UniProtKB - P02791 (FRIL_HORSE)
Ferritin light chain
FTL
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 similarityMiscellaneous
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 54 | IronPROSITE-ProRule annotation | 1 | |
Metal bindingi | 57 | IronPROSITE-ProRule annotation | 1 | |
Metal bindingi | 58 | IronPROSITE-ProRule annotation | 1 | |
Metal bindingi | 61 | IronPROSITE-ProRule annotation | 1 | |
Metal bindingi | 64 | IronPROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- ferric iron binding Source: GO_Central
- ferrous iron binding Source: GO_Central
- iron ion binding Source: UniProtKB
GO - Biological processi
- intracellular sequestering of iron ion Source: GO_Central
- iron ion transport Source: InterPro
Keywordsi
Biological process | Iron storage |
Ligand | Iron, Metal-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Ferritin light chainShort name: Ferritin L subunit |
Gene namesi | Name:FTL |
Organismi | Equus caballus (Horse) |
Taxonomic identifieri | 9796 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus › |
Proteomesi |
|
Subcellular locationi
Other locations
- cytoplasm Source: GO_Central
- intracellular ferritin complex Source: UniProtKB
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed2 Publications | |||
ChainiPRO_0000201059 | 2 – 175 | Ferritin light chainAdd BLAST | 174 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserine1 Publication | 1 |
Keywords - PTMi
AcetylationProteomic databases
PeptideAtlasi | P02791 |
PTM databases
iPTMneti | P02791 |
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.
Protein-protein interaction databases
STRINGi | 9796.ENSECAP00000045456 |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P02791 |
PCDDBi | P02791 |
SASBDBi | P02791 |
SMRi | P02791 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P02791 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 7 – 156 | Ferritin-like diironPROSITE-ProRule annotationAdd BLAST | 150 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 54 – 61 | Catalytic site for iron oxidation | 8 |
Sequence similaritiesi
Phylogenomic databases
GeneTreei | ENSGT00940000153096 |
InParanoidi | P02791 |
OrthoDBi | 1249457at2759 |
Family and domain databases
Gene3Di | 1.20.1260.10, 1 hit |
InterProi | View protein in InterPro IPR001519, Ferritin IPR012347, Ferritin-like IPR009040, Ferritin-like_diiron IPR009078, Ferritin-like_SF IPR014034, Ferritin_CS IPR008331, Ferritin_DPS_dom |
PANTHERi | PTHR11431, PTHR11431, 1 hit |
Pfami | View protein in Pfam PF00210, Ferritin, 1 hit |
SUPFAMi | SSF47240, SSF47240, 1 hit |
PROSITEi | View protein in PROSITE PS00540, FERRITIN_1, 1 hit PS00204, FERRITIN_2, 1 hit PS50905, FERRITIN_LIKE, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 94 | L → P in BAA03396 (PubMed:16040348).Curated | 1 | |
Sequence conflicti | 136 – 138 | DEE → NEQ no nucleotide entry (PubMed:8357841).Curated | 3 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D14523 mRNA Translation: BAA03396.1 AB175617 mRNA Translation: BAD96182.1 |
PIRi | S36118, FRHOL |
RefSeqi | NP_001108012.1, NM_001114540.1 |
Genome annotation databases
Ensembli | ENSECAT00000052660; ENSECAP00000045456; ENSECAG00000029371 |
GeneIDi | 100051593 |
KEGGi | ecb:100051593 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D14523 mRNA Translation: BAA03396.1 AB175617 mRNA Translation: BAD96182.1 |
PIRi | S36118, FRHOL |
RefSeqi | NP_001108012.1, NM_001114540.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1AEW | X-ray | 1.95 | A | 2-175 | [»] | |
1DAT | X-ray | 2.05 | A | 2-175 | [»] | |
1GWG | X-ray | 2.01 | A | 2-175 | [»] | |
1HRS | X-ray | 2.60 | A | 2-175 | [»] | |
1IER | X-ray | 2.26 | A | 2-175 | [»] | |
1IES | X-ray | 2.60 | A/B/C/D/E/F | 2-175 | [»] | |
1XZ1 | X-ray | 1.75 | A | 2-175 | [»] | |
1XZ3 | X-ray | 1.75 | A | 2-175 | [»] | |
2G4H | X-ray | 2.00 | A | 2-175 | [»] | |
2GYD | X-ray | 1.72 | A | 3-172 | [»] | |
2V2I | X-ray | 2.00 | A | 2-175 | [»] | |
2V2J | X-ray | 2.22 | A | 2-175 | [»] | |
2V2L | X-ray | 1.90 | A | 2-175 | [»] | |
2V2M | X-ray | 1.65 | A | 2-175 | [»] | |
2V2N | X-ray | 1.55 | A | 2-175 | [»] | |
2V2O | X-ray | 1.87 | A | 2-175 | [»] | |
2V2P | X-ray | 1.15 | A | 2-175 | [»] | |
2V2R | X-ray | 1.90 | A | 2-175 | [»] | |
2V2S | X-ray | 1.37 | A | 2-175 | [»] | |
2W0O | X-ray | 1.50 | A | 2-175 | [»] | |
2Z5P | X-ray | 1.65 | A | 2-175 | [»] | |
2Z5Q | X-ray | 2.10 | A | 2-175 | [»] | |
2Z5R | X-ray | 2.50 | A | 2-175 | [»] | |
2ZA6 | X-ray | 1.75 | A | 1-175 | [»] | |
2ZA7 | X-ray | 1.40 | A | 5-175 | [»] | |
2ZA8 | X-ray | 1.40 | A | 9-175 | [»] | |
2ZG7 | X-ray | 1.70 | X | 2-175 | [»] | |
2ZG8 | X-ray | 1.60 | X | 2-175 | [»] | |
2ZG9 | X-ray | 1.75 | X | 2-175 | [»] | |
2ZUR | X-ray | 1.80 | X | 2-175 | [»] | |
3AF7 | X-ray | 1.58 | X | 2-175 | [»] | |
3AF8 | X-ray | 1.66 | X | 2-175 | [»] | |
3AF9 | X-ray | 1.85 | X | 2-175 | [»] | |
3F32 | X-ray | 1.70 | A | 2-175 | [»] | |
3F33 | X-ray | 1.70 | A | 2-175 | [»] | |
3F34 | X-ray | 1.68 | A | 2-175 | [»] | |
3F35 | X-ray | 1.92 | A | 2-175 | [»] | |
3F36 | X-ray | 1.70 | A | 2-175 | [»] | |
3F37 | X-ray | 1.54 | A | 2-175 | [»] | |
3F38 | X-ray | 1.75 | A | 2-175 | [»] | |
3F39 | X-ray | 1.85 | A | 2-175 | [»] | |
3FI6 | X-ray | 1.80 | A | 2-175 | [»] | |
3H7G | X-ray | 1.65 | A | 2-175 | [»] | |
3NOZ | X-ray | 1.52 | X | 2-175 | [»] | |
3NP0 | X-ray | 1.48 | X | 2-175 | [»] | |
3NP2 | X-ray | 1.86 | X | 2-175 | [»] | |
3O7R | X-ray | 1.90 | A | 2-175 | [»] | |
3O7S | X-ray | 1.73 | A | 2-175 | [»] | |
3RAV | X-ray | 1.90 | A | 2-175 | [»] | |
3RD0 | X-ray | 2.00 | A | 2-175 | [»] | |
3U90 | X-ray | 1.90 | A | 2-175 | [»] | |
3WVU | X-ray | 1.92 | A | 2-175 | [»] | |
3WVV | X-ray | 1.82 | A | 2-175 | [»] | |
3WVW | X-ray | 2.00 | A | 2-175 | [»] | |
4DE6 | X-ray | 2.18 | A | 2-175 | [»] | |
4V1W | electron microscopy | 4.70 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X | 2-175 | [»] | |
4Z3B | X-ray | 1.42 | A | 2-175 | [»] | |
5AXS | X-ray | 1.67 | A | 2-175 | [»] | |
5CZU | X-ray | 1.60 | A | 2-175 | [»] | |
5E1U | X-ray | 1.56 | A | 2-175 | [»] | |
5E2D | X-ray | 1.87 | A | 2-175 | [»] | |
5ERJ | X-ray | 1.45 | A | 2-175 | [»] | |
5ERK | X-ray | 2.00 | A | 2-175 | [»] | |
5GU0 | X-ray | 1.95 | X | 2-175 | [»] | |
5GU1 | X-ray | 2.05 | X | 2-175 | [»] | |
5GU2 | X-ray | 2.12 | X | 2-175 | [»] | |
5GU3 | X-ray | 2.03 | X | 2-175 | [»] | |
5HQO | X-ray | 1.81 | A | 2-175 | [»] | |
5IX6 | X-ray | 1.85 | A | 2-175 | [»] | |
5LG2 | X-ray | 2.22 | A | 3-173 | [»] | |
5MIJ | X-ray | 1.49 | A | 2-175 | [»] | |
5MIK | X-ray | 1.96 | A | 2-175 | [»] | |
6ENV | X-ray | 1.82 | A | 2-175 | [»] | |
6ENW | X-ray | 2.60 | A | 2-175 | [»] | |
6FX8 | X-ray | 1.80 | A | 2-175 | [»] | |
6FX9 | X-ray | 1.50 | A | 2-175 | [»] | |
6GXJ | X-ray | 1.43 | A | 2-175 | [»] | |
6HJT | X-ray | 1.33 | A | 2-175 | [»] | |
6HJU | X-ray | 1.58 | A | 2-175 | [»] | |
6JEE | X-ray | 1.30 | A | 2-175 | [»] | |
6JEF | X-ray | 1.58 | A | 2-175 | [»] | |
6MSX | X-ray | 1.43 | A | 2-175 | [»] | |
6PXM | electron microscopy | 2.10 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/V/W/X/Y | 1-175 | [»] | |
6RA8 | X-ray | 2.00 | A | 2-174 | [»] | |
6RJH | electron microscopy | 2.00 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X | 3-173 | [»] | |
6TRZ | X-ray | 2.02 | AAA | 1-175 | [»] | |
6TSS | X-ray | 2.18 | AAA | 1-175 | [»] | |
6TSX | X-ray | 2.02 | AAA | 1-175 | [»] | |
7BD7 | X-ray | 1.50 | A | 2-173 | [»] | |
7BOM | X-ray | 1.93 | X | 2-175 | [»] | |
7BON | X-ray | 1.48 | A | 2-175 | [»] | |
AlphaFoldDBi | P02791 | |||||
PCDDBi | P02791 | |||||
SASBDBi | P02791 | |||||
SMRi | P02791 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 9796.ENSECAP00000045456 |
Chemistry databases
ChEMBLi | CHEMBL1293254 |
PTM databases
iPTMneti | P02791 |
Proteomic databases
PeptideAtlasi | P02791 |
Genome annotation databases
Ensembli | ENSECAT00000052660; ENSECAP00000045456; ENSECAG00000029371 |
GeneIDi | 100051593 |
KEGGi | ecb:100051593 |
Organism-specific databases
CTDi | 2512 |
Phylogenomic databases
GeneTreei | ENSGT00940000153096 |
InParanoidi | P02791 |
OrthoDBi | 1249457at2759 |
Miscellaneous databases
EvolutionaryTracei | P02791 |
Family and domain databases
Gene3Di | 1.20.1260.10, 1 hit |
InterProi | View protein in InterPro IPR001519, Ferritin IPR012347, Ferritin-like IPR009040, Ferritin-like_diiron IPR009078, Ferritin-like_SF IPR014034, Ferritin_CS IPR008331, Ferritin_DPS_dom |
PANTHERi | PTHR11431, PTHR11431, 1 hit |
Pfami | View protein in Pfam PF00210, Ferritin, 1 hit |
SUPFAMi | SSF47240, SSF47240, 1 hit |
PROSITEi | View protein in PROSITE PS00540, FERRITIN_1, 1 hit PS00204, FERRITIN_2, 1 hit PS50905, FERRITIN_LIKE, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | FRIL_HORSE | |
Accessioni | P02791Primary (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: | May 25, 2022 | |
This is version 163 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families