FRRS1_DROME
ID FRRS1_DROME Reviewed; 647 AA.
AC Q8MSU3; Q9V7I1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Putative ferric-chelate reductase 1 homolog;
DE Short=DmSDR2;
DE EC=1.-.-.-;
GN ORFNames=CG8399;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP FUNCTION.
RX PubMed=14499595; DOI=10.1016/s1570-9639(03)00242-5;
RA Vargas J.D., Herpers B., McKie A.T., Gledhill S., McDonnell J.,
RA van den Heuvel M., Davies K.E., Ponting C.P.;
RT "Stromal cell-derived receptor 2 and cytochrome b561 are functional ferric
RT reductases.";
RL Biochim. Biophys. Acta 1651:116-123(2003).
CC -!- FUNCTION: Putative ferric-chelate reductases reduce Fe(3+) to Fe(2+)
CC before its transport from the endosome to the cytoplasm.
CC {ECO:0000269|PubMed:14499595}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FRRS1 family. {ECO:0000305}.
CC -!- CAUTION: The cytochrome b561 domain lacks the conserved His residue
CC that binds iron in the heme. The reductase activity is therefore unsure
CC in vivo. {ECO:0000305}.
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DR EMBL; AE013599; AAF58074.2; -; Genomic_DNA.
DR EMBL; AY118595; AAM49964.1; -; mRNA.
DR RefSeq; NP_611079.2; NM_137235.3.
DR AlphaFoldDB; Q8MSU3; -.
DR SMR; Q8MSU3; -.
DR STRING; 7227.FBpp0086349; -.
DR TCDB; 5.B.2.2.3; the eukaryotic cytochrome b561 (cytb561) family.
DR GlyGen; Q8MSU3; 2 sites.
DR SwissPalm; Q8MSU3; -.
DR PaxDb; Q8MSU3; -.
DR PRIDE; Q8MSU3; -.
DR DNASU; 36768; -.
DR EnsemblMetazoa; FBtr0087207; FBpp0086349; FBgn0034067.
DR GeneID; 36768; -.
DR KEGG; dme:Dmel_CG8399; -.
DR UCSC; CG8399-RA; d. melanogaster.
DR FlyBase; FBgn0034067; CG8399.
DR VEuPathDB; VectorBase:FBgn0034067; -.
DR eggNOG; KOG4293; Eukaryota.
DR GeneTree; ENSGT00940000170494; -.
DR HOGENOM; CLU_028305_0_0_1; -.
DR InParanoid; Q8MSU3; -.
DR OMA; PLTMRSW; -.
DR PhylomeDB; Q8MSU3; -.
DR BioGRID-ORCS; 36768; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36768; -.
DR PRO; PR:Q8MSU3; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034067; Expressed in second segment of antenna (Drosophila) and 19 other tissues.
DR ExpressionAtlas; Q8MSU3; baseline and differential.
DR Genevisible; Q8MSU3; DM.
DR GO; GO:0016021; C:integral component of membrane; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016722; F:oxidoreductase activity, acting on metal ions; IDA:UniProtKB.
DR GO; GO:0140571; F:transmembrane ascorbate ferrireductase activity; IDA:FlyBase.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IDA:ARUK-UCL.
DR CDD; cd08544; Reeler; 1.
DR Gene3D; 2.60.40.4060; -; 1.
DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR InterPro; IPR005018; DOMON_domain.
DR InterPro; IPR002861; Reeler_dom.
DR InterPro; IPR042307; Reeler_sf.
DR Pfam; PF02014; Reeler; 1.
DR SMART; SM00665; B561; 1.
DR SMART; SM00664; DoH; 1.
DR PROSITE; PS50939; CYTOCHROME_B561; 1.
DR PROSITE; PS50836; DOMON; 1.
DR PROSITE; PS51019; REELIN; 1.
PE 2: Evidence at transcript level;
KW Electron transport; Glycoprotein; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..647
FT /note="Putative ferric-chelate reductase 1 homolog"
FT /id="PRO_0000314847"
FT TRANSMEM 10..30
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 480..500
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 515..535
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 616..636
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT DOMAIN 25..195
FT /note="Reelin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00363"
FT DOMAIN 245..368
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT DOMAIN 372..570
FT /note="Cytochrome b561"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT BINDING 409
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 450
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 480
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 516
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 CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 647 AA; 70285 MW; BBBDD090AFDF301D CRC64;
MMQALTMRSW LATLVTALLA VAIWPDPGQS LPQGAPETVC DTMLPFHSGG SVLPQNSVSP
FSVETSSSTL GQGQTLRVDL TGVPAGLSFG GYMIQARNRN PPHQIIGQFG PARDGTIKLM
NCENSVNNSA THSNAGPKQQ VILEWQSPVD FLGQVVFNAT IAQSYNEFWV GVPSQPVQIV
RRDLSAAPPL PTQSPSAPAG TTRAPYVPPS YVAPNNVVAV SSDPIYNGCG QSKNCFGFPD
GCVATKSCTS ITVVTVRGDV FEFEIQSGKG TNAAYVAVGL SDDAKMGDDL TTECVPENGR
VNLYSSLTSA SPYSAVRSNV NQNSARLLDA SIVDGVIYCR VQRDAVTNVQ GRTFDLRNGK
YHLLVASGSS LKENSVGYHD IGRLPSAQPI NLAEVQDLSG SSRLLIQLHG AFMIAAWIGT
TSLGIIFARY FKQTWVGSQS CGTDQWFAWH RLLMVTTWSL TVAAYVLIWV ELKQAVWHAH
SIIGLITVIL CFIQPIGALF RPGPNDKKRP YFNWGHWLGG NLAHILGIVT IFFSVKLPKA
ELPEWMDWIL VSFVVVHVLV HLIFSIGGMA SERHLSQRAN TFQMGDMSHH QQHAMRNGMS
MERKMDAPYA GMRKGLLGVY GVVLILFVTV LILLVVLAPI EQFLGKS
