MAVI_CUCPE
ID MAVI_CUCPE Reviewed; 108 AA.
AC P80728;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Mavicyanin;
OS Cucurbita pepo (Vegetable marrow) (Summer squash).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX NCBI_TaxID=3663;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Peelings;
RX PubMed=8841377; DOI=10.1016/0167-4838(96)00079-9;
RA Schinina M.E., Maritano S., Barra D., Mondovi B., Marchesini A.;
RT "Mavicyanin, a stellacyanin-like protein from zucchini peelings: primary
RT structure and comparison with other cupredoxins.";
RL Biochim. Biophys. Acta 1297:28-32(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=15858169; DOI=10.1093/jb/mvi062;
RA Xie Y., Inoue T., Miyamoto Y., Matsumura H., Kataoka K., Yamaguchi K.,
RA Nojini M., Suzuki S., Kai Y.;
RT "Structural reorganization of the copper binding site involving Thr15 of
RT mavicyanin from Cucurbita pepo medullosa (zucchini) upon reduction.";
RL J. Biochem. 137:455-461(2005).
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is +285 mV.;
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DR PIR; S72218; S72218.
DR PDB; 1WS7; X-ray; 1.90 A; A/B/C/D=1-108.
DR PDB; 1WS8; X-ray; 1.60 A; A/B/C/D=1-108.
DR PDBsum; 1WS7; -.
DR PDBsum; 1WS8; -.
DR AlphaFoldDB; P80728; -.
DR SMR; P80728; -.
DR EvolutionaryTrace; P80728; -.
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 3D-structure; Copper; Direct protein sequencing; Disulfide bond;
KW Electron transport; Glycoprotein; Metal-binding; Transport.
FT CHAIN 1..108
FT /note="Mavicyanin"
FT /id="PRO_0000085554"
FT DOMAIN 2..103
FT /note="Phytocyanin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT BINDING 44
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 85
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 90
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 95
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 57..91
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1WS8"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:1WS8"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1WS8"
FT HELIX 20..25
FT /evidence="ECO:0007829|PDB:1WS8"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:1WS8"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:1WS8"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:1WS8"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:1WS8"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1WS8"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:1WS8"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:1WS8"
FT TURN 88..94
FT /evidence="ECO:0007829|PDB:1WS8"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:1WS8"
SQ SEQUENCE 108 AA; 11747 MW; 52F88899D6881652 CRC64;
ATVHKVGDST GWTTLVPYDY AKWASSNKFH VGDSLLFNYN NKFHNVLQVD QEQFKSCNSS
SPAASYTSGA DSIPLKRPGT FYFLCGIPGH CQLGQKVEIK VDPGSSSA
