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P19130 (FRIH_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 90. 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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length181 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. 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 By similarity.

Sequence similarities

Belongs to the ferritin family.

Contains 1 ferritin-like diiron domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 181181Ferritin heavy chain
PRO_0000201051
Initiator methionine11Removed; alternate By similarity
Chain2 – 181180Ferritin heavy chain, N-terminally processed
PRO_0000424475

Regions

Domain11 – 160150Ferritin-like diiron

Amino acid modifications

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

Natural variations

Natural variant1111V → M.
Natural variant1161L → H.

Experimental info

Sequence conflict1031F → C AA sequence Ref.2
Sequence conflict107 – 1082VV → LE AA sequence Ref.2
Sequence conflict1121Y → N AA sequence Ref.2
Sequence conflict1401H → D AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P19130 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8E6D9710CC57F757

FASTA18121,045
        10         20         30         40         50         60 
MTTSCSSQVR QNYHQDSEAA INRQINLELY ASYVYLSMSY YFDRDDVALK NFAKYFLHQS 

        70         80         90        100        110        120 
HGGRGHAEKL MKLQTQRGAR IFLQDIMKPE RDDWENGLTA MEFALHVVKN VYQSLLELHK 

       130        140        150        160        170        180 
LATDKNDPHL CDFIETHYLH EQVKAIKELG DHITNLHRMG APEYGMAEYL FDKHTLGSSE 


S 

« Hide

References

[1]Hamasima N., Suzuki H., Fujii H., Ito T., Murakami Y., Yamada R., Yazawa T., Yasue H.
Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Isolation and partial amino acid sequence of three subunit species of porcine spleen ferritin: evidence of multiple H subunits."
Collawn J.F. Jr., Gowan L.K., Crow H., Schwabe C., Fish W.W.
Arch. Biochem. Biophys. 259:105-113(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 102-181.
Tissue: Spleen.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D15071 mRNA. Translation: BAA03666.1.
PIRS06279.
RefSeqNP_999140.1. NM_213975.1.
UniGeneSsc.23940.
Ssc.42834.
Ssc.61.

3D structure databases

ProteinModelPortalP19130.
SMRP19130. Positions 6-177.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397030.
KEGGssc:397030.

Organism-specific databases

CTD2495.

Phylogenomic databases

HOVERGENHBG000410.
KOK00522.

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...

Entry information

Entry nameFRIH_PIG
AccessionPrimary (citable) accession number: P19130
Secondary accession number(s): P19131
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 90 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