: UniProtKB-KW transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 15

15

Ref.2

Chain

16 – 189

174

Bilin-binding protein

PRO_0000017880

Amino acid modifications

Disulfide bond

23 ↔ 130

Ref.2

Disulfide bond

57 ↔ 185

Ref.2

Secondary structure

1

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189

Helix Strand Turn

Details...

Beta strand

17 – 22

6

Helix

34 – 36

3

Beta strand

39 – 46

8

Turn

51 – 54

4

Beta strand

56 – 64

9

Beta strand

69 – 77

9

Beta strand

80 – 92

13

Beta strand

96 – 105

10

Beta strand

108 – 119

12

Beta strand

121 – 133

13

Turn

134 – 137

4

Beta strand

138 – 151

14

Helix

154 – 166

13

Helix

172 – 174

3

Helix

182 – 185

4

Sequences

	Sequence		Length	Mass (Da)
	P09464 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: DDC2B53072E63412	FASTA	189	21,306
	10 20 30 40 50 60 MQYLIVLALV AAASANVYHD GACPEVKPVD NFDWSNYHGK WWEVAKYPNS VEKYGKCGWA 70 80 90 100 110 120 EYTPEGKSVK VSNYHVIHGK EYFIEGTAYP VGDSKIGKIY HKLTYGGVTK ENVFNVLSTD 130 140 150 160 170 180 NKNYIIGYYC KYDEDKKGHQ DFVWVLSRSK VLTGEAKTAV ENYLIGSPVV DSQKLVYSDF SEAACKVNN

References

[1]	"The bilin-binding protein of Pieris brassicae. cDNA sequence and regulation of expression reveal distinct features of this insect pigment protein." Schmidt F.S., Skerra A. Eur. J. Biochem. 219:855-863(1994) [PubMed: 8112337] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The complete amino-acid sequence of the bilin-binding protein from Pieris brassicae and its similarity to a family of serum transport proteins like the retinol-binding proteins." Suter F., Kayser H., Zuber H. Biol. Chem. Hoppe-Seyler 369:497-505(1988) [PubMed: 3202956] [Abstract] Cited for: PROTEIN SEQUENCE OF 16-189, DISULFIDE BONDS, FUNCTION, SUBCELLULAR LOCATION.
[3]	"Molecular structure of the bilin binding protein (BBP) from Pieris brassicae after refinement at 2.0-A resolution." Huber M., Schneider M., Mayr I., Mueller R., Deutzmann R., Suter F., Zuber H., Falk H., Kayser H. J. Mol. Biol. 198:499-513(1987) [PubMed: 3430616] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X76568 mRNA. Translation: CAA54063.1.

PIR

S41410.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BBP	X-ray	2.00	A/B/C/D	16-188	[»]
1KXO	X-ray	1.80	A	17-189	[»]
1LKE	X-ray	1.90	A	17-189	[»]
1LNM	X-ray	1.90	A	17-189	[»]
1N0S	X-ray	2.00	A/B	17-189	[»]
1T0V	NMR	-	A	17-189	[»]

ProteinModelPortal

P09464.

SMR

P09464. Positions 16-188.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR012674. Calycin.
IPR011038. Calycin-like.
IPR003057. Invtbrt_color.
IPR022271. Lipocalin_ApoD.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[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.

SUPFAM

SSF50814. Calycin. 1 hit.

PROSITE

PS00213. LIPOCALIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00693. Fluorescein.

Entry information

Entry name

BBP_PIEBR

Accession

Primary (citable) accession number: P09464

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	October 1, 1996
Last modified:	May 31, 2011
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)