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Protein

Ferritin light chain

Gene

FTL

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
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. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi54IronPROSITE-ProRule annotation1
Metal bindingi57IronPROSITE-ProRule annotation1
Metal bindingi58IronPROSITE-ProRule annotation1
Metal bindingi61IronPROSITE-ProRule annotation1
Metal bindingi64IronPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processIron storage
LigandIron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ferritin light chain
Short name:
Ferritin L subunit
Gene namesi
Name:FTL
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
Proteomesi
  • UP000001595 Componenti: Unplaced

Subcellular locationi

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002010642 – 175Ferritin light chainAdd BLAST174

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiQ5R538.

Interactioni

Subunit structurei

Oligomer of 24 subunits. There are two types of subunits: L (light) chain and H (heavy) chain. The major chain can be light or heavy, depending on the species and tissue type. The functional molecule forms a roughly spherical shell with a diameter of 12 nm and contains a central cavity into which the insoluble mineral iron core is deposited.

Structurei

3D structure databases

ProteinModelPortaliQ5R538.
SMRiQ5R538.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 156Ferritin-like diironPROSITE-ProRule annotationAdd BLAST150

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni54 – 61Catalytic site for iron oxidation8

Sequence similaritiesi

Belongs to the ferritin family.Curated

Phylogenomic databases

eggNOGiENOG410IU16. Eukaryota.
ENOG4111Q1M. LUCA.
HOVERGENiHBG000410.
InParanoidiQ5R538.
KOiK13625.

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
PS00540. FERRITIN_1. 1 hit.
PS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5R538-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSQIRQNYS TDVEAAVNSL VNMYLQASYT YLSLGFYFDR DDVALEGVSH
60 70 80 90 100
FFRELAEEKR EGYERLLKMQ NQRGGRALFQ DIKKPAEDEW GKTPDAMKAA
110 120 130 140 150
MALEKKLNQA LLDLHALGSA HTDPHLCDFL ETHFLDEEVK LIKKMGDHLT
160 170
NLHRLGGPEA GLGEYLFERL TLKHD
Length:175
Mass (Da):20,019
Last modified:January 23, 2007 - v3
Checksum:iB7A89021EE977B04
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR861037 mRNA. Translation: CAH93128.1.
RefSeqiNP_001126850.1. NM_001133378.1.

Genome annotation databases

GeneIDi100173858.
KEGGipon:100173858.

Similar proteinsi

Entry informationi

Entry nameiFRIL_PONAB
AccessioniPrimary (citable) accession number: Q5R538
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: January 23, 2007
Last modified: February 15, 2017
This is version 68 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families