ERFE_HUMAN
ID ERFE_HUMAN Reviewed; 354 AA.
AC Q4G0M1; W8S2M9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 102.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=24880340; DOI=10.1038/ng.2996;
RA Kautz L., Jung G., Valore E.V., Rivella S., Nemeth E., Ganz T.;
RT "Identification of erythroferrone as an erythroid regulator of iron
RT metabolism.";
RL Nat. Genet. 46:678-684(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 220-354.
RC TISSUE=Testis;
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).
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}.
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; KF984314; AHL84165.1; -; mRNA.
DR EMBL; AC016757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047423; AAH47423.1; -; mRNA.
DR CCDS; CCDS77548.1; -.
DR RefSeq; NP_001278761.1; NM_001291832.1.
DR AlphaFoldDB; Q4G0M1; -.
DR BioGRID; 127350; 45.
DR IntAct; Q4G0M1; 2.
DR STRING; 9606.ENSP00000442304; -.
DR GlyGen; Q4G0M1; 3 sites.
DR iPTMnet; Q4G0M1; -.
DR PhosphoSitePlus; Q4G0M1; -.
DR BioMuta; ERFE; -.
DR DMDM; 190359335; -.
DR MassIVE; Q4G0M1; -.
DR MaxQB; Q4G0M1; -.
DR PaxDb; Q4G0M1; -.
DR PeptideAtlas; Q4G0M1; -.
DR PRIDE; Q4G0M1; -.
DR ProteomicsDB; 62110; -.
DR Antibodypedia; 77392; 4 antibodies from 4 providers.
DR DNASU; 151176; -.
DR Ensembl; ENST00000546354.6; ENSP00000442304.1; ENSG00000178752.16.
DR GeneID; 151176; -.
DR KEGG; hsa:151176; -.
DR MANE-Select; ENST00000546354.6; ENSP00000442304.1; NM_001291832.2; NP_001278761.1.
DR UCSC; uc061udn.1; human.
DR CTD; 151176; -.
DR DisGeNET; 151176; -.
DR GeneCards; ERFE; -.
DR HGNC; HGNC:26727; ERFE.
DR HPA; ENSG00000178752; Tissue enhanced (skeletal muscle, testis, thyroid gland).
DR MIM; 615099; gene.
DR neXtProt; NX_Q4G0M1; -.
DR OpenTargets; ENSG00000178752; -.
DR VEuPathDB; HostDB:ENSG00000178752; -.
DR eggNOG; ENOG502RNS4; Eukaryota.
DR GeneTree; ENSGT00940000162100; -.
DR HOGENOM; CLU_057344_1_1_1; -.
DR InParanoid; Q4G0M1; -.
DR OMA; DPRDTWM; -.
DR OrthoDB; 1462460at2759; -.
DR PhylomeDB; Q4G0M1; -.
DR TreeFam; TF331282; -.
DR PathwayCommons; Q4G0M1; -.
DR SignaLink; Q4G0M1; -.
DR BioGRID-ORCS; 151176; 4 hits in 214 CRISPR screens.
DR ChiTaRS; ERFE; human.
DR GenomeRNAi; 151176; -.
DR Pharos; Q4G0M1; Tbio.
DR PRO; PR:Q4G0M1; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q4G0M1; protein.
DR Bgee; ENSG00000178752; Expressed in tibialis anterior and 111 other tissues.
DR ExpressionAtlas; Q4G0M1; baseline and differential.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005179; F:hormone activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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; IEA:Ensembl.
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; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hormone; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..354
FT /note="Erythroferrone"
FT /id="PRO_0000340250"
FT DOMAIN 199..354
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 26..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 220..229
FT /note="ALHELGVYYL -> SRGDHPCPSQ (in Ref. 3; AAH47423)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 37279 MW; F336BBFC1068FF52 CRC64;
MAPARRPAGA RLLLVYAGLL AAAAAGLGSP EPGAPSRSRA RREPPPGNEL PRGPGESRAG
PAARPPEPTA ERAHSVDPRD AWMLFVRQSD KGVNGKKRSR GKAKKLKFGL PGPPGPPGPQ
GPPGPIIPPE ALLKEFQLLL KGAVRQRERA EPEPCTCGPA GPVAASLAPV SATAGEDDDD
VVGDVLALLA APLAPGPRAP RVEAAFLCRL RRDALVERRA LHELGVYYLP DAEGAFRRGP
GLNLTSGQYR APVAGFYALA ATLHVALGEP PRRGPPRPRD HLRLLICIQS RCQRNASLEA
IMGLESSSEL FTISVNGVLY LQMGQWTSVF LDNASGCSLT VRSGSHFSAV LLGV
