Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ferritin light chain

Gene

FTL

Organism
Equus caballus (Horse)
Status
Reviewed-Annotation score: Annotation score: 4 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. 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

Complete GO annotation...

Keywords - Biological processi

Iron storage

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ferritin light chain
Short name:
Ferritin L subunit
Gene namesi
Name:FTL
OrganismiEquus caballus (Horse)
Taxonomic identifieri9796 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
Proteomesi
  • UP000002281 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1293254.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00002010592 – 175Ferritin light chainAdd BLAST174

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

PeptideAtlasiP02791.
PRIDEiP02791.

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

Secondary structure

1175
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni3 – 5Combined sources3
Helixi11 – 38Combined sources28
Turni41 – 43Combined sources3
Helixi46 – 73Combined sources28
Helixi93 – 120Combined sources28
Helixi124 – 133Combined sources10
Helixi135 – 158Combined sources24
Helixi160 – 170Combined sources11
Turni171 – 174Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AEWX-ray1.95A2-175[»]
1DATX-ray2.05A2-175[»]
1GWGX-ray2.01A2-175[»]
1HRSX-ray2.60A2-175[»]
1IERX-ray2.26A2-175[»]
1IESX-ray2.60A/B/C/D/E/F2-175[»]
1XZ1X-ray1.75A2-175[»]
1XZ3X-ray1.75A2-175[»]
2G4HX-ray2.00A2-175[»]
2GYDX-ray1.72A3-172[»]
2V2IX-ray2.00A2-175[»]
2V2JX-ray2.22A2-175[»]
2V2LX-ray1.90A2-175[»]
2V2MX-ray1.65A2-175[»]
2V2NX-ray1.55A2-175[»]
2V2OX-ray1.87A2-175[»]
2V2PX-ray1.15A2-175[»]
2V2RX-ray1.90A2-175[»]
2V2SX-ray1.37A2-175[»]
2W0OX-ray1.50A2-175[»]
2Z5PX-ray1.65A2-175[»]
2Z5QX-ray2.10A2-175[»]
2Z5RX-ray2.50A2-175[»]
2ZA6X-ray1.75A1-175[»]
2ZA7X-ray1.40A5-175[»]
2ZA8X-ray1.40A9-175[»]
2ZG7X-ray1.70X2-175[»]
2ZG8X-ray1.60X2-175[»]
2ZG9X-ray1.75X2-175[»]
2ZURX-ray1.80X2-175[»]
3AF7X-ray1.58X2-175[»]
3AF8X-ray1.66X2-175[»]
3AF9X-ray1.85X2-175[»]
3F32X-ray1.70A2-175[»]
3F33X-ray1.70A2-175[»]
3F34X-ray1.68A2-175[»]
3F35X-ray1.92A2-175[»]
3F36X-ray1.70A2-175[»]
3F37X-ray1.54A2-175[»]
3F38X-ray1.75A2-175[»]
3F39X-ray1.85A2-175[»]
3FI6X-ray1.80A2-175[»]
3H7GX-ray1.65A2-175[»]
3NOZX-ray1.52X2-175[»]
3NP0X-ray1.48X2-175[»]
3NP2X-ray1.86X2-175[»]
3O7RX-ray1.90A2-175[»]
3O7SX-ray1.73A2-175[»]
3RAVX-ray1.90A2-175[»]
3RD0X-ray2.00A2-175[»]
3U90X-ray1.90A2-175[»]
3WVUX-ray1.92A2-175[»]
3WVVX-ray1.82A2-175[»]
3WVWX-ray2.00A2-175[»]
4DE6X-ray2.18A2-175[»]
4V1Welectron microscopy4.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X2-175[»]
4Z3BX-ray1.42A2-175[»]
5AXSX-ray1.67A2-175[»]
5CZUX-ray1.60A2-175[»]
5E1UX-ray1.56A2-175[»]
5E2DX-ray1.87A2-175[»]
5ERJX-ray1.45A2-175[»]
5ERKX-ray2.00A2-175[»]
5HQOX-ray1.81A2-175[»]
5IX6X-ray1.85A2-175[»]
ProteinModelPortaliP02791.
SMRiP02791.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02791.

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

Phylogenomic databases

HOGENOMiHOG000223383.
HOVERGENiHBG000410.
InParanoidiP02791.
KOiK13625.

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.

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

P02791-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSQIRQNYS TEVEAAVNRL VNLYLRASYT YLSLGFYFDR DDVALEGVCH
60 70 80 90 100
FFRELAEEKR EGAERLLKMQ NQRGGRALFQ DLQKPSQDEW GTTLDAMKAA
110 120 130 140 150
IVLEKSLNQA LLDLHALGSA QADPHLCDFL ESHFLDEEVK LIKKMGDHLT
160 170
NIQRLVGSQA GLGEYLFERL TLKHD
Length:175
Mass (Da):19,978
Last modified:January 23, 2007 - v4
Checksum:i2CA54242A04CB93F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti94L → P in BAA03396 (PubMed:16040348).Curated1
Sequence conflicti136 – 138DEE → NEQ no nucleotide entry (PubMed:8357841).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14523 mRNA. Translation: BAA03396.1.
AB175617 mRNA. Translation: BAD96182.1.
PIRiS36118. FRHOL.
RefSeqiNP_001108012.1. NM_001114540.1.
UniGeneiEca.13126.

Genome annotation databases

GeneIDi100051593.
KEGGiecb:100051593.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14523 mRNA. Translation: BAA03396.1.
AB175617 mRNA. Translation: BAD96182.1.
PIRiS36118. FRHOL.
RefSeqiNP_001108012.1. NM_001114540.1.
UniGeneiEca.13126.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AEWX-ray1.95A2-175[»]
1DATX-ray2.05A2-175[»]
1GWGX-ray2.01A2-175[»]
1HRSX-ray2.60A2-175[»]
1IERX-ray2.26A2-175[»]
1IESX-ray2.60A/B/C/D/E/F2-175[»]
1XZ1X-ray1.75A2-175[»]
1XZ3X-ray1.75A2-175[»]
2G4HX-ray2.00A2-175[»]
2GYDX-ray1.72A3-172[»]
2V2IX-ray2.00A2-175[»]
2V2JX-ray2.22A2-175[»]
2V2LX-ray1.90A2-175[»]
2V2MX-ray1.65A2-175[»]
2V2NX-ray1.55A2-175[»]
2V2OX-ray1.87A2-175[»]
2V2PX-ray1.15A2-175[»]
2V2RX-ray1.90A2-175[»]
2V2SX-ray1.37A2-175[»]
2W0OX-ray1.50A2-175[»]
2Z5PX-ray1.65A2-175[»]
2Z5QX-ray2.10A2-175[»]
2Z5RX-ray2.50A2-175[»]
2ZA6X-ray1.75A1-175[»]
2ZA7X-ray1.40A5-175[»]
2ZA8X-ray1.40A9-175[»]
2ZG7X-ray1.70X2-175[»]
2ZG8X-ray1.60X2-175[»]
2ZG9X-ray1.75X2-175[»]
2ZURX-ray1.80X2-175[»]
3AF7X-ray1.58X2-175[»]
3AF8X-ray1.66X2-175[»]
3AF9X-ray1.85X2-175[»]
3F32X-ray1.70A2-175[»]
3F33X-ray1.70A2-175[»]
3F34X-ray1.68A2-175[»]
3F35X-ray1.92A2-175[»]
3F36X-ray1.70A2-175[»]
3F37X-ray1.54A2-175[»]
3F38X-ray1.75A2-175[»]
3F39X-ray1.85A2-175[»]
3FI6X-ray1.80A2-175[»]
3H7GX-ray1.65A2-175[»]
3NOZX-ray1.52X2-175[»]
3NP0X-ray1.48X2-175[»]
3NP2X-ray1.86X2-175[»]
3O7RX-ray1.90A2-175[»]
3O7SX-ray1.73A2-175[»]
3RAVX-ray1.90A2-175[»]
3RD0X-ray2.00A2-175[»]
3U90X-ray1.90A2-175[»]
3WVUX-ray1.92A2-175[»]
3WVVX-ray1.82A2-175[»]
3WVWX-ray2.00A2-175[»]
4DE6X-ray2.18A2-175[»]
4V1Welectron microscopy4.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X2-175[»]
4Z3BX-ray1.42A2-175[»]
5AXSX-ray1.67A2-175[»]
5CZUX-ray1.60A2-175[»]
5E1UX-ray1.56A2-175[»]
5E2DX-ray1.87A2-175[»]
5ERJX-ray1.45A2-175[»]
5ERKX-ray2.00A2-175[»]
5HQOX-ray1.81A2-175[»]
5IX6X-ray1.85A2-175[»]
ProteinModelPortaliP02791.
SMRiP02791.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

ChEMBLiCHEMBL1293254.

Proteomic databases

PeptideAtlasiP02791.
PRIDEiP02791.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100051593.
KEGGiecb:100051593.

Organism-specific databases

CTDi2512.

Phylogenomic databases

HOGENOMiHOG000223383.
HOVERGENiHBG000410.
InParanoidiP02791.
KOiK13625.

Miscellaneous databases

EvolutionaryTraceiP02791.

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...

Entry informationi

Entry nameiFRIL_HORSE
AccessioniPrimary (citable) accession number: P02791
Secondary accession number(s): Q53VB4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 134 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

In horse spleen the light chain is the major chain.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.