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Protein

Erythroferrone

Gene

FAM132B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Iron-regulatory hormone that acts as an erythroid regulator after hemorrhage: produced by erythroblasts following blood loss and mediates suppression of hepcidin (HAMP) expression in the liver, thereby promoting increased iron absorption and mobilization from stores. Promotes lipid uptake into adipocytes and hepatocytes via transcriptional up-regulation of genes involved in fatty acid uptake (By similarity).By similarity

GO - Molecular functioni

  1. hormone activity Source: UniProtKB

GO - Biological processi

  1. cellular iron ion homeostasis Source: UniProtKB
  2. positive regulation of fatty acid transport Source: Ensembl
  3. regulation of fatty acid metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hormone

Names & Taxonomyi

Protein namesi
Recommended name:
Erythroferrone
Alternative name(s):
Complement C1q tumor necrosis factor-related protein 15
Myonectin
Gene namesi
Name:FAM132B
Synonyms:C1QTNF15, CTRP15, ERFE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:26727. FAM132B.

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
  2. extracellular space Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence AnalysisAdd
BLAST
Chaini29 – 354326ErythroferronePRO_0000340250Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi243 – 2431N-linked (GlcNAc...)Sequence Analysis
Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ4G0M1.
PaxDbiQ4G0M1.
PRIDEiQ4G0M1.

Expressioni

Gene expression databases

BgeeiQ4G0M1.
CleanExiHS_FAM132B.
GenevestigatoriQ4G0M1.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. May form heteromeric complexes with C1QTNF2 and FAM132A and, to a lesser extent, with C1QTNF5 and C1QTNF10 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ4G0M1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini199 – 354156C1qPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi111 – 12919Pro-richAdd
BLAST
Compositional biasi177 – 1804Poly-Asp

Sequence similaritiesi

Belongs to the adipolin/erythroferrone family.Curated
Contains 1 C1q domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG42889.
GeneTreeiENSGT00390000007846.
HOGENOMiHOG000112436.
HOVERGENiHBG107865.
InParanoidiQ4G0M1.
OMAiGSHFSAI.
OrthoDBiEOG7XSTFH.
PhylomeDBiQ4G0M1.
TreeFamiTF331282.

Family and domain databases

InterProiIPR001073. C1q.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiPS50871. C1Q. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q4G0M1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPARRPAGA RLLLVYAGLL AAAAAGLGSP EPGAPSRSRA RREPPPGNEL
60 70 80 90 100
PRGPGESRAG PAARPPEPTA ERAHSVDPRD AWMLFVRQSD KGVNGKKRSR
110 120 130 140 150
GKAKKLKFGL PGPPGPPGPQ GPPGPIIPPE ALLKEFQLLL KGAVRQRERA
160 170 180 190 200
EPEPCTCGPA GPVAASLAPV SATAGEDDDD VVGDVLALLA APLAPGPRAP
210 220 230 240 250
RVEAAFLCRL RRDALVERRA LHELGVYYLP DAEGAFRRGP GLNLTSGQYR
260 270 280 290 300
APVAGFYALA ATLHVALGEP PRRGPPRPRD HLRLLICIQS RCQRNASLEA
310 320 330 340 350
IMGLESSSEL FTISVNGVLY LQMGQWTSVF LDNASGCSLT VRSGSHFSAV

LLGV
Length:354
Mass (Da):37,279
Last modified:June 10, 2008 - v2
Checksum:iF336BBFC1068FF52
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti220 – 22910ALHELGVYYL → SRGDHPCPSQ in AAH47423 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KF984314 mRNA. Translation: AHL84165.1.
AC016757 Genomic DNA. No translation available.
BC047423 mRNA. Translation: AAH47423.1.
RefSeqiNP_001278761.1. NM_001291832.1.
UniGeneiHs.24951.
Hs.742300.

Genome annotation databases

EnsembliENST00000546354; ENSP00000442304; ENSG00000178752.
GeneIDi151176.
KEGGihsa:151176.

Polymorphism databases

DMDMi190359335.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KF984314 mRNA. Translation: AHL84165.1.
AC016757 Genomic DNA. No translation available.
BC047423 mRNA. Translation: AAH47423.1.
RefSeqiNP_001278761.1. NM_001291832.1.
UniGeneiHs.24951.
Hs.742300.

3D structure databases

ProteinModelPortaliQ4G0M1.
ModBaseiSearch...
MobiDBiSearch...

Polymorphism databases

DMDMi190359335.

Proteomic databases

MaxQBiQ4G0M1.
PaxDbiQ4G0M1.
PRIDEiQ4G0M1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000546354; ENSP00000442304; ENSG00000178752.
GeneIDi151176.
KEGGihsa:151176.

Organism-specific databases

CTDi151176.
GeneCardsiGC02P239067.
HGNCiHGNC:26727. FAM132B.
MIMi615099. gene.
neXtProtiNX_Q4G0M1.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG42889.
GeneTreeiENSGT00390000007846.
HOGENOMiHOG000112436.
HOVERGENiHBG107865.
InParanoidiQ4G0M1.
OMAiGSHFSAI.
OrthoDBiEOG7XSTFH.
PhylomeDBiQ4G0M1.
TreeFamiTF331282.

Miscellaneous databases

PROiQ4G0M1.
SOURCEiSearch...

Gene expression databases

BgeeiQ4G0M1.
CleanExiHS_FAM132B.
GenevestigatoriQ4G0M1.

Family and domain databases

InterProiIPR001073. C1q.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiPS50871. C1Q. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of erythroferrone as an erythroid regulator of iron metabolism."
    Kautz L., Jung G., Valore E.V., Rivella S., Nemeth E., Ganz T.
    Nat. Genet. 46:678-684(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 220-354.
    Tissue: Testis.

Entry informationi

Entry nameiERFE_HUMAN
AccessioniPrimary (citable) accession number: Q4G0M1
Secondary accession number(s): W8S2M9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: March 4, 2015
This is version 58 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.