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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)DescriptionActionsGraphical viewLength
Metal bindingi108Zinc; shared with dimeric partner1
Metal bindingi112Zinc; via tele nitrogen; shared with dimeric partner1

GO - Molecular functioni

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

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003329641 – 113RanasmurfinAdd BLAST113

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki2 ↔ 31Lysine tyrosylquinone (Tyr-Lys)1 Publication
Modified residuei22',4',5'-topaquinone1 Publication1
Disulfide bondi4 ↔ 621 Publication
Modified residuei9Aminomalonic acid (Ser); in chain B1 Publication1
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 residuei65Cysteine sulfenic acid (-SOH); in chain B2 Publications1
Modified residuei1082',4',5'-topaquinone1 Publication1
Cross-linki1085'-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

1113
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi17 – 24Combined sources8
Helixi26 – 40Combined sources15
Helixi42 – 44Combined sources3
Helixi46 – 63Combined sources18
Helixi76 – 78Combined sources3
Helixi79 – 90Combined sources12
Helixi94 – 96Combined sources3
Helixi97 – 107Combined sources11

3D structure databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP85511.

Family and domain databases

ProtoNetiSearch...

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: November 2, 2016
This is version 37 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

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 one 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.