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Protein

Mitoferrin

Gene

mfrn

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Mitochondrial iron transporter that mediates iron uptake. Probably required for heme synthesis of hemoproteins and Fe-S cluster assembly.1 Publication

GO - Molecular functioni

GO - Biological processi

  • mitochondrial iron ion transport Source: UniProtKB
  • mitochondrial transport Source: FlyBase
  • multicellular organismal iron ion homeostasis Source: FlyBase
  • spermatid differentiation Source: FlyBase
  • translation Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Ion transport, Iron transport, Transport

Keywords - Ligandi

Iron

Names & Taxonomyi

Protein namesi
Recommended name:
Mitoferrin
Short name:
dmfrn
Gene namesi
Name:mfrn
ORF Names:CG4963
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0039561. mfrn.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei14 – 3320Helical; Name=1Sequence analysisAdd
BLAST
Transmembranei73 – 9220Helical; Name=2Sequence analysisAdd
BLAST
Transmembranei108 – 12417Helical; Name=3Sequence analysisAdd
BLAST
Transmembranei164 – 18320Helical; Name=4Sequence analysisAdd
BLAST
Transmembranei198 – 21720Helical; Name=5Sequence analysisAdd
BLAST
Transmembranei256 – 27520Helical; Name=6Sequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial inner membrane Source: UniProtKB
  • mitochondrial membrane Source: FlyBase
  • mitochondrion Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 379379MitoferrinPRO_0000235262Add
BLAST

Proteomic databases

PaxDbiQ9VAY3.
PRIDEiQ9VAY3.

Expressioni

Gene expression databases

BgeeiQ9VAY3.
GenevisibleiQ9VAY3. DM.

Interactioni

Protein-protein interaction databases

BioGridi68234. 8 interactions.
IntActiQ9VAY3. 1 interaction.
MINTiMINT-321780.
STRINGi7227.FBpp0084635.

Structurei

3D structure databases

ProteinModelPortaliQ9VAY3.
SMRiQ9VAY3. Positions 14-279.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati12 – 9887Solcar 1Add
BLAST
Repeati105 – 18985Solcar 2Add
BLAST
Repeati196 – 28186Solcar 3Add
BLAST

Sequence similaritiesi

Contains 3 Solcar repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0760. Eukaryota.
ENOG410XNT2. LUCA.
GeneTreeiENSGT00550000074721.
InParanoidiQ9VAY3.
KOiK15113.
OMAiPMRGLNI.
OrthoDBiEOG77DJ7B.
PhylomeDBiQ9VAY3.

Family and domain databases

Gene3Di1.50.40.10. 1 hit.
InterProiIPR002067. Mit_carrier.
IPR018108. Mitochondrial_sb/sol_carrier.
IPR023395. Mt_carrier_dom.
[Graphical view]
PfamiPF00153. Mito_carr. 3 hits.
[Graphical view]
PRINTSiPR00926. MITOCARRIER.
SUPFAMiSSF103506. SSF103506. 1 hit.
PROSITEiPS50920. SOLCAR. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VAY3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIDDYESLP TTSVGVNMTA GAIAGVLEHV VMYPLDSVKT RMQSLSPPTK
60 70 80 90 100
NMNIVSTLRT MITREGLLRP IRGASAVVLG AGPAHSLYFA AYEMTKELTA
110 120 130 140 150
KFTSVRNLNY VISGAVATLI HDAISSPTDV IKQRMQMYNS PYTSVVSCVR
160 170 180 190 200
DIYKREGFKA FYRAYGTQLV MNLPYQTIHF TTYEFFQNKM NLERKYNPPV
210 220 230 240 250
HMAAGAAAGA CAAAVTTPLD VIKTLLNTQE TGLTRGMIEA SRKIYHMAGP
260 270 280 290 300
LGFFRGTTAR VLYSMPATAI CWSTYEFFKF YLCGLDADQY KSSITGSSEP
310 320 330 340 350
RKADYVLPRT TDEEQIDQER EAAKEKDTTA TLHSAPTSVN ASGAIKTVCE
360 370
LSTRPAGPTI NLHTRHTDVK SPYERGFST
Length:379
Mass (Da):41,795
Last modified:May 1, 2000 - v1
Checksum:iF6A20BABA35F5C2E
GO

Sequence cautioni

The sequence AAF73387.1 differs from that shown. Reason: Frameshift at positions 133 and 144. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841A → T in AAF73387 (PubMed:9275195).Curated
Sequence conflicti312 – 3121D → E in AAF73387 (PubMed:9275195).Curated
Sequence conflicti334 – 3341S → C in AAF73387 (PubMed:9275195).Curated
Sequence conflicti339 – 3391V → F in AAF73387 (PubMed:9275195).Curated
Sequence conflicti376 – 3761G → A in AAF73387 (PubMed:9275195).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF217402 mRNA. Translation: AAF73387.1. Frameshift.
AE014297 Genomic DNA. Translation: AAF56764.1.
AY060268 mRNA. Translation: AAL25307.1.
RefSeqiNP_651600.1. NM_143343.3.
UniGeneiDm.4065.

Genome annotation databases

EnsemblMetazoaiFBtr0085266; FBpp0084635; FBgn0039561.
GeneIDi43353.
KEGGidme:Dmel_CG4963.
UCSCiCG4963-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF217402 mRNA. Translation: AAF73387.1. Frameshift.
AE014297 Genomic DNA. Translation: AAF56764.1.
AY060268 mRNA. Translation: AAL25307.1.
RefSeqiNP_651600.1. NM_143343.3.
UniGeneiDm.4065.

3D structure databases

ProteinModelPortaliQ9VAY3.
SMRiQ9VAY3. Positions 14-279.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68234. 8 interactions.
IntActiQ9VAY3. 1 interaction.
MINTiMINT-321780.
STRINGi7227.FBpp0084635.

Proteomic databases

PaxDbiQ9VAY3.
PRIDEiQ9VAY3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0085266; FBpp0084635; FBgn0039561.
GeneIDi43353.
KEGGidme:Dmel_CG4963.
UCSCiCG4963-RA. d. melanogaster.

Organism-specific databases

CTDi43353.
FlyBaseiFBgn0039561. mfrn.

Phylogenomic databases

eggNOGiKOG0760. Eukaryota.
ENOG410XNT2. LUCA.
GeneTreeiENSGT00550000074721.
InParanoidiQ9VAY3.
KOiK15113.
OMAiPMRGLNI.
OrthoDBiEOG77DJ7B.
PhylomeDBiQ9VAY3.

Miscellaneous databases

ChiTaRSimfrn. fly.
GenomeRNAii43353.
PROiQ9VAY3.

Gene expression databases

BgeeiQ9VAY3.
GenevisibleiQ9VAY3. DM.

Family and domain databases

Gene3Di1.50.40.10. 1 hit.
InterProiIPR002067. Mit_carrier.
IPR018108. Mitochondrial_sb/sol_carrier.
IPR023395. Mt_carrier_dom.
[Graphical view]
PfamiPF00153. Mito_carr. 3 hits.
[Graphical view]
PRINTSiPR00926. MITOCARRIER.
SUPFAMiSSF103506. SSF103506. 1 hit.
PROSITEiPS50920. SOLCAR. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A screen for fast evolving genes from Drosophila."
    Schmid K.J., Tautz D.
    Proc. Natl. Acad. Sci. U.S.A. 94:9746-9750(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Canton-S.
    Tissue: Embryo.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  5. "Overexpression of Drosophila mitoferrin in l(2)mbn cells results in dysregulation of Fer1HCH expression."
    Metzendorf C., Wu W., Lind M.I.
    Biochem. J. 421:463-471(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiMFRN_DROME
AccessioniPrimary (citable) accession number: Q9VAY3
Secondary accession number(s): Q9NHY6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  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.