ACFR2_MAIZE
ID ACFR2_MAIZE Reviewed; 236 AA.
AC C4IYS8; B6TAB6;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Ascorbate-specific transmembrane electron transporter 2;
DE EC=1.-.-.-;
DE AltName: Full=Cytochrome b561-2;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73;
RA Yu Y., Currie J., Lomeli R., Angelova A., Collura K., Wissotski M.,
RA Campos D., Kudrna D., Golser W., Ashely E., Descour A., Fernandes J.,
RA Soderlund C., Walbot V.;
RT "Maize full-length cDNA project.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Two-heme-containing cytochrome. Catalyzes ascorbate-dependent
CC trans-membrane electron transfer by utilizing a concerted H(+)/e(-)
CC transfer mechanism (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:Q9SWS1};
CC Note=Binds 2 heme b groups non-covalently.
CC {ECO:0000250|UniProtKB:Q9SWS1};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; EU961931; ACG34049.1; -; mRNA.
DR EMBL; BT083725; ACR34078.1; -; mRNA.
DR RefSeq; NP_001170569.1; NM_001177098.1.
DR AlphaFoldDB; C4IYS8; -.
DR SMR; C4IYS8; -.
DR STRING; 4577.GRMZM2G066885_P01; -.
DR PaxDb; C4IYS8; -.
DR EnsemblPlants; Zm00001eb248610_T001; Zm00001eb248610_P001; Zm00001eb248610.
DR GeneID; 100384594; -.
DR Gramene; Zm00001eb248610_T001; Zm00001eb248610_P001; Zm00001eb248610.
DR KEGG; zma:100384594; -.
DR eggNOG; KOG1619; Eukaryota.
DR HOGENOM; CLU_069712_0_1_1; -.
DR OMA; VQFSFGF; -.
DR OrthoDB; 1503869at2759; -.
DR Proteomes; UP000007305; Chromosome 5.
DR ExpressionAtlas; C4IYS8; baseline and differential.
DR Genevisible; C4IYS8; ZM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR InterPro; IPR043205; CYB561/CYBRD1-like.
DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR PANTHER; PTHR10106; PTHR10106; 1.
DR Pfam; PF03188; Cytochrom_B561; 1.
DR SMART; SM00665; B561; 1.
DR PROSITE; PS50939; CYTOCHROME_B561; 1.
PE 2: Evidence at transcript level;
KW Electron transport; Heme; Iron; Membrane; Metal-binding; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..236
FT /note="Ascorbate-specific transmembrane electron
FT transporter 2"
FT /id="PRO_0000416688"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..50
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..122
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..201
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 15..219
FT /note="Cytochrome b561"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT BINDING 52
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q9SWS1"
FT BINDING 67..75
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q9SWS1"
FT BINDING 116..125
FT /ligand="monodehydro-L-ascorbate radical"
FT /ligand_id="ChEBI:CHEBI:59513"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q9SWS1"
FT BINDING 159
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q9SWS1"
FT CONFLICT 80
FT /note="E -> G (in Ref. 1; ACG34049)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 236 AA; 25439 MW; 08C6531EFD1CEEB2 CRC64;
MGLGLGVRAA PFTYAAHALA VAAAAMVLVW AIYFRGGLAI EATNKNLIFN VHPVLMLIGY
IIIGGEAIMV YRVLPTSNHE TNKLIHLVLH GIALVLGAVG IYFAFKNHNE SGIANLYSLH
SWIGIGTITL YGIQWIVGFV TFFFPGAAPN VKKGVLPWHI LFGLFVYILA LANAELGFLE
KLTFLESSGL DKYGTEAFLV NFTALVVVLF GASVVVAAIA PVRLEEPQGY VPIPEN
