ID RANSM_POLLE Reviewed; 113 AA. AC P85511; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 22-FEB-2023, entry version 46. DE RecName: Full=Ranasmurfin; DE AltName: Full=RSF-1; OS Polypedates leucomystax (Common tree frog) (Hyla leucomystax). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Neobatrachia; Ranoidea; Rhacophoridae; Rhacophorinae; OC Polypedates. OX NCBI_TaxID=68444; RN [1] {ECO:0000305} RP PROTEIN SEQUENCE, SUBUNIT, TISSUE SPECIFICITY, ZINC BINDING, AMINOMALONIC RP ACID FORMATION AT SER-9, DISULFIDE BONDS, AND CROSS-LINK FORMATION. RC TISSUE=Foam nest {ECO:0000269|Ref.1}; RA Muse O., Ching R.T.Y., Carter L.G., Johnson K.A., Liu H., Mcmahon S.A., RA White M.F., Bloch C. Jr., Botting C.H., Walsh M.A., Latiff A.A., RA Kennedy M.W., Cooper A., Naismith J.H.; RT "Unusual chromophores and crosslinks in ranasmurfin - a blue protein from RT the foam nests of a tropical frog."; RL Submitted (FEB-2008) to UniProtKB. RN [2] {ECO:0000305} RP SUBUNIT, ZINC-BINDING, AND CRYSTALLIZATION. RX PubMed=17077494; DOI=10.1107/s1744309106040036; RA McMahon S.A., Walsh M.A., Ching R.T.Y., Carter L.G., Dorward M., RA Johnson K.A., Liu H., Oke M., Bloch C. Jr., Kennedy M.W., Latiff A.A., RA Cooper A., Taylor G.L., White M.F., Naismith J.H.; RT "Crystallization of ranasmurfin, a blue-coloured protein from Polypedates RT leucomystax."; RL Acta Crystallogr. F 62:1124-1126(2006). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) IN COMPLEX WITH ZINC IONS, SUBUNIT, RP DISULFIDE BONDS, OXIDATION AT CYS-65, CROSS-LINKS, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RX PubMed=18781570; DOI=10.1002/anie.200802901; RA Oke M., Ching R.T.Y., Carter L.G., Johnson K.A., Liu H., McMahon S.A., RA White M.F., Bloch C. Jr., Botting C.H., Walsh M.A., Latiff A.A., RA Kennedy M.W., Cooper A., Naismith J.H.; RT "Unusual chromophore and cross-links in ranasmurfin: a blue protein from RT the foam nests of a tropical frog."; RL Angew. Chem. Int. Ed. 47:7853-7856(2008). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:17077494, ECO:0000269|Ref.1}; CC Note=Binds 1 zinc ion per dimer. {ECO:0000269|PubMed:17077494, CC ECO:0000269|Ref.1}; CC -!- SUBUNIT: Homodimer. The two chains, designated A and B, differ in their CC modifications, but not, it is thought, in their sequence. CC {ECO:0000269|PubMed:17077494, ECO:0000269|PubMed:18781570, CC ECO:0000269|Ref.1}. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Foam nest. {ECO:0000269|Ref.1}. CC -!- MISCELLANEOUS: After isolation, the blue protein turns green on CC exposure to air and sunlight. {ECO:0000269|Ref.1}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=About the blues - Issue 103 CC of March 2009; CC URL="https://web.expasy.org/spotlight/back_issues/103"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR PDB; 2VH3; X-ray; 1.16 A; A/B=1-113. DR PDBsum; 2VH3; -. DR AlphaFoldDB; P85511; -. DR SMR; P85511; -. DR EvolutionaryTrace; P85511; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 1.20.120.1410; -; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; LTQ; KW Metal-binding; Oxidation; Secreted; TPQ; Zinc. FT CHAIN 1..113 FT /note="Ranasmurfin" FT /id="PRO_0000332964" FT BINDING 108 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared between dimeric partners" FT BINDING 112 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared between dimeric partners" FT MOD_RES 2 FT /note="2',4',5'-topaquinone" FT /evidence="ECO:0000269|Ref.1" FT MOD_RES 9 FT /note="Aminomalonic acid (Ser); in chain B" FT /evidence="ECO:0000269|Ref.1" FT MOD_RES 65 FT /note="Cysteine sulfenic acid (-SOH); in chain B" FT /evidence="ECO:0000269|PubMed:18781570, ECO:0000269|Ref.1" FT MOD_RES 108 FT /note="2',4',5'-topaquinone" FT /evidence="ECO:0000269|Ref.1" FT DISULFID 4..62 FT /evidence="ECO:0000269|Ref.1" FT DISULFID 17..65 FT /note="In chain A" FT /evidence="ECO:0000269|Ref.1" FT DISULFID 37..101 FT /evidence="ECO:0000269|Ref.1" FT CROSSLNK 2..31 FT /note="Lysine tyrosylquinone (Tyr-Lys)" FT /evidence="ECO:0000269|Ref.1" FT CROSSLNK 17..65 FT /note="S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys); in FT chain B" FT CROSSLNK 30..108 FT /note="Lysine tyrosylquinone (Lys-Tyr)" FT /evidence="ECO:0000269|Ref.1" FT CROSSLNK 108 FT /note="5'-tyrosyl-5'-aminotyrosine (Tyr-Tyr) (interchain FT with Y-108)" FT HELIX 17..24 FT /evidence="ECO:0007829|PDB:2VH3" FT HELIX 26..40 FT /evidence="ECO:0007829|PDB:2VH3" FT HELIX 42..44 FT /evidence="ECO:0007829|PDB:2VH3" FT HELIX 46..63 FT /evidence="ECO:0007829|PDB:2VH3" FT HELIX 76..78 FT /evidence="ECO:0007829|PDB:2VH3" FT HELIX 79..90 FT /evidence="ECO:0007829|PDB:2VH3" FT HELIX 94..96 FT /evidence="ECO:0007829|PDB:2VH3" FT HELIX 97..107 FT /evidence="ECO:0007829|PDB:2VH3" SQ SEQUENCE 113 AA; 12598 MW; 2AE528C28C856EA7 CRC64; AYACSFPPSE IPGSKECLAE ALQKHQGFKK KSYALICAYL NYKEDAENYE RAAEDFDSAV KCTGCKEGVD LHEGNPELIE EGFEKFLASL KIDRKALGSL CTLFQKLYAI PHN //