BCP_PETHY
ID BCP_PETHY Reviewed; 266 AA.
AC A0A0M4FTF3;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Blue copper protein {ECO:0000303|PubMed:25971550};
DE Short=PhBcp {ECO:0000303|PubMed:25971550};
DE Flags: Precursor;
GN Name=BCP {ECO:0000303|PubMed:25971550};
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY RAM1 AND RHIZOPHAGUS
RP IRREGULARIS.
RC STRAIN=cv. W138;
RX PubMed=25971550; DOI=10.1104/pp.15.00310;
RA Rich M.K., Schorderet M., Bapaume L., Falquet L., Morel P.,
RA Vandenbussche M., Reinhardt D.;
RT "The Petunia GRAS transcription factor ATA/RAM1 regulates symbiotic gene
RT expression and fungal morphogenesis in arbuscular mycorrhiza.";
RL Plant Physiol. 168:788-797(2015).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- INDUCTION: Accumulates in roots, in a RAM1-dependent manner, during
CC colonization by arbuscular mycorrhizal (AM) fungi (e.g. Rhizophagus
CC irregularis); the expression level correlates tightly with AM
CC development. {ECO:0000269|PubMed:25971550}.
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DR EMBL; KR612268; ALC79558.1; -; mRNA.
DR AlphaFoldDB; A0A0M4FTF3; -.
DR SMR; A0A0M4FTF3; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009610; P:response to symbiotic fungus; IEP:UniProtKB.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR039391; Phytocyanin.
DR InterPro; IPR003245; Phytocyanin_dom.
DR PANTHER; PTHR33021; PTHR33021; 3.
DR Pfam; PF02298; Cu_bind_like; 2.
DR SUPFAM; SSF49503; SSF49503; 2.
DR PROSITE; PS51485; PHYTOCYANIN; 1.
PE 2: Evidence at transcript level;
KW Copper; Disulfide bond; Electron transport; Glycoprotein; Membrane;
KW Metal-binding; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..266
FT /note="Blue copper protein"
FT /id="PRO_0000450028"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 25..56
FT /note="Phytocyanin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT DOMAIN 57..102
FT /note="Phytocyanin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT DOMAIN 116..216
FT /note="Phytocyanin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT BINDING 156
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT BINDING 197
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT BINDING 202
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT BINDING 208
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 169..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
SQ SEQUENCE 266 AA; 29001 MW; 0336587FB2E8ECF9 CRC64;
MAYSKILFCF MIGFVGFLPA ITMATQYLVG DDRGWTLDFD YQTWAKNKTF KVGDTLAPPP
SEGLTSGYDV ITLTKPGKKW YICGVPTHCS DYNQKLVITV EDGAPAPAPA SPAPQTEYWV
GDDKGWTIDV DYQAWAKGKT FKVGDTLVFK YTKGHHNVFK VNQTGFQNCI APPPSEGLTS
GHDVITLAAP GKKWYICGFP THCSEHKQKL AITVEGAPAQ TPPVWAPAPA PGTPKKIDTG
NSYKITSPYK MFVGGAVSIW TILTLV
