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Protein

Ferric-chelate reductase 1

Gene

FRRS1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Ferric-chelate reductases reduce Fe3+ to Fe2+ before its transport from the endosome to the cytoplasm.1 Publication

Cofactori

hemeBy similarityNote: Binds 2 heme groups non-covalently.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi373 – 3731Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi414 – 4141Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi446 – 4461Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi482 – 4821Iron (heme axial ligand)PROSITE-ProRule annotation

GO - Molecular functioni

  • ferric-chelate reductase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ferric-chelate reductase 1 (EC:1.-.-.-)
Alternative name(s):
Stromal cell-derived receptor 2
Short name:
SDR-2
Gene namesi
Name:FRRS1
Synonyms:Sdfr2, Sdr2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:108076. Frrs1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei2 – 2221Helical; Name=1Sequence analysisAdd
BLAST
Transmembranei372 – 39221Helical; Name=2Sequence analysisAdd
BLAST
Transmembranei415 – 43521Helical; Name=3Sequence analysisAdd
BLAST
Transmembranei446 – 46621Helical; Name=4Sequence analysisAdd
BLAST
Transmembranei477 – 49923Helical; Name=5Sequence analysisAdd
BLAST
Transmembranei515 – 53521Helical; Name=6Sequence analysisAdd
BLAST
Transmembranei569 – 58921Helical; Name=7Sequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 592592Ferric-chelate reductase 1PRO_0000314844Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi85 – 851N-linked (GlcNAc...)Sequence analysis
Glycosylationi308 – 3081N-linked (GlcNAc...)Sequence analysis
Glycosylationi321 – 3211N-linked (GlcNAc...)1 Publication
Glycosylationi353 – 3531N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ8K385.
PaxDbiQ8K385.
PRIDEiQ8K385.

PTM databases

PhosphoSiteiQ8K385.

Expressioni

Tissue specificityi

Expressed in spleen, liver and kidney with low expression in brain. Localizes in adult brain to the choroid plexus of the fourth, third, and lateral ventricles and to ependymal cells that line the ventricles.2 Publications

Inductioni

Down-regulated in kidney and liver of mice lacking hypotransferrinemic (hpx), which have iron overload of the liver and pancreas.1 Publication

Gene expression databases

BgeeiQ8K385.
CleanExiMM_FRRS1.

Interactioni

Protein-protein interaction databases

BioGridi203144. 1 interaction.
STRINGi10090.ENSMUSP00000039487.

Structurei

3D structure databases

ProteinModelPortaliQ8K385.
SMRiQ8K385. Positions 58-154.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 179167ReelinPROSITE-ProRule annotationAdd
BLAST
Domaini216 – 331116DOMONPROSITE-ProRule annotationAdd
BLAST
Domaini335 – 534200Cytochrome b561PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the FRRS1 family.Curated
Contains 1 cytochrome b561 domain.PROSITE-ProRule annotation
Contains 1 DOMON domain.PROSITE-ProRule annotation
Contains 1 reelin domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4293. Eukaryota.
ENOG410XR70. LUCA.
HOGENOMiHOG000112648.
HOVERGENiHBG107929.
InParanoidiQ8K385.
OrthoDBiEOG7K3TKQ.
PhylomeDBiQ8K385.
TreeFamiTF316169.

Family and domain databases

InterProiIPR006593. Cyt_b561/ferric_Rdtase_TM.
IPR005018. DOMON_domain.
IPR002861. Reeler_dom.
[Graphical view]
PfamiPF03351. DOMON. 1 hit.
PF02014. Reeler. 1 hit.
[Graphical view]
SMARTiSM00665. B561. 1 hit.
SM00664. DoH. 1 hit.
[Graphical view]
PROSITEiPS50939. CYTOCHROME_B561. 1 hit.
PS50836. DOMON. 1 hit.
PS51019. REELIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8K385-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPQITLSV LVIALLTCSV TAYPNGKVPM SCGGMIPQHN HSPQSEPIHQ
60 70 80 90 100
ITVSQTTFKP GDQIEVTLSG PPFRGFLLEA RDAENLSGPP IGSFTLIDSE
110 120 130 140 150
ESQLLTCTDV QGLAVSHTRS SKKTEIKVYW DAPSPAPDHI RFLATVVQKF
160 170 180 190 200
KIYWVKIPSP VISQPNAPPF TTPKATTQPL TTPPSVSHLT KPFSAFECGN
210 220 230 240 250
KKFCVRSPLN CDPEKEPACV FLSFTRDNQS VMVEMSGPSD GYVSFAFSHD
260 270 280 290 300
QWMGDDDAYL CIREDQTVDI QPSYLTGRSY PVMDSRGTLE DMAWRLADGV
310 320 330 340 350
IQCSFRRNIT LPEAKNRFVL NESYYIFFAE GPSHDGRIFR HSQQPLITYE
360 370 380 390 400
KYNVTDTPKS VGGSRSSPLL KAHGALMFVA WMTTVSIGVL VARFFRSVWS
410 420 430 440 450
KAFFLREAAW FQVHRMLMVA TSLLTCVAFV LPFVYRGGWS WRAGYHPYLG
460 470 480 490 500
CTVMTLAVLQ PLLATFRPPL HDPRRQVFNW THWSVGTAAR IIAVAAMFLG
510 520 530 540 550
MDLPGLNLPS PQKTYAMMGF VVWHIGTEVI LEIHAYRLSR KVEILDNDRI
560 570 580 590
QILQSLTVAE AEGHVFKKVV LAVYICGNVI FLSIFLSAIN HI
Length:592
Mass (Da):66,047
Last modified:October 1, 2002 - v1
Checksum:iEAC9146163E85ED3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91S → R in BAA09055 (PubMed:8938438).Curated
Sequence conflicti61 – 611G → E in BAA09055 (PubMed:8938438).Curated
Sequence conflicti65 – 651E → K in BAE26143 (PubMed:16141072).Curated
Sequence conflicti65 – 651E → K in BAE39395 (PubMed:16141072).Curated
Sequence conflicti65 – 651E → K in BAE37025 (PubMed:16141072).Curated
Sequence conflicti272 – 2721P → S in BAE39395 (PubMed:16141072).Curated
Sequence conflicti272 – 2721P → S in BAE37025 (PubMed:16141072).Curated
Sequence conflicti299 – 2991G → S in BAE39395 (PubMed:16141072).Curated
Sequence conflicti299 – 2991G → S in BAE37025 (PubMed:16141072).Curated
Sequence conflicti419 – 4191V → I in BAA09055 (PubMed:8938438).Curated
Sequence conflicti428 – 4281A → G in BAA09055 (PubMed:8938438).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50464 mRNA. Translation: BAA09055.1.
AK144933 mRNA. Translation: BAE26143.1.
AK162693 mRNA. Translation: BAE37025.1.
AK167289 mRNA. Translation: BAE39395.1.
BC027770 mRNA. Translation: AAH27770.1.
CCDSiCCDS17792.1.
RefSeqiNP_001106950.1. NM_001113478.1.
NP_033172.2. NM_009146.3.
XP_011238351.1. XM_011240049.1.
UniGeneiMm.66293.

Genome annotation databases

GeneIDi20321.
KEGGimmu:20321.
UCSCiuc008rcv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50464 mRNA. Translation: BAA09055.1.
AK144933 mRNA. Translation: BAE26143.1.
AK162693 mRNA. Translation: BAE37025.1.
AK167289 mRNA. Translation: BAE39395.1.
BC027770 mRNA. Translation: AAH27770.1.
CCDSiCCDS17792.1.
RefSeqiNP_001106950.1. NM_001113478.1.
NP_033172.2. NM_009146.3.
XP_011238351.1. XM_011240049.1.
UniGeneiMm.66293.

3D structure databases

ProteinModelPortaliQ8K385.
SMRiQ8K385. Positions 58-154.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203144. 1 interaction.
STRINGi10090.ENSMUSP00000039487.

PTM databases

PhosphoSiteiQ8K385.

Proteomic databases

MaxQBiQ8K385.
PaxDbiQ8K385.
PRIDEiQ8K385.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi20321.
KEGGimmu:20321.
UCSCiuc008rcv.2. mouse.

Organism-specific databases

CTDi391059.
MGIiMGI:108076. Frrs1.

Phylogenomic databases

eggNOGiKOG4293. Eukaryota.
ENOG410XR70. LUCA.
HOGENOMiHOG000112648.
HOVERGENiHBG107929.
InParanoidiQ8K385.
OrthoDBiEOG7K3TKQ.
PhylomeDBiQ8K385.
TreeFamiTF316169.

Miscellaneous databases

ChiTaRSiFrrs1. mouse.
NextBioi298119.
PROiQ8K385.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K385.
CleanExiMM_FRRS1.

Family and domain databases

InterProiIPR006593. Cyt_b561/ferric_Rdtase_TM.
IPR005018. DOMON_domain.
IPR002861. Reeler_dom.
[Graphical view]
PfamiPF03351. DOMON. 1 hit.
PF02014. Reeler. 1 hit.
[Graphical view]
SMARTiSM00665. B561. 1 hit.
SM00664. DoH. 1 hit.
[Graphical view]
PROSITEiPS50939. CYTOCHROME_B561. 1 hit.
PS50836. DOMON. 1 hit.
PS51019. REELIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of novel secreted and membrane proteins isolated by the signal sequence trap method."
    Shirozu M., Tada H., Tashiro K., Nakamura T., Lopez N.D., Nazarea M., Hamada T., Sato T., Nakano T., Honjo T.
    Genomics 37:273-280(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Mammary gland and Vagina.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "Stromal cell-derived receptor 2 and cytochrome b561 are functional ferric reductases."
    Vargas J.D., Herpers B., McKie A.T., Gledhill S., McDonnell J., van den Heuvel M., Davies K.E., Ponting C.P.
    Biochim. Biophys. Acta 1651:116-123(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME ACTIVITY, TISSUE SPECIFICITY, INDUCTION.
  5. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-321 AND ASN-353.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Liver.

Entry informationi

Entry nameiFRRS1_MOUSE
AccessioniPrimary (citable) accession number: Q8K385
Secondary accession number(s): P97301, Q3TJV0, Q3UMF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 1, 2002
Last modified: May 11, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.