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Protein

Ferritin heavy chain

Gene

FTH1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processIron storage
LigandIron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ferritin heavy chain (EC:1.16.3.1)
Short name:
Ferritin H subunit
Cleaved into the following chain:
Gene namesi
Name:FTH1
Synonyms:FTH
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004244751 – 181Ferritin heavy chainAdd BLAST181
Initiator methionineiRemoved; alternateBy similarity
ChainiPRO_00002010512 – 181Ferritin heavy chain, N-terminally processedAdd BLAST180

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei2N-acetylthreonine; in Ferritin heavy chain, N-terminally processedBy similarity1
Modified residuei179PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PeptideAtlasiP19130.
PRIDEiP19130.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

IntActiP19130. 1 interactor.

Structurei

3D structure databases

ProteinModelPortaliP19130.
SMRiP19130.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 160Ferritin-like diironPROSITE-ProRule annotationAdd BLAST150

Sequence similaritiesi

Belongs to the ferritin family.Curated

Phylogenomic databases

HOVERGENiHBG000410.
InParanoidiP19130.
KOiK00522.

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
InterProiView protein in InterPro
IPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR014034. Ferritin_CS.
IPR008331. Ferritin_DPS_dom.
PANTHERiPTHR11431. PTHR11431. 1 hit.
PfamiView protein in Pfam
PF00210. Ferritin. 1 hit.
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiView protein in PROSITE
PS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19130-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTSCSSQVR QNYHQDSEAA INRQINLELY ASYVYLSMSY YFDRDDVALK
60 70 80 90 100
NFAKYFLHQS HGGRGHAEKL MKLQTQRGAR IFLQDIMKPE RDDWENGLTA
110 120 130 140 150
MEFALHVVKN VYQSLLELHK LATDKNDPHL CDFIETHYLH EQVKAIKELG
160 170 180
DHITNLHRMG APEYGMAEYL FDKHTLGSSE S
Length:181
Mass (Da):21,045
Last modified:January 23, 2007 - v3
Checksum:i8E6D9710CC57F757
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti103F → C AA sequence (PubMed:3688879).Curated1
Sequence conflicti107 – 108VV → LE AA sequence (PubMed:3688879).Curated2
Sequence conflicti112Y → N AA sequence (PubMed:3688879).Curated1
Sequence conflicti140H → D AA sequence (PubMed:3688879).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti111V → M. 1
Natural varianti116L → H. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D15071 mRNA. Translation: BAA03666.1.
PIRiS06279.
RefSeqiNP_999140.1. NM_213975.1.
UniGeneiSsc.23940.
Ssc.42834.
Ssc.61.

Genome annotation databases

GeneIDi397030.
KEGGissc:397030.

Similar proteinsi

Entry informationi

Entry nameiFRIH_PIG
AccessioniPrimary (citable) accession number: P19130
Secondary accession number(s): P19131
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: August 30, 2017
This is version 106 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families