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Protein

Ferritin heavy chain

Gene

FTH1

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi28Iron 1PROSITE-ProRule annotation1
Metal bindingi63Iron 1PROSITE-ProRule annotation1
Metal bindingi63Iron 2PROSITE-ProRule annotation1
Metal bindingi66Iron 1PROSITE-ProRule annotation1
Metal bindingi108Iron 2PROSITE-ProRule annotation1
Metal bindingi142Iron 2PROSITE-ProRule annotation1

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
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componentsi: Chromosome 11, Chromosome 18

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002010461 – 183Ferritin heavy chainAdd BLAST183
Initiator methionineiRemoved; alternateBy similarity
ChainiPRO_00004244692 – 183Ferritin heavy chain, N-terminally processedAdd BLAST182

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
Modified residuei183PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ95MP7.
PRIDEiQ95MP7.

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.

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000033829.

Structurei

3D structure databases

ProteinModelPortaliQ95MP7.
SMRiQ95MP7.
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

eggNOGiKOG2332. Eukaryota.
COG1528. LUCA.
GeneTreeiENSGT00760000119129.
HOGENOMiHOG000223383.
HOVERGENiHBG000410.
InParanoidiQ95MP7.
KOiK00522.
OMAiFMEYQNQ.
OrthoDBiEOG091G0J20.
TreeFamiTF313885.

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.
PROSITEiPS00540. FERRITIN_1. 1 hit.
PS00204. 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.

Q95MP7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTASPSQVR QNYHQDSEAA INRQINLELY ASYVYLSMSY YFDRDDVALK
60 70 80 90 100
NFAKYFLHQS HEEREHAEKL MKLQNQRGGR IFLQDIKKPD RDDWENGLNA
110 120 130 140 150
MECALHLEKS VNQSLLELHK LATDKNDPHL CDFIETHYLN EQVKSIKELG
160 170 180
DHVTNLRKMG APESGMAEYL FDKHTLGNSD NES
Length:183
Mass (Da):21,308
Last modified:January 23, 2007 - v3
Checksum:i9D22750A1AC4BE72
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF285177 mRNA. Translation: AAK82992.1.
AB175610 mRNA. Translation: BAD96175.1.
AB175611 mRNA. Translation: BAD96176.1.
RefSeqiNP_001003080.1. NM_001003080.1.
NP_001180585.1. NM_001193656.1.
UniGeneiCfa.38608.
Cfa.47833.

Genome annotation databases

EnsembliENSCAFT00000025200; ENSCAFP00000023396; ENSCAFG00000015901.
ENSCAFT00000038151; ENSCAFP00000033829; ENSCAFG00000030465.
GeneIDi100499480.
403631.
KEGGicfa:100499480.
cfa:403631.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF285177 mRNA. Translation: AAK82992.1.
AB175610 mRNA. Translation: BAD96175.1.
AB175611 mRNA. Translation: BAD96176.1.
RefSeqiNP_001003080.1. NM_001003080.1.
NP_001180585.1. NM_001193656.1.
UniGeneiCfa.38608.
Cfa.47833.

3D structure databases

ProteinModelPortaliQ95MP7.
SMRiQ95MP7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000033829.

Proteomic databases

PaxDbiQ95MP7.
PRIDEiQ95MP7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCAFT00000025200; ENSCAFP00000023396; ENSCAFG00000015901.
ENSCAFT00000038151; ENSCAFP00000033829; ENSCAFG00000030465.
GeneIDi100499480.
403631.
KEGGicfa:100499480.
cfa:403631.

Organism-specific databases

CTDi2495.

Phylogenomic databases

eggNOGiKOG2332. Eukaryota.
COG1528. LUCA.
GeneTreeiENSGT00760000119129.
HOGENOMiHOG000223383.
HOVERGENiHBG000410.
InParanoidiQ95MP7.
KOiK00522.
OMAiFMEYQNQ.
OrthoDBiEOG091G0J20.
TreeFamiTF313885.

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.
PROSITEiPS00540. FERRITIN_1. 1 hit.
PS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFRIH_CANLF
AccessioniPrimary (citable) accession number: Q95MP7
Secondary accession number(s): Q53VC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 96 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, 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.