FRIL_CANLF
ID FRIL_CANLF Reviewed; 175 AA.
AC Q53VB8;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Ferritin light chain;
DE Short=Ferritin L subunit;
GN Name=FTL;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney, Liver, and Spleen;
RX PubMed=16040348; DOI=10.1080/10425170400024359;
RA Orino K., Miura T., Muto S., Watanabe K.;
RT "Sequence analysis of canine and equine ferritin H and L subunit cDNAs.";
RL DNA Seq. 16:58-64(2005).
CC -!- FUNCTION: Stores iron in a soluble, non-toxic, readily available form.
CC Important for iron homeostasis. Iron is taken up in the ferrous form
CC and deposited as ferric hydroxides after oxidation. Also plays a role
CC in delivery of iron to cells. Mediates iron uptake in capsule cells of
CC the developing kidney (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Oligomer of 24 subunits. There are two types of subunits: L
CC (light) chain and H (heavy) chain. The major chain can be light or
CC heavy, depending on the species and tissue type. The functional
CC molecule forms a roughly spherical shell with a diameter of 12 nm and
CC contains a central cavity into which the insoluble mineral iron core is
CC deposited (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR EMBL; AB175612; BAD96177.1; -; mRNA.
DR EMBL; AB175613; BAD96178.1; -; mRNA.
DR EMBL; AB175614; BAD96179.1; -; mRNA.
DR RefSeq; NP_001019807.1; NM_001024636.2.
DR RefSeq; XP_005634393.1; XM_005634336.2.
DR AlphaFoldDB; Q53VB8; -.
DR SMR; Q53VB8; -.
DR STRING; 9612.ENSCAFP00000005761; -.
DR PaxDb; Q53VB8; -.
DR Ensembl; ENSCAFT00030026497; ENSCAFP00030023130; ENSCAFG00030014341.
DR Ensembl; ENSCAFT00845000775; ENSCAFP00845000573; ENSCAFG00845000481.
DR GeneID; 102155200; -.
DR GeneID; 477042; -.
DR KEGG; cfa:477042; -.
DR CTD; 2512; -.
DR VEuPathDB; HostDB:ENSCAFG00845000481; -.
DR eggNOG; KOG2332; Eukaryota.
DR GeneTree; ENSGT00940000153096; -.
DR HOGENOM; CLU_065681_4_0_1; -.
DR InParanoid; Q53VB8; -.
DR OMA; SQDEWGT; -.
DR OrthoDB; 1249457at2759; -.
DR TreeFam; TF313885; -.
DR Reactome; R-CFA-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-CFA-6798695; Neutrophil degranulation.
DR Reactome; R-CFA-917937; Iron uptake and transport.
DR Proteomes; UP000002254; Chromosome 1.
DR Bgee; ENSCAFG00000003861; Expressed in cartilage tissue and 47 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008043; C:intracellular ferritin complex; ISS:UniProtKB.
DR GO; GO:0008199; F:ferric iron binding; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central.
DR GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR Gene3D; 1.20.1260.10; -; 1.
DR InterPro; IPR001519; Ferritin.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009040; Ferritin-like_diiron.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR014034; Ferritin_CS.
DR InterPro; IPR008331; Ferritin_DPS_dom.
DR PANTHER; PTHR11431; PTHR11431; 1.
DR Pfam; PF00210; Ferritin; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00540; FERRITIN_1; 1.
DR PROSITE; PS00204; FERRITIN_2; 1.
DR PROSITE; PS50905; FERRITIN_LIKE; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Iron; Iron storage; Metal-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02791"
FT CHAIN 2..175
FT /note="Ferritin light chain"
FT /id="PRO_0000252365"
FT DOMAIN 7..156
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 54
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 57
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 61
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 64
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P02791"
SQ SEQUENCE 175 AA; 20095 MW; 384590C616CC52CE CRC64;
MSSQIRQNYS TEVEAAVNRL VNMHLRASYT YLSLGFYFDR DDVALEGVGH FFRELAEEKR
EGAERFLKMQ NQRGGRALFQ DVQKPSQDEW GKTLDAMEAA LLLEKSLNQA LLDLHALGSA
RADPHLCDFL ENHFLDEEVK LIKKMGDHLT NLRRLATPQA GLGEYLFERL TLKHD
