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P09528 (FRIH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 127. 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 heavy chain
Short name=Ferritin H subunit
EC=1.16.3.1
Gene names
Name:Fth1
Synonyms:Fth
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 length182 AA.
Sequence statusComplete.
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. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney. Ref.9

Catalytic activity

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

Subunit structure

Oligomer of 24 subunits. There are two types of subunits: L (light) chain and H (heavy) chain. The major chain can be light or heavy, depending on the species and tissue type. The functional molecule forms a roughly spherical shell with a diameter of 12 nm and contains a central cavity into which the insoluble mineral iron core is deposited.

Sequence similarities

Belongs to the ferritin family.

Contains 1 ferritin-like diiron domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 182182Ferritin heavy chain
PRO_0000201049

Regions

Domain11 – 160150Ferritin-like diiron

Sites

Metal binding281Iron 1 By similarity
Metal binding631Iron 1 By similarity
Metal binding631Iron 2 By similarity
Metal binding661Iron 1 By similarity
Metal binding1081Iron 2 By similarity
Metal binding1421Iron 2 By similarity

Experimental info

Sequence conflict171A → S in AAA37612. Ref.5
Sequence conflict1371Y → H in AAA37612. Ref.5
Sequence conflict1401S → N in AAA37612. Ref.5
Sequence conflict1641A → S in AAA37612. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P09528 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 129A8887A2BC650B

FASTA18221,067
        10         20         30         40         50         60 
MTTASPSQVR QNYHQDAEAA INRQINLELY ASYVYLSMSC YFDRDDVALK NFAKYFLHQS 

        70         80         90        100        110        120 
HEEREHAEKL MKLQNQRGGR IFLQDIKKPD RDDWESGLNA MECALHLEKS VNQSLLELHK 

       130        140        150        160        170        180 
LATDKNDPHL CDFIETYYLS EQVKSIKELG DHVTNLRKMG APEAGMAEYL FDKHTLGHGD 


ES

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the mouse ferritin H chain gene."
Yachaou A., Renaudie F., Grandchamp B., Beaumont C.
Nucleic Acids Res. 17:8005-8005(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: BALB/c.
[2]"Nucleotide sequence of cDNA encoding the heavy subunit of mouse macrophage ferritin."
Miyazaki Y., Setoguchi M., Higuchi Y., Yoshida S., Akizuki S., Yamamoto S.
Nucleic Acids Res. 16:10373-10373(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ICR.
Tissue: Macrophage.
[3]"The molecular cloning and characterization of murine ferritin heavy chain, a tumor necrosis factor-inducible gene."
Torti S.V., Kwak E.L., Miller S.C., Miller L.L., Ringold G.M., Myambo K.B., Young A.P., Torti F.M.
J. Biol. Chem. 263:12638-12644(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Murine ferritin heavy chain: isolation and characterization of a functional gene."
Kwak E.L., Torti S.V., Torti F.M.
Gene 94:255-261(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[5]"Transcriptional regulation of ferritin H and L subunits in adult erythroid and liver cells from the mouse. Unambiguous identification of mouse ferritin subunits and in vitro formation of the ferritin shells."
Beaumont C., Dugast I., Renaudie F., Souroujon M., Grandchamp B.
J. Biol. Chem. 264:7498-7504(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]"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: Amnion, Heart and Kidney.
[7]"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: C57BL/6J.
Tissue: Mammary tumor.
[8]Lubec G., Klug S.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 11-23 AND 55-64, MASS SPECTROMETRY.
Tissue: Hippocampus.
[9]"Scara5 is a ferritin receptor mediating non-transferrin iron delivery."
Li J.Y., Paragas N., Ned R.M., Qiu A., Viltard M., Leete T., Drexler I.R., Chen X., Sanna-Cherchi S., Mohammed F., Williams D., Lin C.S., Schmidt-Ott K.M., Andrews N.C., Barasch J.
Dev. Cell 16:35-46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X52561 Genomic DNA. Translation: CAA36795.1.
X12812 mRNA. Translation: CAA31300.1.
J03941 mRNA. Translation: AAA37611.1.
M60170 Genomic DNA. Translation: AAA37613.1.
M24509 mRNA. Translation: AAA37612.1.
AK027998 mRNA. Translation: BAC25694.1.
AK139622 mRNA. Translation: BAE24084.1.
AK147082 mRNA. Translation: BAE27662.1.
AK150262 mRNA. Translation: BAE29419.1.
AK150508 mRNA. Translation: BAE29621.1.
AK150628 mRNA. Translation: BAE29718.1.
AK150679 mRNA. Translation: BAE29759.1.
AK150693 mRNA. Translation: BAE29772.1.
AK151192 mRNA. Translation: BAE30189.1.
AK151241 mRNA. Translation: BAE30233.1.
AK151399 mRNA. Translation: BAE30367.1.
AK151609 mRNA. Translation: BAE30548.1.
AK151675 mRNA. Translation: BAE30600.1.
AK152071 mRNA. Translation: BAE30924.1.
AK152542 mRNA. Translation: BAE31297.1.
AK152702 mRNA. Translation: BAE31431.1.
AK153017 mRNA. Translation: BAE31651.1.
AK153195 mRNA. Translation: BAE31795.1.
AK153199 mRNA. Translation: BAE31799.1.
AK159243 mRNA. Translation: BAE34925.1.
AK168601 mRNA. Translation: BAE40468.1.
AK169004 mRNA. Translation: BAE40803.1.
BC012314 mRNA. Translation: AAH12314.1.
IPIIPI00230145.
PIRS06070.
RefSeqNP_034369.1. NM_010239.2.
UniGeneMm.1776.

3D structure databases

ProteinModelPortalP09528.
SMRP09528. Positions 7-177.
ModBaseSearch...

Protein-protein interaction databases

IntActP09528. 3 interactions.
STRING10090.ENSMUSP00000025563.

PTM databases

PhosphoSiteP09528.

2D gel databases

REPRODUCTION-2DPAGEP09528.

Proteomic databases

PaxDbP09528.
PRIDEP09528.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025563; ENSMUSP00000025563; ENSMUSG00000024661.
GeneID14319.
KEGGmmu:14319.
UCSCuc008got.1. mouse.

Organism-specific databases

CTD2495.
MGIMGI:95588. Fth1.

Phylogenomic databases

eggNOGCOG1528.
GeneTreeENSGT00700000104283.
HOGENOMHOG000223383.
HOVERGENHBG000410.
InParanoidP09528.
KOK00522.
OMAASENNDP.
OrthoDBEOG47PX78.

Gene expression databases

BgeeP09528.
CleanExMM_FTH1.
GenevestigatorP09528.
GermOnlineENSMUSG00000024661. 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

ChiTaRSFTH1. mouse.
NextBio285759.
SOURCESearch...

Entry information

Entry nameFRIH_MOUSE
AccessionPrimary (citable) accession number: P09528
Secondary accession number(s): Q3UI44
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 127 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