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Protein

Ferritin heavy chain B

Gene

fth1-b

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 3 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 (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 B
Short name:
Ferritin H subunit B
Alternative name(s):
Ferritin heavy chain 1 (EC:1.16.3.1)
Gene namesi
Name:fth1-b
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6256345. fth1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 176176Ferritin heavy chain BPRO_0000201077Add
BLAST

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

ProteinModelPortaliP17663.
SMRiP17663. Positions 3-172.
ModBaseiSearch...
MobiDBiSearch...

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.Curated
Contains 1 ferritin-like diiron domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG000410.
KOiK00522.

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.

P17663-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQSQVRQNFN SDCEAAINRM VNLEMYASYV YLSMSYYFDR DDVALHHVAK
60 70 80 90 100
FFKEQSHEER EHAEKFLKYQ NKRGGRVVLQ DIKKPERDEW SNTLEAMQAA
110 120 130 140 150
LQLEKTVNQA LLDLHKLASD KVDPQLCDFL ESEYLEEQVK AMKELGDYIT
160 170
NLKRLGVPQN GMGEYLFDKH TLGESS
Length:176
Mass (Da):20,563
Last modified:November 1, 1991 - v2
Checksum:iC325E410FB3EC648
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61R → L in CAA35760. (PubMed:2336402)Curated
Sequence conflicti15 – 151A → I in CAA35760. (PubMed:2336402)Curated
Sequence conflicti157 – 1582VP → A in CAA35760. (PubMed:2336402)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA37959. FRXL.
RefSeqiNP_001079580.1. NM_001086111.1.
UniGeneiXl.2168.

Genome annotation databases

GeneIDi379267.
KEGGixla:379267.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA37959. FRXL.
RefSeqiNP_001079580.1. NM_001086111.1.
UniGeneiXl.2168.

3D structure databases

ProteinModelPortaliP17663.
SMRiP17663. Positions 3-172.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi379267.
KEGGixla:379267.

Organism-specific databases

CTDi379267.
XenbaseiXB-GENE-6256345. fth1.

Phylogenomic databases

HOVERGENiHBG000410.
KOiK00522.

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

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiFRIHB_XENLA
AccessioniPrimary (citable) accession number: P17663
Secondary accession number(s): B7ZS33, Q66LL5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 1, 1991
Last modified: October 1, 2014
This is version 88 of the entry and version 2 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

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.