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Protein

Ranasmurfin

Gene
N/A
Organism
Polypedates leucomystax (Common tree frog) (Hyla leucomystax)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Cofactori

Zn2+2 PublicationsNote: Binds 1 zinc ion per dimer.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi108 – 1081Zinc; shared with dimeric partner
Metal bindingi112 – 1121Zinc; via tele nitrogen; shared with dimeric partner

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Ranasmurfin
Alternative name(s):
RSF-1
OrganismiPolypedates leucomystax (Common tree frog) (Hyla leucomystax)
Taxonomic identifieri68444 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaRanoideaRhacophoridaeRhacophorinaePolypedates

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 113113RanasmurfinPRO_0000332964Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki2 ↔ 31Lysine tyrosylquinone (Tyr-Lys)1 Publication
Modified residuei2 – 212',4',5'-topaquinone1 Publication
Disulfide bondi4 ↔ 621 Publication
Modified residuei9 – 91Aminomalonic acid (Ser); in chain B1 Publication
Disulfide bondi17 ↔ 65In chain A1 Publication
Cross-linki17 ↔ 65S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys); in chain B
Cross-linki30 ↔ 108Lysine tyrosylquinone (Lys-Tyr)1 Publication
Disulfide bondi37 ↔ 1011 Publication
Modified residuei65 – 651Cysteine sulfenic acid (-SOH); in chain B2 Publications
Modified residuei108 – 10812',4',5'-topaquinone1 Publication
Cross-linki108 – 1085'-tyrosyl-5'-aminotyrosine (Tyr-Tyr) (interchain with Y-108)

Keywords - PTMi

Disulfide bond, LTQ, Oxidation, TPQ

Expressioni

Tissue specificityi

Foam nest.1 Publication

Interactioni

Subunit structurei

Homodimer. The two chains, designated A and B, differ in their modifications, but not, it is thought, in their sequence.3 Publications

Structurei

Secondary structure

1
113
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 248Combined sources
Helixi26 – 4015Combined sources
Helixi42 – 443Combined sources
Helixi46 – 6318Combined sources
Helixi76 – 783Combined sources
Helixi79 – 9012Combined sources
Helixi94 – 963Combined sources
Helixi97 – 10711Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VH3X-ray1.16A/B1-113[»]
ProteinModelPortaliP85511.
SMRiP85511. Positions 3-112.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP85511.

Sequencei

Sequence statusi: Complete.

P85511-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AYACSFPPSE IPGSKECLAE ALQKHQGFKK KSYALICAYL NYKEDAENYE
60 70 80 90 100
RAAEDFDSAV KCTGCKEGVD LHEGNPELIE EGFEKFLASL KIDRKALGSL
110
CTLFQKLYAI PHN
Length:113
Mass (Da):12,598
Last modified:April 29, 2008 - v1
Checksum:i2AE528C28C856EA7
GO

Cross-referencesi

Web resourcesi

Protein Spotlight

About the blues - Issue 103 of March 2009

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VH3X-ray1.16A/B1-113[»]
ProteinModelPortaliP85511.
SMRiP85511. Positions 3-112.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP85511.

Family and domain databases

ProtoNetiSearch...

Publicationsi

  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 nest1 Publication.
  2. 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, OXIDATION AT CYS-65, CROSS-LINKS, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiRANSM_POLLE
AccessioniPrimary (citable) accession number: P85511
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 29, 2008
Last modified: January 7, 2015
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

After isolation, the blue protein turns green on exposure to air and sunlight.1 Publication

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

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.