FRIL1_RAT
ID FRIL1_RAT Reviewed; 183 AA.
AC P02793; Q6P7T1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Ferritin light chain 1;
DE AltName: Full=Ferritin L subunit 1;
GN Name=Ftl1; Synonyms=Ftl;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=6546756; DOI=10.1016/s0021-9258(17)43049-3;
RA Leibold E.A., Aziz N., Brown A.J.P., Munro H.N.;
RT "Conservation in rat liver of light and heavy subunit sequences of
RT mammalian ferritin. Presence of unique octopeptide in the light subunit.";
RL J. Biol. Chem. 259:4327-4334(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=3584116; DOI=10.1016/s0021-9258(18)48241-5;
RA Leibold E.A., Munro H.N.;
RT "Characterization and evolution of the expressed rat ferritin light subunit
RT gene and its pseudogene family. Conservation of sequences within noncoding
RT regions of ferritin genes.";
RL J. Biol. Chem. 262:7335-7341(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1555892; DOI=10.1002/ijc.2910500619;
RA Denis M.G.;
RT "Isolation of cDNA clones corresponding to genes differentially expressed
RT in two colon-carcinoma cell lines differing by their tumorigenicity.";
RL Int. J. Cancer 50:930-936(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, and Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 106-137, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
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 -!- TISSUE SPECIFICITY: In rat liver, the light chain is the major chain.
CC -!- DOMAIN: The rat light chain has an octopeptide insertion after residue
CC 158 compared with other light chains.
CC -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR EMBL; K01930; AAA41154.1; -; mRNA.
DR EMBL; J02741; AAA41155.1; -; Genomic_DNA.
DR EMBL; L01122; AAA41152.1; -; mRNA.
DR EMBL; BC061525; AAH61525.1; -; mRNA.
DR EMBL; BC086583; AAH86583.1; -; mRNA.
DR EMBL; BC088756; AAH88756.1; -; mRNA.
DR PIR; A29575; FRRTL.
DR PIR; I54774; I54774.
DR RefSeq; NP_071945.3; NM_022500.4.
DR RefSeq; XP_002726683.1; XM_002726637.5.
DR RefSeq; XP_002729599.1; XM_002729553.5.
DR AlphaFoldDB; P02793; -.
DR SMR; P02793; -.
DR BioGRID; 247961; 1.
DR IntAct; P02793; 2.
DR STRING; 10116.ENSRNOP00000028315; -.
DR iPTMnet; P02793; -.
DR PhosphoSitePlus; P02793; -.
DR World-2DPAGE; 0004:P02793; -.
DR jPOST; P02793; -.
DR PaxDb; P02793; -.
DR PRIDE; P02793; -.
DR GeneID; 100360087; -.
DR GeneID; 29292; -.
DR KEGG; rno:100360087; -.
DR KEGG; rno:29292; -.
DR UCSC; RGD:61813; rat.
DR CTD; 14325; -.
DR RGD; 61813; Ftl1.
DR VEuPathDB; HostDB:ENSRNOG00000031506; -.
DR VEuPathDB; HostDB:ENSRNOG00000064385; -.
DR eggNOG; KOG2332; Eukaryota.
DR HOGENOM; CLU_065681_4_0_1; -.
DR InParanoid; P02793; -.
DR OMA; SQDEWGT; -.
DR OrthoDB; 1249457at2759; -.
DR PhylomeDB; P02793; -.
DR TreeFam; TF313885; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-917937; Iron uptake and transport.
DR PRO; PR:P02793; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000020843; Expressed in kidney and 19 other tissues.
DR Genevisible; P02793; RN.
DR GO; GO:0044754; C:autolysosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
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:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:RGD.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central.
DR GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR GO; GO:0010288; P:response to lead ion; IEP:RGD.
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 1: Evidence at protein level;
KW Direct protein sequencing; Iron; Iron storage; Metal-binding;
KW Reference proteome.
FT CHAIN 1..183
FT /note="Ferritin light chain 1"
FT /id="PRO_0000201066"
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 CONFLICT 98
FT /note="E -> K (in Ref. 1; AAA41154)"
FT /evidence="ECO:0000305"
FT CONFLICT 121..122
FT /note="RT -> QA (in Ref. 1; AAA41154)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="L -> F (in Ref. 3; AAA41152)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="V -> W (in Ref. 1; AAA41154)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="A -> Q (in Ref. 1; AAA41154 and 2; AAA41155)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 183 AA; 20749 MW; E6AB306251D55106 CRC64;
MTSQIRQNYS TEVEAAVNRL VNLHLRASYT YLSLGFFFDR DDVALEGVGH FFRELAEEKR
EGAERLLKLQ NERGGRALFQ DVQKPSQDEW GKTLEAMEAA LALEKNLNQA LLDLHALGSA
RTDPHLCDFL ESHFLDKEVK LIKKMGNHLT NLRRVAGPQP AQTGVAQASL GEYLFERLTL
KHD
