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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

  1. ferric iron binding Source: InterPro
  2. ferroxidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular iron ion homeostasis Source: UniProtKB-KW
  2. iron ion transport Source: InterPro
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
ProteomesiUP000008227 Componenti: Unplaced

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 181181Ferritin heavy chainPRO_0000201051Add
BLAST
Initiator methioninei1 – 11Removed; alternateBy similarity
Chaini2 – 181180Ferritin heavy chain, N-terminally processedPRO_0000424475Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylthreonine; in Ferritin heavy chain, N-terminally processedBy similarity
Modified residuei179 – 1791PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

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.
SMRiP19130. Positions 6-177.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 160150Ferritin-like diironPROSITE-ProRule annotationAdd
BLAST

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 22, 2007 - v3
Checksum:i8E6D9710CC57F757
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti103 – 1031F → C AA sequence (PubMed:3688879).Curated
Sequence conflicti107 – 1082VV → LE AA sequence (PubMed:3688879).Curated
Sequence conflicti112 – 1121Y → N AA sequence (PubMed:3688879).Curated
Sequence conflicti140 – 1401H → D AA sequence (PubMed:3688879).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti111 – 1111V → M.
Natural varianti116 – 1161L → H.

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.
SMRiP19130. Positions 6-177.
ModBaseiSearch...
MobiDBiSearch...

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...

Publicationsi

  1. Hamasima N., Suzuki H., Fujii H., Ito T., Murakami Y., Yamada R., Yazawa T., Yasue H.
    Submitted (APR-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(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 102-181.
    Tissue: Spleen.

Entry informationi

Entry nameiFRIH_PIG
AccessioniPrimary (citable) accession number: P19130
Secondary accession number(s): P19131
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1990
Last sequence update: January 22, 2007
Last modified: March 3, 2015
This is version 94 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

External Data

Dasty 3

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 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.