Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q7SXA6 (FRIH3_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ferritin heavy chain, oocyte isoform
EC=1.16.3.1
Alternative name(s):
A-ferritin
GV-HCH
XeAF
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length177 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Subunit structure

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.

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.

Sequence similarities

Belongs to the ferritin family.

Contains 1 ferritin-like diiron domain.

Ontologies

Keywords
   Biological processIron storage
   LigandIron
Metal-binding
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcellular iron ion homeostasis

Inferred from electronic annotation. Source: UniProtKB-KW

iron ion transport

Inferred from electronic annotation. Source: InterPro

   Molecular_functionferric iron binding

Inferred from electronic annotation. Source: InterPro

ferroxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 177177Ferritin heavy chain, oocyte isoform
PRO_0000201079

Regions

Domain7 – 156150Ferritin-like diiron

Sites

Metal binding241Iron 1 By similarity UniProtKB P02794
Metal binding591Iron 1 By similarity UniProtKB P02794
Metal binding591Iron 2 By similarity
Metal binding621Iron 1 By similarity UniProtKB P02794
Metal binding1041Iron 2 By similarity UniProtKB P02794
Metal binding1381Iron 2 By similarity UniProtKB P02794

Experimental info

Sequence conflict821I → L AA sequence Ref.1
Sequence conflict1111I → L AA sequence Ref.1
Sequence conflict149 – 1502IT → LA AA sequence Ref.1
Sequence conflict173 – 1742GE → W AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q7SXA6 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: EC490899B62B0C7B

FASTA17720,918
        10         20         30         40         50         60 
MNSQIRQNFH QECEAAINRQ VNMELYASYV YLSMSYYFDR DDVALKNFAK YFLHQSHEER 

        70         80         90        100        110        120 
EHAEKLMKMQ NQRGGRLFLQ DIKKPERDEW ANGLEALECS LQLEKNVNQS ILELHKLSTD 

       130        140        150        160        170 
HNDPHLCDFL ESHYLDEQVK SMKELGDHIT NLRRMGAPSN GLAEYLFDKH TLGEDHE

« Hide

References

[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: Oocyte.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF538970 mRNA. Translation: AAQ10928.1.
UniGeneXl.5269.

3D structure databases

ProteinModelPortalQ7SXA6.
SMRQ7SXA6. Positions 3-173.
ModBaseSearch...

Proteomic databases

PRIDEQ7SXA6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

XenbaseXB-GENE-955508. ftmt.

Phylogenomic databases

HOVERGENHBG000410.

Family and domain databases

Gene3D1.20.1260.10. 1 hit.
InterProIPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR014034. Ferritin_CS.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PANTHERPTHR11431. PTHR11431. 1 hit.
PfamPF00210. Ferritin. 1 hit.
[Graphical view]
SUPFAMSSF47240. Ferritin/RR_like. 1 hit.
PROSITEPS00540. FERRITIN_1. 1 hit.
PS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFRIH3_XENLA
AccessionPrimary (citable) accession number: Q7SXA6
Secondary accession number(s): P83457 expand/collapse secondary AC list , P83460, P83462, P83463
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: October 1, 2003
Last modified: May 1, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents