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Q8N4E7 (FTMT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ferritin, mitochondrial

EC=1.16.3.1
Gene names
Name:FTMT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length242 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Ref.2 Ref.3

Catalytic activity

4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.

Subunit structure

Homooligomer of 24 subunits. The functional molecule is roughly spherical and contains a central cavity into which the polymeric mineral iron core is deposited.

Subcellular location

Mitochondrion Ref.2.

Tissue specificity

Detected in testis and erythroleukemia. Expression is very low or not detectable in brain, colon, heart, kidney, liver, lung, muscle, placental, spleen and small intestine. Ref.2

Sequence similarities

Belongs to the ferritin family.

Contains 1 ferritin-like diiron domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4949Mitochondrion Potential
Chain50 – 242193Ferritin, mitochondrial
PRO_0000008850

Regions

Domain70 – 219150Ferritin-like diiron

Sites

Metal binding871Iron 1
Metal binding1221Iron 1
Metal binding1221Iron 2
Metal binding1251Iron 1
Metal binding1671Iron 2
Metal binding2011Iron 2 By similarity

Experimental info

Mutagenesis2041S → A: Increases ferroxidase activity and iron binding. Ref.3

Secondary structure

................ 242
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8N4E7 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 29E4B41616A74A3F

FASTA24227,538
        10         20         30         40         50         60 
MLSCFRLLSR HISPSLASLR PVRCCFALPL RWAPGRPLDP RQIAPRRPLA AAASSRDPTG 

        70         80         90        100        110        120 
PAAGPSRVRQ NFHPDSEAAI NRQINLELYA SYVYLSMAYY FSRDDVALNN FSRYFLHQSR 

       130        140        150        160        170        180 
EETEHAEKLM RLQNQRGGRI RLQDIKKPEQ DDWESGLHAM ECALLLEKNV NQSLLELHAL 

       190        200        210        220        230        240 
ASDKGDPHLC DFLETYYLNE QVKSIKELGD HVHNLVKMGA PDAGLAEYLF DTHTLGNENK 


QN 

« Hide

References

« Hide 'large scale' references
[1]"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].
Tissue: Brain.
[2]"A human mitochondrial ferritin encoded by an intronless gene."
Levi S., Corsi B., Bosisio M., Invernizzi R., Volz A., Sanford D., Arosio P., Drysdale J.
J. Biol. Chem. 276:24437-24440(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]"Crystal structure and biochemical properties of the human mitochondrial ferritin and its mutant Ser144Ala."
Langlois d'Estaintot B., Santambrogio P., Granier T., Gallois B., Chevalier J.M., Precigoux G., Levi S., Arosio P.
J. Mol. Biol. 340:277-293(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 61-242, FUNCTION, MUTAGENESIS OF SER-204.
+Additional computationally mapped references.

Web resources

Wikipedia

Ferritin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC034419 mRNA. Translation: AAH34419.1.
RefSeqNP_803431.1. NM_177478.1.
UniGeneHs.105324.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1R03X-ray1.70A61-242[»]
ProteinModelPortalQ8N4E7.
SMRQ8N4E7. Positions 66-235.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000313691.

Polymorphism databases

DMDM62900307.

Proteomic databases

PaxDbQ8N4E7.
PRIDEQ8N4E7.

Protocols and materials databases

DNASU94033.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000321339; ENSP00000313691; ENSG00000181867.
GeneID94033.
KEGGhsa:94033.
UCSCuc003kss.3. human.

Organism-specific databases

CTD94033.
GeneCardsGC05P121215.
HGNCHGNC:17345. FTMT.
MIM608847. gene.
neXtProtNX_Q8N4E7.
PharmGKBPA134941146.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1528.
HOGENOMHOG000223383.
HOVERGENHBG000410.
InParanoidQ8N4E7.
KOK00522.
OMAFLETYYL.
OrthoDBEOG7DRJ49.
PhylomeDBQ8N4E7.
TreeFamTF313885.

Gene expression databases

BgeeQ8N4E7.
CleanExHS_FTMT.
GenevestigatorQ8N4E7.

Family and domain databases

Gene3D1.20.1260.10. 1 hit.
InterProIPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR014034. Ferritin_CS.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PANTHERPTHR11431. PTHR11431. 1 hit.
PfamPF00210. Ferritin. 1 hit.
[Graphical view]
SUPFAMSSF47240. SSF47240. 1 hit.
PROSITEPS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8N4E7.
GeneWikiMitochondrial_ferritin.
GenomeRNAi94033.
NextBio78343.
PROQ8N4E7.
SOURCESearch...

Entry information

Entry nameFTMT_HUMAN
AccessionPrimary (citable) accession number: Q8N4E7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: October 1, 2002
Last modified: February 19, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM