RANSM_POLLE
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 03-AUG-2022, entry version 45.
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";
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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.
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
