ACET1_MAIZE
ID ACET1_MAIZE Reviewed; 236 AA.
AC Q6I681; C0P777;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Ascorbate-specific transmembrane electron transporter 1;
DE EC=1.-.-.-;
DE AltName: Full=Cytochrome b561-1;
DE Short=Zmb561;
GN Name=ZCYB;
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 [MRNA].
RC STRAIN=cv. Golden cross Bantam T51;
RA Takigami T., Kawabata T., Nakanishi N., Imoto K., Hase T., Orii H.,
RA Asada A., Tsubaki M.;
RT "cDNA cloning of Zea mays cytochrome b561.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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., Haller K., Descour A.,
RA Fernandes J., Zuccolo A., Soderlund C., Walbot V.;
RT "Maize full-length cDNA project.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP PROTEIN SEQUENCE OF 2-11, FUNCTION, AND MUTAGENESIS OF ARG-72; LYS-83;
RP SER-118 AND TRP-122.
RC STRAIN=cv. Golden cross Bantam T51;
RX PubMed=19803484; DOI=10.1021/bi9010682;
RA Nakanishi N., Rahman M.M., Sakamoto Y., Takigami T., Kobayashi K., Hori H.,
RA Hase T., Park S.Y., Tsubaki M.;
RT "Importance of the conserved lysine 83 residue of Zea mays cytochrome
RT b(561) for ascorbate-specific transmembrane electron transfer as revealed
RT by site-directed mutagenesis studies.";
RL Biochemistry 48:10665-10678(2009).
RN [5]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=19762344; DOI=10.1093/jb/mvp146;
RA Nakanishi N., Rahman M.M., Sakamoto Y., Miura M., Takeuchi F., Park S.Y.,
RA Tsubaki M.;
RT "Inhibition of electron acceptance from ascorbate by the specific N-
RT carbethoxylations of maize cytochrome b561: a common mechanism for the
RT transmembrane electron transfer in cytochrome b561 protein family.";
RL J. Biochem. 146:857-866(2009).
CC -!- FUNCTION: Two-heme-containing cytochrome. Catalyzes ascorbate-dependent
CC trans-membrane electron transfer by utilizing a concerted H(+)/e(-)
CC transfer mechanism. {ECO:0000269|PubMed:19762344,
CC ECO:0000269|PubMed:19803484}.
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 -!- ACTIVITY REGULATION: Inhibited by diethylpyrocarbonate.
CC {ECO:0000269|PubMed:19762344}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Initial time lag in electron acceptance from ascorbate
CC observed in acidic pH.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACN28843.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AB182641; BAD24966.1; -; mRNA.
DR EMBL; BT039983; ACF84988.1; -; mRNA.
DR EMBL; BT064146; ACN28843.1; ALT_SEQ; mRNA.
DR EMBL; EU962707; ACG34825.1; -; mRNA.
DR RefSeq; NP_001140931.1; NM_001147459.1.
DR AlphaFoldDB; Q6I681; -.
DR SMR; Q6I681; -.
DR STRING; 4577.GRMZM2G060357_P01; -.
DR TCDB; 5.B.2.1.6; the eukaryotic cytochrome b561 (cytb561) family.
DR PaxDb; Q6I681; -.
DR EnsemblPlants; Zm00001eb185950_T001; Zm00001eb185950_P001; Zm00001eb185950.
DR GeneID; 100273009; -.
DR Gramene; Zm00001eb185950_T001; Zm00001eb185950_P001; Zm00001eb185950.
DR KEGG; zma:100273009; -.
DR eggNOG; KOG1619; Eukaryota.
DR HOGENOM; CLU_069712_0_1_1; -.
DR OrthoDB; 1503869at2759; -.
DR BRENDA; 7.2.1.3; 6752.
DR Proteomes; UP000007305; Chromosome 4.
DR ExpressionAtlas; Q6I681; baseline and differential.
DR Genevisible; Q6I681; 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 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..236
FT /note="Ascorbate-specific transmembrane electron
FT transporter 1"
FT /id="PRO_0000416687"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..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 MUTAGEN 72
FT /note="R->A: Fast electron transfer at acidic pH."
FT /evidence="ECO:0000269|PubMed:19803484"
FT MUTAGEN 83
FT /note="K->A,D: Decreased redox potential of cytoplasmic
FT heme."
FT /evidence="ECO:0000269|PubMed:19803484"
FT MUTAGEN 83
FT /note="K->E: No effect."
FT /evidence="ECO:0000269|PubMed:19803484"
FT MUTAGEN 118
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:19803484"
FT MUTAGEN 122
FT /note="W->A: No effect."
FT /evidence="ECO:0000269|PubMed:19803484"
SQ SEQUENCE 236 AA; 25425 MW; F61AA8A5112503F1 CRC64;
MGLGLGVRAA PFTYAAHALA VAAAAMVLVW SIQFRGGLAI ESTNKNLIFN VHPVLMLIGY
VIIGGEAIMV YRVLPTSNHD TTKLIHLILH GIALVLGAVG IYFAFKNHNE SGIANLYSLH
SWIGIGTITL YGIQWIIGFV TFFFPGAAPN VKKGVLPWHV LFGLFVYILA LANAELGFLE
KLTFLESSGL DKYGTEAFLV NFTALVVVLF GASVVVAAIA PVRLEEPQGY DPIPEN
