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Protein

Ferritin, middle subunit

Gene
N/A
Organism
Trematomus newnesi (Dusky notothen)
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 (By similarity).By similarity

Catalytic activityi

4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.1 Publication

Temperature dependencei

Thermostable.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi24 – 241Iron 1PROSITE-ProRule annotationBy similarity
Metal bindingi59 – 591Iron 1PROSITE-ProRule annotationBy similarity
Metal bindingi59 – 591Iron 2PROSITE-ProRule annotationBy similarity
Metal bindingi62 – 621Iron 1PROSITE-ProRule annotationBy similarity
Metal bindingi104 – 1041Iron 2PROSITE-ProRule annotationBy similarity
Metal bindingi138 – 1381Iron 2PROSITE-ProRule annotationBy similarity

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, middle subunit1 Publication (EC:1.16.3.1)
Short name:
Ferritin M1 Publication
OrganismiTrematomus newnesi (Dusky notothen)
Taxonomic identifieri35730 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataEupercariaPerciformesNotothenioideiNototheniidaeTrematomus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 176176Ferritin, middle subunitPRO_0000352783Add
BLAST

Expressioni

Tissue specificityi

Liver and spleen (at protein level).1 Publication

Interactioni

Subunit structurei

In liver, forms a heteropolymer consisting of middle and heavy subunits. In spleen, forms a homopolymer. 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.Curated1 Publication

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 156150Ferritin-like diironPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ferritin family.Sequence Analysis
Contains 1 ferritin-like diiron domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG000410.

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.

P85835-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSQVRQNYH RDCEAAVNRM INMELFASYS YTSMAFYFSR DDVALPGFAH
60 70 80 90 100
FFKENSEEER EHADKLLTFQ NSRGGRIFLQ DIKKPERDEW GSGLDALQSS
110 120 130 140 150
LQLEKNVNQA LLDLHKIASD HTDPHMCDFL ETHYLNEQVE SIKKLGDFIT
160 170
NLSRMDAVKN KMAEYLFDKH TMGGKN
Length:176
Mass (Da):20,450
Last modified:October 14, 2008 - v1
Checksum:i161929EF2565AC4B
GO

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG000410.

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. "The unusual co-assembly of H- and M-chains in the ferritin molecule from the Antarctic teleosts Trematomus bernacchii and Trematomus newnesi."
    Giorgi A., Mignogna G., Bellapadrona G., Gattoni M., Chiaraluce R., Consalvi V., Chiancone E., Stefanini S.
    Arch. Biochem. Biophys. 478:69-74(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, TISSUE SPECIFICITY.
    Tissue: Liver1 Publication and Spleen1 Publication.

Entry informationi

Entry nameiFRIM_TRENE
AccessioniPrimary (citable) accession number: P85835
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: October 14, 2008
Last modified: October 29, 2014
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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.