FRIL_BOVIN
ID FRIL_BOVIN Reviewed; 175 AA.
AC O46415; Q3ZBZ3; Q53YP3;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Ferritin light chain;
DE Short=Ferritin L subunit;
GN Name=FTL;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RX PubMed=9467878; DOI=10.1016/s0305-0491(97)00277-0;
RA Orino K., Eguchi K., Nakayama T., Yamamoto S., Watanabe K.;
RT "Sequencing of cDNA clones that encode bovine ferritin H and L chains.";
RL Comp. Biochem. Physiol. 118B:667-673(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shin M.L., Cui X.S., Park S.Y., Kim E.Y., Park S.P., Lee W.J., Hwang K.C.,
RA Kim N.H.;
RT "Analysis of gene expression in the bovine blastocyst or hatched blastocyst
RT in vitro using ACP method.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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.
CC -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
CC -!- CAUTION: Lys-57 is present instead of the conserved Glu which is
CC expected to bind iron. {ECO:0000305}.
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DR EMBL; AB003094; BAA24819.1; -; mRNA.
DR EMBL; AY528246; AAS20594.1; -; mRNA.
DR EMBL; BC103021; AAI03022.1; -; mRNA.
DR RefSeq; NP_777217.1; NM_174792.3.
DR RefSeq; XP_003583967.2; XM_003583919.4.
DR RefSeq; XP_003587783.2; XM_003587735.4.
DR AlphaFoldDB; O46415; -.
DR SMR; O46415; -.
DR STRING; 9913.ENSBTAP00000009965; -.
DR PaxDb; O46415; -.
DR PeptideAtlas; O46415; -.
DR PRIDE; O46415; -.
DR Ensembl; ENSBTAT00000009965; ENSBTAP00000009965; ENSBTAG00000013343.
DR GeneID; 286861; -.
DR GeneID; 788801; -.
DR KEGG; bta:286861; -.
DR KEGG; bta:788801; -.
DR CTD; 2512; -.
DR VEuPathDB; HostDB:ENSBTAG00000013343; -.
DR eggNOG; KOG2332; Eukaryota.
DR GeneTree; ENSGT00940000153096; -.
DR HOGENOM; CLU_065681_4_0_1; -.
DR InParanoid; O46415; -.
DR OMA; SQDEWGT; -.
DR TreeFam; TF313885; -.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Reactome; R-BTA-917937; Iron uptake and transport.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000013343; Expressed in metanephros cortex and 105 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_0000201058"
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 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; 19988 MW; 47EFC85BB18DC978 CRC64;
MSSQIRQNYS TEVEAAVNRL VNMQLRASYT YLSLGFYFDR DDVALEGVGH FFRELAKEKR
EGAERLLKLQ NQRGGRALFL DVQKPSQDEW GKTQDAMEAA LLVEKNLNQA LLDLHGLASA
RGDPHICDFL ENHFLDEEVK LIKKMGDHLT NLRRLAGPQA GLGEYLFERL TLKHD
