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P17663

- FRIHB_XENLA

UniProt

P17663 - FRIHB_XENLA

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Protein
Ferritin heavy chain B
Gene
fth1-b
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - 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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi24 – 241Iron 1 By similarity
Metal bindingi59 – 591Iron 1 By similarity
Metal bindingi59 – 591Iron 2 By similarity
Metal bindingi62 – 621Iron 1 By similarity
Metal bindingi104 – 1041Iron 2 By similarity
Metal bindingi138 – 1381Iron 2 By 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 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 B
PRO_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.

Structurei

3D structure databases

ProteinModelPortaliP17663.
SMRiP17663. Positions 3-172.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 156150Ferritin-like diiron
Add
BLAST

Sequence similaritiesi

Belongs to the ferritin family.

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

MQSQVRQNFN SDCEAAINRM VNLEMYASYV YLSMSYYFDR DDVALHHVAK    50
FFKEQSHEER EHAEKFLKYQ NKRGGRVVLQ DIKKPERDEW SNTLEAMQAA 100
LQLEKTVNQA LLDLHKLASD KVDPQLCDFL ESEYLEEQVK AMKELGDYIT 150
NLKRLGVPQN GMGEYLFDKH TLGESS 176
Length:176
Mass (Da):20,563
Last modified:November 1, 1991 - v2
Checksum:iC325E410FB3EC648
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61R → L in CAA35760. 1 Publication
Sequence conflicti15 – 151A → I in CAA35760. 1 Publication
Sequence conflicti157 – 1582VP → A in CAA35760. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi A37959. FRXL.
RefSeqi NP_001079580.1. NM_001086111.1.
UniGenei Xl.2168.

3D structure databases

ProteinModelPortali P17663.
SMRi P17663. Positions 3-172.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 379267.
KEGGi xla:379267.

Organism-specific databases

CTDi 379267.
Xenbasei XB-GENE-6256345. fth1.

Phylogenomic databases

HOVERGENi HBG000410.
KOi K00522.

Family and domain databases

Gene3Di 1.20.1260.10. 1 hit.
InterProi IPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR014034. Ferritin_CS.
IPR008331. Ferritin_DPS_dom.
[Graphical view ]
PANTHERi PTHR11431. PTHR11431. 1 hit.
Pfami PF00210. Ferritin. 1 hit.
[Graphical view ]
SUPFAMi SSF47240. SSF47240. 1 hit.
PROSITEi PS00540. FERRITIN_1. 1 hit.
PS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 16, 2013
This is version 87 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.

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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