Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9D5H4 (FTMT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ferritin, mitochondrial
EC=1.16.3.1
Gene names
Name:Ftmt
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length237 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

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 By similarity.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the ferritin family.

Contains 1 ferritin-like diiron domain.

Sequence caution

The sequence BAB29806.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4949Mitochondrion Potential
Chain50 – 237188Ferritin, mitochondrial
PRO_0000008851

Regions

Domain66 – 215150Ferritin-like diiron

Sites

Metal binding831Iron 1 By similarity
Metal binding1181Iron 1 By similarity
Metal binding1181Iron 2 By similarity
Metal binding1211Iron 1 By similarity
Metal binding1631Iron 2 By similarity
Metal binding1971Iron 2 By similarity

Experimental info

Sequence conflict1631E → G in BAB29831. Ref.1
Sequence conflict1641K → R in BAB29806. Ref.1
Sequence conflict1671N → T in BAB29806. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9D5H4 [UniParc].

Last modified April 26, 2005. Version 2.
Checksum: 6EC3D9B1539B3B5E

FASTA23727,158
        10         20         30         40         50         60 
MLSCFWFFSK HISSALMSLP RVLHRFTAPQ CLASRYPLGP LLASPRRLLA SVASSQDSTR 

        70         80         90        100        110        120 
PSRVRQNFHP DSEAAINRQI NLELYASYVY LSMAYYFSRD DVALYNFSKY FLRQSLEERE 

       130        140        150        160        170        180 
HAEKLMKLQN QRGGRICLQD IKKPDKDDWE CGLRAMECAL LLEKNVNQSL LDLHTLASEK 

       190        200        210        220        230 
GDPHLCDFLE THYLHEQVKS IKELGDHVHN LVTMGAPAAG LAEYLFDKHT LGSESKH

« Hide

References

[1]"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. expand/collapse author list , 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: Testis.
[2]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK015346 mRNA. Translation: BAB29806.1. Different initiation.
AK015400 mRNA. Translation: BAB29831.1.
AK133009 mRNA. Translation: BAE21468.1.
BC115514 mRNA. Translation: AAI15515.1.
BC115515 mRNA. Translation: AAI15516.1.
IPIIPI00107983.
RefSeqNP_080562.2. NM_026286.3.
UniGeneMm.179144.

3D structure databases

ProteinModelPortalQ9D5H4.
SMRQ9D5H4. Positions 62-231.
ModBaseSearch...

Proteomic databases

PaxDbQ9D5H4.
PRIDEQ9D5H4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025388; ENSMUSP00000025388; ENSMUSG00000024510.
GeneID67634.
KEGGmmu:67634.
UCSCuc008exc.2. mouse.

Organism-specific databases

CTD94033.
MGIMGI:1914884. Ftmt.

Phylogenomic databases

eggNOGCOG1528.
GeneTreeENSGT00700000104283.
HOGENOMHOG000223383.
HOVERGENHBG000410.
InParanoidQ14BZ8.
KOK00522.
OMADYLNRIG.
OrthoDBEOG47PX78.

Gene expression databases

BgeeQ9D5H4.
CleanExMM_FTMT.
GenevestigatorQ9D5H4.
GermOnlineENSMUSG00000024510. Mus musculus.

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. Ferritin/RR_like. 1 hit.
PROSITEPS00540. FERRITIN_1. 1 hit.
PS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio325089.
SOURCESearch...

Entry information

Entry nameFTMT_MOUSE
AccessionPrimary (citable) accession number: Q9D5H4
Secondary accession number(s): Q14BZ8, Q3V0N6, Q9D5F4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 26, 2005
Last modified: May 1, 2013
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents