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Protein

Ferritin heavy chain, oocyte isoform

Gene
N/A
Organism
Xenopus laevis (African clawed frog)
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.

Sites

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

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, oocyte isoform (EC:1.16.3.1)
Alternative name(s):
A-ferritin
GV-HCH
XeAF
OrganismiXenopus laevis (African clawed frog)Imported
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-955508. ftmt.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 177177Ferritin heavy chain, oocyte isoformPRO_0000201079Add
BLAST

Proteomic databases

PRIDEiQ7SXA6.

Interactioni

Subunit structurei

Oligomer of 24 subunits. The functional molecule is roughly spherical and contains a central cavity into which the polymeric mineral iron core is deposited (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ7SXA6.
SMRiQ7SXA6. Positions 3-173.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Belongs to the ferritin family.Curated
Contains 1 ferritin-like diiron domain.CuratedPROSITE-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.
PROSITEiPS00540. FERRITIN_1. 1 hit.
PS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7SXA6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSQIRQNFH QECEAAINRQ VNMELYASYV YLSMSYYFDR DDVALKNFAK
60 70 80 90 100
YFLHQSHEER EHAEKLMKMQ NQRGGRLFLQ DIKKPERDEW ANGLEALECS
110 120 130 140 150
LQLEKNVNQS ILELHKLSTD HNDPHLCDFL ESHYLDEQVK SMKELGDHIT
160 170
NLRRMGAPSN GLAEYLFDKH TLGEDHE
Length:177
Mass (Da):20,918
Last modified:October 1, 2003 - v1
Checksum:iEC490899B62B0C7B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821I → L AA sequence (PubMed:14509834).Curated
Sequence conflicti111 – 1111I → L AA sequence (PubMed:14509834).Curated
Sequence conflicti149 – 1502IT → LA AA sequence (PubMed:14509834).Curated
Sequence conflicti173 – 1742GE → W AA sequence (PubMed:14509834).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF538970 mRNA. Translation: AAQ10928.1.
UniGeneiXl.5269.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF538970 mRNA. Translation: AAQ10928.1.
UniGeneiXl.5269.

3D structure databases

ProteinModelPortaliQ7SXA6.
SMRiQ7SXA6. Positions 3-173.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ7SXA6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

XenbaseiXB-GENE-955508. ftmt.

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

Publicationsi

  1. "Two types of new ferritin cDNA sequences from Xenopus laevis germinal vesicle oocytes."
    Huang W.-H., Guo H.-B., Huang X.-Y., Sun F.-Z.
    DNA Seq. 14:211-214(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 77-83; 106-116; 144-153 AND 155-177.
    Tissue: Oocyte1 Publication.

Entry informationi

Entry nameiFRIH3_XENLA
AccessioniPrimary (citable) accession number: Q7SXA6
Secondary accession number(s): P83457
, P83460, P83462, P83463
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: October 1, 2003
Last modified: October 1, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

There are three types of ferritin subunits in amphibia: L, M and H chains. M and H chains are fast mineralizing; the L chain is very slow mineralizing (By similarity).By similarity

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.