Skip Header

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

P17663 (FRIHB_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 86. 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 B
Short name=Ferritin H subunit B
Alternative name(s):
Ferritin heavy chain 1
EC=1.16.3.1
Gene names
Name:fth1-b
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 length176 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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
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 – 176176Ferritin heavy chain B
PRO_0000201077

Regions

Domain7 – 156150Ferritin-like diiron

Sites

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

Experimental info

Sequence conflict61R → L in CAA35760. Ref.1
Sequence conflict151A → I in CAA35760. Ref.1
Sequence conflict157 – 1582VP → A in CAA35760. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P17663 [UniParc].

Last modified November 1, 1991. Version 2.
Checksum: C325E410FB3EC648

FASTA17620,563
        10         20         30         40         50         60 
MQSQVRQNFN SDCEAAINRM VNLEMYASYV YLSMSYYFDR DDVALHHVAK FFKEQSHEER 

        70         80         90        100        110        120 
EHAEKFLKYQ NKRGGRVVLQ DIKKPERDEW SNTLEAMQAA LQLEKTVNQA LLDLHKLASD 

       130        140        150        160        170 
KVDPQLCDFL ESEYLEEQVK AMKELGDYIT NLKRLGVPQN GMGEYLFDKH TLGESS

« Hide

References

« Hide 'large scale' references
[1]"Sequence of Xenopus laevis ferritin mRNA."
Moskaitis J.E., Pastori R.L., Schoenberg D.
Nucleic Acids Res. 18:2184-2184(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Xenopus liver ferritin H subunit: cDNA sequence and mRNA production in the liver following estrogen treatment."
Holland L.J., Wall A.A., Bhattacharya A.
Biochemistry 30:1965-1972(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[3]NIH - Xenopus Gene Collection (XGC) project
Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo and Tail bud.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X51395 mRNA. Translation: CAA35760.1.
M55010 mRNA. Translation: AAA49708.1.
BC044961 mRNA. Translation: AAH44961.1.
BC170380 mRNA. Translation: AAI70380.1.
BC170382 mRNA. Translation: AAI70382.1.
PIRFRXL. A37959.
RefSeqNP_001079580.1. NM_001086111.1.
UniGeneXl.2168.

3D structure databases

ProteinModelPortalP17663.
SMRP17663. Positions 3-172.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID379267.
KEGGxla:379267.

Organism-specific databases

CTD379267.
XenbaseXB-GENE-6256345. fth1.

Phylogenomic databases

HOVERGENHBG000410.
KOK00522.

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 nameFRIHB_XENLA
AccessionPrimary (citable) accession number: P17663
Secondary accession number(s): B7ZS33, Q66LL5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 1, 1991
Last modified: May 1, 2013
This is version 86 of the entry and version 2 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