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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi54 – 541IronPROSITE-ProRule annotation
Metal bindingi57 – 571IronPROSITE-ProRule annotation
Metal bindingi58 – 581IronPROSITE-ProRule annotation
Metal bindingi61 – 611IronPROSITE-ProRule annotation
Metal bindingi64 – 641IronPROSITE-ProRule annotation

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

ChEMBLiCHEMBL1293254.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 175174Ferritin light chainPRO_0000201059Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication

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

1
175
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 53Combined sources
Helixi11 – 3828Combined sources
Turni41 – 433Combined sources
Helixi46 – 7328Combined sources
Helixi93 – 12028Combined sources
Helixi124 – 13310Combined sources
Helixi135 – 15824Combined sources
Helixi160 – 17011Combined sources
Turni171 – 1744Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP02791.
SMRiP02791. Positions 2-175.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02791.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 156150Ferritin-like diironPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 618Catalytic site for iron oxidation

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941L → P in BAA03396 (PubMed:16040348).Curated
Sequence conflicti136 – 1383DEE → NEQ no nucleotide entry (PubMed:8357841).Curated

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
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[»]
ProteinModelPortaliP02791.
SMRiP02791. Positions 2-175.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

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: July 6, 2016
This is version 132 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.