ERFE_RAT
ID ERFE_RAT Reviewed; 341 AA.
AC D4AB34;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Erythroferrone;
DE AltName: Full=Complement C1q tumor necrosis factor-related protein 15;
DE AltName: Full=Myonectin;
DE Flags: Precursor;
GN Name=Erfe; Synonyms=C1qtnf15, Ctrp15, Fam132b;
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 [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=22351773; DOI=10.1074/jbc.m111.336834;
RA Seldin M.M., Peterson J.M., Byerly M.S., Wei Z., Wong G.W.;
RT "Myonectin (CTRP15), a novel myokine that links skeletal muscle to systemic
RT lipid homeostasis.";
RL J. Biol. Chem. 287:11968-11980(2012).
CC -!- FUNCTION: Iron-regulatory hormone that acts as an erythroid regulator
CC after hemorrhage: produced by erythroblasts following blood loss and
CC mediates suppression of hepcidin (HAMP) expression in the liver,
CC thereby promoting increased iron absorption and mobilization from
CC stores. Promotes lipid uptake into adipocytes and hepatocytes via
CC transcriptional up-regulation of genes involved in fatty acid uptake.
CC {ECO:0000250|UniProtKB:Q6PGN1, ECO:0000269|PubMed:22351773}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. May form heteromeric complexes
CC with C1QTNF2 and C1QTNF12 and, to a lesser extent, with C1QTNF5 and
CC C1QTNF10. {ECO:0000250|UniProtKB:Q6PGN1}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q6PGN1}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6PGN1}.
CC -!- SIMILARITY: Belongs to the adipolin/erythroferrone family.
CC {ECO:0000305}.
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DR EMBL; CH473997; EDL92028.1; -; Genomic_DNA.
DR RefSeq; XP_001060107.2; XM_001060107.5.
DR RefSeq; XP_003754598.1; XM_003754550.4.
DR AlphaFoldDB; D4AB34; -.
DR STRING; 10116.ENSRNOP00000045074; -.
DR GlyGen; D4AB34; 4 sites.
DR PaxDb; D4AB34; -.
DR PRIDE; D4AB34; -.
DR Ensembl; ENSRNOT00000051810; ENSRNOP00000045074; ENSRNOG00000024688.
DR GeneID; 681056; -.
DR UCSC; RGD:1584688; rat.
DR CTD; 151176; -.
DR RGD; 1584688; Erfe.
DR eggNOG; ENOG502RNS4; Eukaryota.
DR GeneTree; ENSGT00940000162100; -.
DR HOGENOM; CLU_057344_1_1_1; -.
DR InParanoid; D4AB34; -.
DR OMA; DPRDTWM; -.
DR OrthoDB; 1462460at2759; -.
DR PhylomeDB; D4AB34; -.
DR TreeFam; TF331282; -.
DR PRO; PR:D4AB34; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Proteomes; UP000234681; Chromosome 9.
DR Bgee; ENSRNOG00000024688; Expressed in skeletal muscle tissue and 7 other tissues.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005179; F:hormone activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0015908; P:fatty acid transport; IEA:Ensembl.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IBA:GO_Central.
DR GO; GO:2000193; P:positive regulation of fatty acid transport; ISO:RGD.
DR GO; GO:0046326; P:positive regulation of glucose import; IBA:GO_Central.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0019217; P:regulation of fatty acid metabolic process; ISO:RGD.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50871; C1Q; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Hormone; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..341
FT /note="Erythroferrone"
FT /id="PRO_0000422122"
FT DOMAIN 186..341
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 30..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..115
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 341 AA; 36369 MW; 9467635C8DEFDBBD CRC64;
MASTRSPGGA RTLLACASLL AAMGLGVPES AEPVGTQARP QPPGTELPAP PAHSPPEPTI
AHAHSVDPRD AWMLFVKQSD KGINSKKRSR TKARRLKLGL PGPPGPPGPQ GPPGPFIPSE
VLLKEFQLLL KGAVRQREST EHCTRDLTTP ASGGPSRDPV TQELESQDQG AVLALLAATL
AQSPRAPRVE AAFHCRLRRD VQVERRALHE LGVYYLPEVE GAFRRGPGLN LTSGQYTAPV
AGFYALAATL HVALTKQPRK GPPQPRDRLR LLICIQSLCQ HNASLETVMG LENSSELFTI
SVNGVLYLQT GHYTSVFLDN ASGSSLTVRG GSHFSAILLG L
