STEL_TOXVR
ID STEL_TOXVR Reviewed; 107 AA.
AC P00302;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Stellacyanin;
OS Toxicodendron vernicifluum (Japanese lacquer tree) (Rhus verniciflua).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Anacardiaceae; Toxicodendron.
OX NCBI_TaxID=4013;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=901509; DOI=10.1016/s0006-291x(77)80084-3;
RA Bergman C., Gandvik E.K., Nyman P.O., Strid L.;
RT "The amino acid sequence of stellacyanin from the lacquer tree.";
RL Biochem. Biophys. Res. Commun. 77:1052-1059(1977).
RN [2]
RP ERRATUM OF PUBMED:901509.
RA Bergman C., Gandvik E.K., Nyman P.O., Strid L.;
RL Biochem. Biophys. Res. Commun. 79:1013-1013(1977).
RN [3]
RP DISULFIDE BOND.
RX PubMed=6723985; DOI=10.1016/0014-5793(84)80499-8;
RA Engeseth H.R., Hermodson M.A., McMillin D.R.;
RT "A new assignment of the disulfide linkage in stellacyanin.";
RL FEBS Lett. 171:257-261(1984).
RN [4]
RP 3D-STRUCTURE MODELING.
RX PubMed=1762145; DOI=10.1016/0022-2836(91)90593-u;
RA Fields B.A., Guss J.M., Freeman H.C.;
RT "Three-dimensional model for stellacyanin, a 'blue' copper-protein.";
RL J. Mol. Biol. 222:1053-1065(1991).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is +184 mV.;
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DR PIR; A00311; SSUL.
DR iPTMnet; P00302; -.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd11014; Mavicyanin; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR028871; BlueCu_1_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR041845; Mavicyanin.
DR InterPro; IPR039391; Phytocyanin.
DR InterPro; IPR003245; Phytocyanin_dom.
DR PANTHER; PTHR33021; PTHR33021; 1.
DR Pfam; PF02298; Cu_bind_like; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR PROSITE; PS00196; COPPER_BLUE; 1.
DR PROSITE; PS51485; PHYTOCYANIN; 1.
PE 1: Evidence at protein level;
KW Copper; Direct protein sequencing; Disulfide bond; Electron transport;
KW Glycoprotein; Metal-binding; Transport.
FT CHAIN 1..107
FT /note="Stellacyanin"
FT /id="PRO_0000085556"
FT DOMAIN 1..105
FT /note="Phytocyanin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT BINDING 46
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 87
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 92
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 97
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:6723985"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:6723985"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:6723985"
FT DISULFID 59..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818,
FT ECO:0000269|PubMed:6723985"
SQ SEQUENCE 107 AA; 12296 MW; 4AF450E1A0461069 CRC64;
TVYTVGDSAG WKVPFFGDVD YDWKWASNKT FHIGDVLVFK YDRRFHNVDK VTQKNYQSCN
DTTPIASYNT GBBRINLKTV GQKYYICGVP KHCDLGQKVH INVTVRS