ID CYAC3_MOUSE Reviewed; 242 AA.
AC Q6P1H1; Q3TVE2; Q3V3G2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 131.
DE RecName: Full=Lysosomal membrane ascorbate-dependent ferrireductase CYB561A3 {ECO:0000305|PubMed:16911521, ECO:0000305|PubMed:16996694};
DE EC=7.2.1.3 {ECO:0000269|PubMed:16911521};
DE AltName: Full=Cytochrome b ascorbate-dependent protein 3 {ECO:0000312|MGI:MGI:2686925};
DE AltName: Full=Cytochrome b561 family member A3 {ECO:0000312|MGI:MGI:2686925};
DE AltName: Full=Lysosomal cytochrome b {ECO:0000303|PubMed:16996694};
DE Short=LCytb {ECO:0000303|PubMed:16996694};
GN Name=Cyb561a3 {ECO:0000312|MGI:MGI:2686925};
GN Synonyms=Cybasc3 {ECO:0000312|MGI:MGI:2686925};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Amnion, Aorta, Egg, Spleen, Thymus, Tongue, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=16996694; DOI=10.1016/j.bbagen.2006.07.019;
RA Zhang D.-L., Su D., Berczi A., Vargas A., Asard H.;
RT "An ascorbate-reducible cytochrome b561 is localized in macrophage
RT lysosomes.";
RL Biochim. Biophys. Acta 1760:1903-1913(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-38; PHE-44; HIS-47;
RP PRO-48; MET-51; TYR-66; ARG-67; HIS-83; HIS-105; ASN-106; HIS-112; SER-115;
RP HIS-117; SER-118; TRP-119; GLN-131; ARG-149; HIS-156; GLU-177; TYR-190 AND
RP GLU-196.
RX PubMed=16911521; DOI=10.1111/j.1742-4658.2006.05381.x;
RA Su D., Asard H.;
RT "Three mammalian cytochromes b561 are ascorbate-dependent
RT ferrireductases.";
RL FEBS J. 273:3722-3734(2006).
CC -!- FUNCTION: Transmembrane reductase that uses ascorbate as an electron
CC donor in the cytoplasm and transfers electrons across membranes to
CC reduce iron cations Fe(3+) into Fe(2+) in the lumen of the late
CC endosome and lysosome (PubMed:16911521). Reduced iron can then be
CC extruded from the late endosome and lysosome to the cytoplasm by
CC divalent metal-specific transporters (Probable). It is therefore most
CC probably involved in endosomal and lysosomal cellular iron homeostasis
CC (Probable). {ECO:0000269|PubMed:16911521, ECO:0000305|PubMed:16911521}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fe(3+)(out) + L-ascorbate(in) = Fe(2+)(out) + H(+) +
CC monodehydro-L-ascorbate radical(in); Xref=Rhea:RHEA:30403,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:59513; EC=7.2.1.3;
CC Evidence={ECO:0000269|PubMed:16911521};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30404;
CC Evidence={ECO:0000305|PubMed:16911521};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:Q53TN4};
CC Note=Binds 2 heme b groups non-covalently.
CC {ECO:0000250|UniProtKB:Q53TN4};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q53TN4}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000269|PubMed:16996694}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q53TN4}. Lysosome membrane
CC {ECO:0000269|PubMed:16996694}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q53TN4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6P1H1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P1H1-2; Sequence=VSP_030398;
CC Name=3;
CC IsoId=Q6P1H1-3; Sequence=VSP_030399;
CC -!- TISSUE SPECIFICITY: Present in lung, spleen, thymus and testis. Present
CC at low level in brain, heart, liver and kidney. Expressed in the
CC alveolar macrophages of the lung, in the white pulp of the spleen,
CC widespread in the thymus, and in the Sertoli cells of the testis (at
CC protein level). {ECO:0000269|PubMed:16996694}.
CC -!- DEVELOPMENTAL STAGE: At 17.5 dpc, it is primarily expressed in lung,
CC spleen, thymus, testis, placenta, small intestine and stomach.
CC {ECO:0000269|PubMed:16996694}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16996694}.
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DR EMBL; AK040692; BAE20585.1; -; mRNA.
DR EMBL; AK139533; BAE24053.1; -; mRNA.
DR EMBL; AK160179; BAE35677.1; -; mRNA.
DR EMBL; AK168841; BAE40664.1; -; mRNA.
DR EMBL; AK169729; BAE41333.1; -; mRNA.
DR EMBL; AK170911; BAE42109.1; -; mRNA.
DR EMBL; AK172638; BAE43109.1; -; mRNA.
DR EMBL; BC065078; AAH65078.1; -; mRNA.
DR CCDS; CCDS29582.1; -. [Q6P1H1-1]
DR CCDS; CCDS89344.1; -. [Q6P1H1-2]
DR RefSeq; NP_001268993.1; NM_001282064.1. [Q6P1H1-1]
DR RefSeq; NP_001268994.1; NM_001282065.1. [Q6P1H1-2]
DR RefSeq; NP_001268996.1; NM_001282067.1. [Q6P1H1-1]
DR RefSeq; NP_958739.1; NM_201351.2. [Q6P1H1-1]
DR RefSeq; XP_006527003.1; XM_006526940.3. [Q6P1H1-2]
DR RefSeq; XP_017173639.1; XM_017318150.1.
DR RefSeq; XP_017173640.1; XM_017318151.1.
DR AlphaFoldDB; Q6P1H1; -.
DR SMR; Q6P1H1; -.
DR STRING; 10090.ENSMUSP00000158186; -.
DR TCDB; 5.B.2.1.5; the eukaryotic cytochrome b561 (cytb561) family.
DR PaxDb; 10090-ENSMUSP00000130680; -.
DR ProteomicsDB; 283992; -. [Q6P1H1-1]
DR ProteomicsDB; 283993; -. [Q6P1H1-2]
DR ProteomicsDB; 283994; -. [Q6P1H1-3]
DR Antibodypedia; 52925; 9 antibodies from 7 providers.
DR Ensembl; ENSMUST00000168445.2; ENSMUSP00000130680.2; ENSMUSG00000034445.9. [Q6P1H1-1]
DR Ensembl; ENSMUST00000235271.2; ENSMUSP00000157672.2; ENSMUSG00000034445.9. [Q6P1H1-1]
DR Ensembl; ENSMUST00000236352.2; ENSMUSP00000157892.2; ENSMUSG00000034445.9. [Q6P1H1-3]
DR Ensembl; ENSMUST00000237581.2; ENSMUSP00000157884.2; ENSMUSG00000034445.9. [Q6P1H1-1]
DR Ensembl; ENSMUST00000237641.2; ENSMUSP00000157602.2; ENSMUSG00000034445.9. [Q6P1H1-2]
DR Ensembl; ENSMUST00000237814.2; ENSMUSP00000158186.2; ENSMUSG00000034445.9. [Q6P1H1-1]
DR GeneID; 225912; -.
DR KEGG; mmu:225912; -.
DR UCSC; uc008gqg.2; mouse. [Q6P1H1-1]
DR UCSC; uc008gqi.2; mouse. [Q6P1H1-2]
DR AGR; MGI:2686925; -.
DR CTD; 220002; -.
DR MGI; MGI:2686925; Cyb561a3.
DR VEuPathDB; HostDB:ENSMUSG00000034445; -.
DR eggNOG; KOG1619; Eukaryota.
DR GeneTree; ENSGT00950000183197; -.
DR HOGENOM; CLU_069712_1_3_1; -.
DR InParanoid; Q6P1H1; -.
DR OMA; FKFHDMV; -.
DR OrthoDB; 2877457at2759; -.
DR PhylomeDB; Q6P1H1; -.
DR TreeFam; TF314222; -.
DR BRENDA; 7.2.1.3; 3474.
DR BioGRID-ORCS; 225912; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Cyb561a3; mouse.
DR PRO; PR:Q6P1H1; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q6P1H1; Protein.
DR Bgee; ENSMUSG00000034445; Expressed in spleen and 229 other cell types or tissues.
DR ExpressionAtlas; Q6P1H1; baseline and differential.
DR Genevisible; Q6P1H1; MM.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0140571; F:transmembrane ascorbate ferrireductase activity; IDA:UniProtKB.
DR GO; GO:0006879; P:intracellular iron ion homeostasis; IDA:UniProtKB.
DR Gene3D; 1.20.120.1770; -; 1.
DR InterPro; IPR043205; CYB561/CYBRD1-like.
DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR PANTHER; PTHR10106; CYTOCHROME B561-RELATED; 1.
DR PANTHER; PTHR10106:SF0; LYSOSOMAL MEMBRANE ASCORBATE-DEPENDENT FERRIREDUCTASE CYB561A3; 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 Alternative splicing; Electron transport; Endosome; Glycoprotein; Heme;
KW Iron; Lysosome; Membrane; Metal-binding; Oxidoreductase;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..242
FT /note="Lysosomal membrane ascorbate-dependent
FT ferrireductase CYB561A3"
FT /id="PRO_0000314839"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..40
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..119
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..202
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT DOMAIN 12..219
FT /note="Cytochrome b561"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT BINDING 47
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:Q53TN4"
FT BINDING 67
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 76
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 80
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 83
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:Q53TN4"
FT BINDING 112..115
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 117
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:Q53TN4"
FT BINDING 149
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 156
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:Q53TN4"
FT BINDING 177
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 224
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT VAR_SEQ 236..242
FT /note="PLLHDRE -> LLLQLLPGSRPFPVTYMPVPLR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030398"
FT VAR_SEQ 236..242
FT /note="PLLHDRE -> DGTCGWRLSPSALMWSPGWNVRMAEDFV (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030399"
FT MUTAGEN 38
FT /note="D->A: No effect on transmembrane ascorbate
FT ferrireductase activity."
FT /evidence="ECO:0000269|PubMed:16911521"
FT MUTAGEN 44
FT /note="F->A: Decreased transmembrane ascorbate
FT ferrireductase activity. Approximately 45% reduction in
FT enzyme activity."
FT /evidence="ECO:0000269|PubMed:16911521"
FT MUTAGEN 47
FT /note="H->A: Loss of transmembrane ascorbate ferrireductase
FT activity."
FT /evidence="ECO:0000269|PubMed:16911521"
FT MUTAGEN 48
FT /note="P->A: No effect on transmembrane ascorbate
FT ferrireductase activity."
FT /evidence="ECO:0000269|PubMed:16911521"
FT MUTAGEN 51
FT /note="M->A: No effect on transmembrane ascorbate
FT ferrireductase activity."
FT /evidence="ECO:0000269|PubMed:16911521"
FT MUTAGEN 66
FT /note="Y->A: Loss of transmembrane ascorbate ferrireductase
FT activity."
FT /evidence="ECO:0000269|PubMed:16911521"
FT MUTAGEN 67
FT /note="R->A: Loss of transmembrane ascorbate ferrireductase
FT activity."
FT /evidence="ECO:0000269|PubMed:16911521"
FT MUTAGEN 83
FT /note="H->A: Loss of transmembrane ascorbate ferrireductase
FT activity."
FT /evidence="ECO:0000269|PubMed:16911521"
FT MUTAGEN 105
FT /note="H->A: No effect on transmembrane ascorbate
FT ferrireductase activity."
FT /evidence="ECO:0000269|PubMed:16911521"
FT MUTAGEN 106
FT /note="N->A: No effect on transmembrane ascorbate
FT ferrireductase activity."
FT /evidence="ECO:0000269|PubMed:16911521"
FT MUTAGEN 112
FT /note="H->A: Decreased transmembrane ascorbate
FT ferrireductase activity."
FT /evidence="ECO:0000269|PubMed:16911521"
FT MUTAGEN 115
FT /note="S->A: Decreased transmembrane ascorbate
FT ferrireductase activity. Approximately 50% reduction in
FT enzyme activity."
FT /evidence="ECO:0000269|PubMed:16911521"
FT MUTAGEN 117
FT /note="H->A: Loss of transmembrane ascorbate ferrireductase
FT activity."
FT /evidence="ECO:0000269|PubMed:16911521"
FT MUTAGEN 118
FT /note="S->A: No effect on transmembrane ascorbate
FT ferrireductase activity."
FT /evidence="ECO:0000269|PubMed:16911521"
FT MUTAGEN 119
FT /note="W->A: Decreased transmembrane ascorbate
FT ferrireductase activity. Approximately 80% reduction in
FT enzyme activity."
FT /evidence="ECO:0000269|PubMed:16911521"
FT MUTAGEN 131
FT /note="Q->A: Decreased transmembrane ascorbate
FT ferrireductase activity. Approximately 55% reduction in
FT enzyme activity."
FT /evidence="ECO:0000269|PubMed:16911521"
FT MUTAGEN 149
FT /note="R->A: Decreased transmembrane ascorbate
FT ferrireductase activity. Approximately 75% reduction in
FT enzyme activity."
FT /evidence="ECO:0000269|PubMed:16911521"
FT MUTAGEN 156
FT /note="H->A: Loss of transmembrane ascorbate ferrireductase
FT activity."
FT /evidence="ECO:0000269|PubMed:16911521"
FT MUTAGEN 177
FT /note="E->A: No effect on transmembrane ascorbate
FT ferrireductase activity."
FT /evidence="ECO:0000269|PubMed:16911521"
FT MUTAGEN 190
FT /note="Y->A: No effect on transmembrane ascorbate
FT ferrireductase activity."
FT /evidence="ECO:0000269|PubMed:16911521"
FT MUTAGEN 196
FT /note="E->A: Decreased transmembrane ascorbate
FT ferrireductase activity. Approximately 75% reduction in
FT enzyme activity."
FT /evidence="ECO:0000269|PubMed:16911521"
SQ SEQUENCE 242 AA; 27086 MW; 675709EC97741761 CRC64;
MASGWFYLSC MVLGSLGSMC ILFTAYWMQY WRGGFAWDGT VLMFNWHPVL MVAGMVVLYG
AASLVYRLPS SWVGPRLPWK VLHAALHLLA FTCTVVGLIA VFRFHNHSRI AHLYSLHSWL
GITTVVLFAC QWFLGFAVFL LPWASQWLRS LLKPLHVFFG ACILSLSITS VISGINEKLF
FVLKNATKPY SSLPGEAVFA NSTGLLVVAF GLLVLYVLLA SSWKRPDPGA LTDRQPLLHD
RE
//
