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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

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Iron storage

Keywords - Ligandi

Iron, 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

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002010511 – 181Ferritin heavy chainAdd BLAST181
Initiator methionineiRemoved; alternateBy similarity
ChainiPRO_00004244752 – 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

Structurei

3D structure databases

ProteinModelPortaliP19130.
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
Contains 1 ferritin-like diiron domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG000410.
InParanoidiP19130.
KOiK00522.

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
InterProiIPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR014034. Ferritin_CS.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PANTHERiPTHR11431. PTHR11431. 1 hit.
PfamiPF00210. Ferritin. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP19130.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PeptideAtlasiP19130.
PRIDEiP19130.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397030.
KEGGissc:397030.

Organism-specific databases

CTDi2495.

Phylogenomic databases

HOVERGENiHBG000410.
InParanoidiP19130.
KOiK00522.

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
InterProiIPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR014034. Ferritin_CS.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PANTHERiPTHR11431. PTHR11431. 1 hit.
PfamiPF00210. Ferritin. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFRIH_PIG
AccessioniPrimary (citable) accession number: P19130
Secondary accession number(s): P19131
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 103 of the entry and version 3 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.