P85511 (RANSM_POLLE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Ranasmurfin Alternative name(s): RSF-1
Organism	Polypedates leucomystax (Common tree frog) (Hyla leucomystax)
Taxonomic identifier	68444 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amphibia › Batrachia › Anura › Neobatrachia › Ranoidea › Rhacophoridae › Rhacophorinae › Polypedates › Polypedates leucomystax species complex

Protein attributes

Sequence length	113 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Cofactor	Binds 1 zinc ion per dimer. Ref.1 Ref.2
Subunit structure	Homodimer. The two chains, designated A and B, differ in their modifications, but not, it is thought, in their sequence. Ref.1 Ref.2 Ref.3
Subcellular location	Secreted.
Tissue specificity	Foam nest. Ref.1
Miscellaneous	After isolation, the blue protein turns green on exposure to air and sunlight. Ref.1

Ontologies

Keywords
Cellular component	Secreted
Ligand	Metal-binding Zinc
PTM	Disulfide bond LTQ Oxidation TPQ
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 113

113

Ranasmurfin

PRO_0000332964

Sites

Metal binding

108

1

Zinc; shared with dimeric partner Ref.1

Metal binding

112

1

Zinc; via tele nitrogen; shared with dimeric partner Ref.1

Amino acid modifications

Modified residue

2

1

2',4',5'-topaquinone Ref.1

Modified residue

9

1

Aminomalonic acid (Ser); in chain B Ref.1

Modified residue

65

1

Cysteine sulfenic acid (-SOH); in chain B Ref.1

Modified residue

108

1

2',4',5'-topaquinone Ref.1

Disulfide bond

4 ↔ 62

Ref.1 Ref.3

Disulfide bond

17 ↔ 65

In chain A Ref.1 Ref.3

Disulfide bond

37 ↔ 101

Ref.1 Ref.3

Cross-link

2 ↔ 31

Lysine tyrosylquinone (Tyr-Lys) Ref.1

Cross-link

17 ↔ 65

S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys); in chain B Ref.1

Cross-link

30 ↔ 108

Lysine tyrosylquinone (Lys-Tyr) Ref.1

Cross-link

108

5'-tyrosyl-5'-aminotyrosine (Tyr-Tyr) (interchain) Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

113

Helix Strand Turn

Details...

Helix

17 – 24

8

Helix

26 – 40

15

Helix

41 – 44

4

Helix

46 – 63

18

Helix

79 – 90

12

Helix

97 – 107

11

Sequences

	Sequence		Length	Mass (Da)
	P85511 [UniParc]. Last modified April 29, 2008. Version 1. Checksum: 2AE528C28C856EA7	FASTA	113	12,598
	10 20 30 40 50 60 AYACSFPPSE IPGSKECLAE ALQKHQGFKK KSYALICAYL NYKEDAENYE RAAEDFDSAV 70 80 90 100 110 KCTGCKEGVD LHEGNPELIE EGFEKFLASL KIDRKALGSL CTLFQKLYAI PHN

References

[1]	"Unusual chromophores and crosslinks in ranasmurfin - a blue protein from the foam nests of a tropical frog." Muse O., Ching R.T.Y., Carter L.G., Johnson K.A., Liu H., Mcmahon S.A., White M.F., Bloch C. Jr., Botting C.H., Walsh M.A., Latiff A.A., Kennedy M.W., Cooper A., Naismith J.H. Submitted (FEB-2008) to UniProtKB Cited for: PROTEIN SEQUENCE, SUBUNIT, TISSUE SPECIFICITY, ZINC BINDING, AMINOMALONIC ACID FORMATION AT SER-9, DISULFIDE BONDS, CROSS-LINK FORMATION. Tissue: Foam nest.
[2]	"Crystallization of ranasmurfin, a blue-coloured protein from Polypedates leucomystax." McMahon S.A., Walsh M.A., Ching R.T.Y., Carter L.G., Dorward M., Johnson K.A., Liu H., Oke M., Bloch C. Jr., Kennedy M.W., Latiff A.A., Cooper A., Taylor G.L., White M.F., Naismith J.H. Acta Crystallogr. F 62:1124-1126(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, ZINC-BINDING, CRYSTALLIZATION.
[3]	"Unusual chromophore and cross-links in ranasmurfin: a blue protein from the foam nests of a tropical frog." Oke M., Ching R.T.Y., Carter L.G., Johnson K.A., Liu H., McMahon S.A., White M.F., Bloch C. Jr., Botting C.H., Walsh M.A., Latiff A.A., Kennedy M.W., Cooper A., Naismith J.H. Angew. Chem. Int. Ed. 47:7853-7856(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) IN COMPLEX WITH ZINC IONS, SUBUNIT, DISULFIDE BONDS, CROSS-LINKS, MASS SPECTROMETRY.

Web resources

Protein Spotlight

About the blues - Issue 103 of March 2009

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VH3	X-ray	1.16	A/B	3-113	[»]

ProteinModelPortal

P85511.

SMR

P85511. Positions 3-112.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

ProtoNet

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Other

EvolutionaryTrace

P85511.

Entry information

Entry name

RANSM_POLLE

Accession

Primary (citable) accession number: P85511

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	April 29, 2008
Last modified:	January 9, 2013
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program