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Protein

Ferritin light chain, oocyte isoform

Gene
N/A
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation (By similarity).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).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi26IronPROSITE-ProRule annotationBy similarity1
Metal bindingi64IronPROSITE-ProRule annotationBy similarity1
Metal bindingi106IronPROSITE-ProRule annotationBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processIron storage
LigandIron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ferritin light chain, oocyte isoform
Alternative name(s):
B-ferritin
GV-LCH
XeBF
OrganismiXenopus laevis (African clawed frog)Imported
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Subcellular locationi

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002010801 – 177Ferritin light chain, oocyte isoformAdd BLAST177

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

ProteinModelPortaliQ7SXA5.
SMRiQ7SXA5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 158Ferritin-like diironPROSITE-ProRule annotationCuratedAdd BLAST150

Sequence similaritiesi

Belongs to the ferritin family.Curated

Phylogenomic databases

HOVERGENiHBG000410.

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
InterProiView protein in InterPro
IPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR014034. Ferritin_CS.
IPR008331. Ferritin_DPS_dom.
PANTHERiPTHR11431. PTHR11431. 1 hit.
PfamiView protein in Pfam
PF00210. Ferritin. 1 hit.
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiView protein in PROSITE
PS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7SXA5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAQSQIRQN YHEESEAGVN RIANLELQAS YLYLSVGYYF DRDDVALSKF
60 70 80 90 100
SKFFRELSEK KRDHAEDFLK FQNKRGGRVV LQDVKKPDDD EWGNGTKAME
110 120 130 140 150
VALNLEKSIN QAVLDLHKIA TDHTDPHMQD YLEHEFLEEE VKLIKKLGDH
160 170
LTNLRRVKAA EEGMGEYLFD KLTLGED
Length:177
Mass (Da):20,538
Last modified:October 1, 2003 - v1
Checksum:i9D79BE23C3E25989
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti109I → L AA sequence (PubMed:14509834).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF538971 mRNA. Translation: AAQ10929.1.
UniGeneiXl.26093.

Similar proteinsi

Entry informationi

Entry nameiFRIL_XENLA
AccessioniPrimary (citable) accession number: Q7SXA5
Secondary accession number(s): P83458, P83459, P83461
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: October 1, 2003
Last modified: February 15, 2017
This is version 55 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families