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Q7SXA6

- FRIH3_XENLA

UniProt

Q7SXA6 - FRIH3_XENLA

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Protein
Ferritin heavy chain, oocyte isoform
Gene
N/A
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - 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.

Catalytic activityi

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

Sites

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

GO - Molecular functioni

  1. ferric iron binding Source: InterPro
  2. ferroxidase activity Source: UniProtKB-EC
Complete GO annotation...

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)
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 isoform
PRO_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.

Structurei

3D structure databases

ProteinModelPortaliQ7SXA6.
SMRiQ7SXA6. Positions 3-173.

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.

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

MNSQIRQNFH QECEAAINRQ VNMELYASYV YLSMSYYFDR DDVALKNFAK    50
YFLHQSHEER EHAEKLMKMQ NQRGGRLFLQ DIKKPERDEW ANGLEALECS 100
LQLEKNVNQS ILELHKLSTD HNDPHLCDFL ESHYLDEQVK SMKELGDHIT 150
NLRRMGAPSN GLAEYLFDKH TLGEDHE 177
Length:177
Mass (Da):20,918
Last modified:October 1, 2003 - v1
Checksum:iEC490899B62B0C7B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821I → L AA sequence 1 Publication
Sequence conflicti111 – 1111I → L AA sequence 1 Publication
Sequence conflicti149 – 1502IT → LA AA sequence 1 Publication
Sequence conflicti173 – 1742GE → W AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF538970 mRNA. Translation: AAQ10928.1.
UniGeneiXl.5269.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF538970 mRNA. Translation: AAQ10928.1 .
UniGenei Xl.5269.

3D structure databases

ProteinModelPortali Q7SXA6.
SMRi Q7SXA6. Positions 3-173.
ModBasei Search...

Proteomic databases

PRIDEi Q7SXA6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

Xenbasei XB-GENE-955508. ftmt.

Phylogenomic databases

HOVERGENi HBG000410.

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

  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.

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 16, 2013
This is version 51 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.

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi