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Q95MP7 (FRIH_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Names and origin

Protein namesRecommended name:
Ferritin heavy chain

Short name=Ferritin H subunit
EC=1.16.3.1

Cleaved into the following chain:

  1. Ferritin heavy chain, N-terminally processed
Gene names
Name:FTH1
Synonyms:FTH
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length183 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. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney By similarity.

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 – 183183Ferritin heavy chain
PRO_0000201046
Initiator methionine11Removed; alternate By similarity
Chain2 – 183182Ferritin heavy chain, N-terminally processed
PRO_0000424469

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

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue21N-acetylthreonine; in Ferritin heavy chain, N-terminally processed By similarity
Modified residue1791Phosphoserine By similarity
Modified residue1831Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q95MP7 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 9D22750A1AC4BE72

FASTA18321,308
        10         20         30         40         50         60 
MTTASPSQVR QNYHQDSEAA INRQINLELY ASYVYLSMSY YFDRDDVALK NFAKYFLHQS 

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

       130        140        150        160        170        180 
LATDKNDPHL CDFIETHYLN EQVKSIKELG DHVTNLRKMG APESGMAEYL FDKHTLGNSD 


NES 

« Hide

References

[1]Jeoung D., Jung D., Kim H.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequence analysis of canine and equine ferritin H and L subunit cDNAs."
Orino K., Miura T., Muto S., Watanabe K.
DNA Seq. 16:58-64(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver and Spleen.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF285177 mRNA. Translation: AAK82992.1.
AB175610 mRNA. Translation: BAD96175.1.
AB175611 mRNA. Translation: BAD96176.1.
RefSeqNP_001003080.1. NM_001003080.1.
NP_001180585.1. NM_001193656.1.
UniGeneCfa.38608.
Cfa.47833.

3D structure databases

ProteinModelPortalQ95MP7.
SMRQ95MP7. Positions 7-177.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ95MP7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSCAFT00000025200; ENSCAFP00000023396; ENSCAFG00000015901.
ENSCAFT00000038151; ENSCAFP00000033829; ENSCAFG00000030465.
GeneID100499480.
403631.
KEGGcfa:100499480.
cfa:403631.

Organism-specific databases

CTD2495.

Phylogenomic databases

eggNOGCOG1528.
GeneTreeENSGT00700000104283.
HOGENOMHOG000223383.
HOVERGENHBG000410.
InParanoidQ95MP7.
KOK00522.
OMAAMAYHFD.
OrthoDBEOG7DRJ49.
TreeFamTF313885.

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

Other

NextBio20817136.

Entry information

Entry nameFRIH_CANFA
AccessionPrimary (citable) accession number: Q95MP7
Secondary accession number(s): Q53VC0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 79 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families