FRRS1_MOUSE
ID FRRS1_MOUSE Reviewed; 592 AA.
AC Q8K385; P97301; Q3TJV0; Q3UMF5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Ferric-chelate reductase 1;
DE EC=1.-.-.-;
DE AltName: Full=Stromal cell-derived receptor 2;
DE Short=SDR-2;
GN Name=FRRS1; Synonyms=Sdfr2, Sdr2;
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 [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=8938438; DOI=10.1006/geno.1996.0560;
RA Shirozu M., Tada H., Tashiro K., Nakamura T., Lopez N.D., Nazarea M.,
RA Hamada T., Sato T., Nakano T., Honjo T.;
RT "Characterization of novel secreted and membrane proteins isolated by the
RT signal sequence trap method.";
RL Genomics 37:273-280(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland, and Vagina;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP FUNCTION, ENZYME ACTIVITY, TISSUE SPECIFICITY, AND INDUCTION.
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).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-321 AND ASN-353.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Ferric-chelate reductases reduce Fe(3+) to Fe(2+) before its
CC 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 -!- TISSUE SPECIFICITY: Expressed in spleen, liver and kidney with low
CC expression in brain. Localizes in adult brain to the choroid plexus of
CC the fourth, third, and lateral ventricles and to ependymal cells that
CC line the ventricles. {ECO:0000269|PubMed:14499595,
CC ECO:0000269|PubMed:8938438}.
CC -!- INDUCTION: Down-regulated in kidney and liver of mice lacking
CC hypotransferrinemic (hpx), which have iron overload of the liver and
CC pancreas. {ECO:0000269|PubMed:14499595}.
CC -!- SIMILARITY: Belongs to the FRRS1 family. {ECO:0000305}.
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DR EMBL; D50464; BAA09055.1; -; mRNA.
DR EMBL; AK144933; BAE26143.1; -; mRNA.
DR EMBL; AK162693; BAE37025.1; -; mRNA.
DR EMBL; AK167289; BAE39395.1; -; mRNA.
DR EMBL; BC027770; AAH27770.1; -; mRNA.
DR CCDS; CCDS17792.1; -.
DR RefSeq; NP_001106950.1; NM_001113478.1.
DR RefSeq; NP_033172.2; NM_009146.3.
DR AlphaFoldDB; Q8K385; -.
DR SMR; Q8K385; -.
DR BioGRID; 203144; 3.
DR STRING; 10090.ENSMUSP00000039487; -.
DR GlyConnect; 2311; 1 N-Linked glycan (1 site).
DR GlyGen; Q8K385; 4 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q8K385; -.
DR PhosphoSitePlus; Q8K385; -.
DR MaxQB; Q8K385; -.
DR PaxDb; Q8K385; -.
DR PeptideAtlas; Q8K385; -.
DR PRIDE; Q8K385; -.
DR ProteomicsDB; 271636; -.
DR DNASU; 20321; -.
DR GeneID; 20321; -.
DR KEGG; mmu:20321; -.
DR UCSC; uc008rcv.2; mouse.
DR CTD; 391059; -.
DR MGI; MGI:108076; Frrs1.
DR eggNOG; KOG4293; Eukaryota.
DR InParanoid; Q8K385; -.
DR OrthoDB; 599276at2759; -.
DR PhylomeDB; Q8K385; -.
DR TreeFam; TF316169; -.
DR BioGRID-ORCS; 20321; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Frrs1; mouse.
DR PRO; PR:Q8K385; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8K385; protein.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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: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 1: Evidence at protein level;
KW Electron transport; Glycoprotein; Heme; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..592
FT /note="Ferric-chelate reductase 1"
FT /id="PRO_0000314844"
FT TRANSMEM 2..22
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..499
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 515..535
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 569..589
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT DOMAIN 13..179
FT /note="Reelin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00363"
FT DOMAIN 216..331
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT DOMAIN 335..534
FT /note="Cytochrome b561"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT BINDING 373
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 414
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 446
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 482
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 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CONFLICT 9
FT /note="S -> R (in Ref. 1; BAA09055)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="G -> E (in Ref. 1; BAA09055)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="E -> K (in Ref. 2; BAE26143/BAE39395/BAE37025)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="P -> S (in Ref. 2; BAE39395/BAE37025)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="G -> S (in Ref. 2; BAE39395/BAE37025)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="V -> I (in Ref. 1; BAA09055)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="A -> G (in Ref. 1; BAA09055)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 592 AA; 66047 MW; EAC9146163E85ED3 CRC64;
MAAPQITLSV LVIALLTCSV TAYPNGKVPM SCGGMIPQHN HSPQSEPIHQ ITVSQTTFKP
GDQIEVTLSG PPFRGFLLEA RDAENLSGPP IGSFTLIDSE ESQLLTCTDV QGLAVSHTRS
SKKTEIKVYW DAPSPAPDHI RFLATVVQKF KIYWVKIPSP VISQPNAPPF TTPKATTQPL
TTPPSVSHLT KPFSAFECGN KKFCVRSPLN CDPEKEPACV FLSFTRDNQS VMVEMSGPSD
GYVSFAFSHD QWMGDDDAYL CIREDQTVDI QPSYLTGRSY PVMDSRGTLE DMAWRLADGV
IQCSFRRNIT LPEAKNRFVL NESYYIFFAE GPSHDGRIFR HSQQPLITYE KYNVTDTPKS
VGGSRSSPLL KAHGALMFVA WMTTVSIGVL VARFFRSVWS KAFFLREAAW FQVHRMLMVA
TSLLTCVAFV LPFVYRGGWS WRAGYHPYLG CTVMTLAVLQ PLLATFRPPL HDPRRQVFNW
THWSVGTAAR IIAVAAMFLG MDLPGLNLPS PQKTYAMMGF VVWHIGTEVI LEIHAYRLSR
KVEILDNDRI QILQSLTVAE AEGHVFKKVV LAVYICGNVI FLSIFLSAIN HI
