HEPC_HUMAN
ID HEPC_HUMAN Reviewed; 84 AA.
AC P81172; Q1HE14; Q9BY68;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Hepcidin {ECO:0000305};
DE AltName: Full=Liver-expressed antimicrobial peptide 1;
DE Short=LEAP-1;
DE AltName: Full=Putative liver tumor regressor;
DE Short=PLTR;
DE Contains:
DE RecName: Full=Hepcidin-25;
DE Short=Hepc25;
DE Contains:
DE RecName: Full=Hepcidin-20;
DE Short=Hepc20;
DE Flags: Precursor;
GN Name=HAMP {ECO:0000312|HGNC:HGNC:15598}; Synonyms=HEPC, LEAP1;
GN ORFNames=UNQ487/PRO1003;
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], AND PROTEIN SEQUENCE OF 60-84.
RC TISSUE=Liver, and Urine;
RX PubMed=11113131; DOI=10.1074/jbc.m008922200;
RA Park C.H., Valore E.V., Waring A.J., Ganz T.;
RT "Hepcidin: a urinary antimicrobial peptide synthesized in the liver.";
RL J. Biol. Chem. 276:7806-7810(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 60-84, TISSUE SPECIFICITY,
RP MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Blood, and Liver;
RX PubMed=11034317; DOI=10.1016/s0014-5793(00)01920-7;
RA Krause A., Neitz S., Maegert H.-J., Schulz A., Forssmann W.-G.,
RA Schulz-Knappe P., Adermann K.;
RT "LEAP-1, a novel highly disulfide-bonded human peptide exhibits
RT antimicrobial activity.";
RL FEBS Lett. 480:147-150(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Jung J.-W., Shin W.-S., Yoon Y., Lee S.-T.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [8]
RP SYNTHESIS OF 60-84.
RX PubMed=12010514; DOI=10.1034/j.1399-3011.2002.00980.x;
RA Kluever E., Schulz A., Forssmann W.-G., Adermann K.;
RT "Chemical synthesis of beta-defensins and LEAP-1/hepcidin.";
RL J. Pept. Res. 59:241-248(2002).
RN [9]
RP INDUCTION BY LPS, AND TISSUE SPECIFICITY.
RX PubMed=15124018; DOI=10.1172/jci200420945;
RA Nemeth E., Rivera S., Gabayan V., Keller C., Taudorf S., Pedersen B.K.,
RA Ganz T.;
RT "IL-6 mediates hypoferremia of inflammation by inducing the synthesis of
RT the iron regulatory hormone hepcidin.";
RL J. Clin. Invest. 113:1271-1276(2004).
RN [10]
RP REVIEW.
RX PubMed=22306005; DOI=10.1016/j.bbamcr.2012.01.014;
RA Ganz T., Nemeth E.;
RT "Hepcidin and iron homeostasis.";
RL Biochim. Biophys. Acta 1823:1434-1443(2012).
RN [11]
RP FUNCTION, AND INTERACTION WITH SLC40A1.
RX PubMed=22682227; DOI=10.1016/j.cmet.2012.03.018;
RA Qiao B., Sugianto P., Fung E., Del-Castillo-Rueda A., Moran-Jimenez M.J.,
RA Ganz T., Nemeth E.;
RT "Hepcidin-induced endocytosis of ferroportin is dependent on ferroportin
RT ubiquitination.";
RL Cell Metab. 15:918-924(2012).
RN [12]
RP FUNCTION, AND INTERACTION WITH SLC40A1.
RX PubMed=29237594; DOI=10.1182/blood-2017-05-786590;
RA Aschemeyer S., Qiao B., Stefanova D., Valore E.V., Sek A.C., Ruwe T.A.,
RA Vieth K.R., Jung G., Casu C., Rivella S., Jormakka M., Mackenzie B.,
RA Ganz T., Nemeth E.;
RT "Structure-function analysis of ferroportin defines the binding site and an
RT alternative mechanism of action of hepcidin.";
RL Blood 131:899-910(2018).
RN [13]
RP STRUCTURE BY NMR OF 60-84, AND PRELIMINARY DISULFIDE BONDS.
RX PubMed=12138110; DOI=10.1074/jbc.m205305200;
RA Hunter H.N., Fulton D.B., Ganz T., Vogel H.J.;
RT "The solution structure of human hepcidin, a peptide hormone with
RT antimicrobial activity that is involved in iron uptake and hereditary
RT hemochromatosis.";
RL J. Biol. Chem. 277:37597-37603(2002).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 60-84, AND DISULFIDE BONDS.
RX PubMed=19553669; DOI=10.1074/jbc.m109.017764;
RA Jordan J.B., Poppe L., Haniu M., Arvedson T., Syed R., Li V., Kohno H.,
RA Kim H., Schnier P.D., Harvey T.S., Miranda L.P., Cheetham J., Sasu B.J.;
RT "Hepcidin revisited, disulfide connectivity, dynamics, and structure.";
RL J. Biol. Chem. 284:24155-24167(2009).
RN [15] {ECO:0007744|PDB:6WBV}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.50 ANGSTROMS) OF 60-84, AND INTERACTION
RP WITH SLC40A1.
RX PubMed=32814342; DOI=10.1038/s41586-020-2668-z;
RA Billesbolle C.B., Azumaya C.M., Kretsch R.C., Powers A.S., Gonen S.,
RA Schneider S., Arvedson T., Dror R.O., Cheng Y., Manglik A.;
RT "Structure of hepcidin-bound ferroportin reveals iron homeostatic
RT mechanisms.";
RL Nature 586:807-811(2020).
RN [16]
RP VARIANT HFE2B ASP-71.
RX PubMed=14633868; DOI=10.1373/clinchem.2003.023440;
RA Biasiotto G., Belloli S., Ruggeri G., Zanella I., Gerardi G., Corrado M.,
RA Gobbi E., Albertini A., Arosio P.;
RT "Identification of new mutations of the HFE, hepcidin, and transferrin
RT receptor 2 genes by denaturing HPLC analysis of individuals with
RT biochemical indications of iron overload.";
RL Clin. Chem. 49:1981-1988(2003).
RN [17]
RP VARIANT HFE2B ASP-71.
RX PubMed=12915468; DOI=10.1093/hmg/ddg225;
RA Merryweather-Clarke A.T., Cadet E., Bomford A., Capron D., Viprakasit V.,
RA Miller A., McHugh P.J., Chapman R.W., Pointon J.J., Wimhurst V.L.,
RA Livesey K.J., Tanphaichitr V., Rochette J., Robson K.J.;
RT "Digenic inheritance of mutations in HAMP and HFE results in different
RT types of haemochromatosis.";
RL Hum. Mol. Genet. 12:2241-2247(2003).
RN [18]
RP VARIANT HFE2B ARG-70.
RX PubMed=14630809; DOI=10.1182/blood-2003-10-3390;
RA Roetto A., Daraio F., Porporato P., Caruso R., Cox T.M., Cazzola M.,
RA Gasparini P., Piperno A., Camaschella C.;
RT "Screening hepcidin for mutations in juvenile hemochromatosis:
RT identification of a new mutation (C70R).";
RL Blood 103:2407-2409(2004).
RN [19]
RP VARIANTS HFE2B GLY-59 AND ASP-71.
RX PubMed=14670915; DOI=10.1182/blood-2003-10-3366;
RA Jacolot S., Le Gac G., Scotet V., Quere I., Mura C., Ferec C.;
RT "HAMP as a modifier gene that increases the phenotypic expression of the
RT HFE pC282Y homozygous genotype.";
RL Blood 103:2835-2840(2004).
RN [20]
RP VARIANT HFE2B TYR-78.
RX PubMed=15099344; DOI=10.1111/j.0009-9163.2004.00254.x;
RA Delatycki M.B., Allen K.J., Gow P., MacFarlane J., Radomski C.,
RA Thompson J., Hayden M.R., Goldberg Y.P., Samuels M.E.;
RT "A homozygous HAMP mutation in a multiply consanguineous family with
RT pseudo-dominant juvenile hemochromatosis.";
RL Clin. Genet. 65:378-383(2004).
CC -!- FUNCTION: Liver-produced hormone that constitutes the main circulating
CC regulator of iron absorption and distribution across tissues. Acts by
CC promoting endocytosis and degradation of ferroportin/SLC40A1, leading
CC to the retention of iron in iron-exporting cells and decreased flow of
CC iron into plasma (PubMed:22682227, PubMed:29237594, PubMed:32814342).
CC Controls the major flows of iron into plasma: absorption of dietary
CC iron in the intestine, recycling of iron by macrophages, which
CC phagocytose old erythrocytes and other cells, and mobilization of
CC stored iron from hepatocytes (PubMed:22306005).
CC {ECO:0000269|PubMed:22306005, ECO:0000269|PubMed:22682227,
CC ECO:0000269|PubMed:29237594, ECO:0000269|PubMed:32814342}.
CC -!- FUNCTION: Has strong antimicrobial activity against E.coli ML35P
CC N.cinerea and weaker against S.epidermidis, S.aureus and group b
CC streptococcus bacteria. Active against the fungus C.albicans. No
CC activity against P.aeruginosa (PubMed:11113131, PubMed:11034317).
CC {ECO:0000269|PubMed:11034317, ECO:0000269|PubMed:11113131}.
CC -!- SUBUNIT: Interacts with SLC40A1; this interaction promotes SLC40A1
CC rapid ubiquitination. {ECO:0000269|PubMed:22682227,
CC ECO:0000269|PubMed:29237594, ECO:0000269|PubMed:32814342}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11034317}.
CC -!- TISSUE SPECIFICITY: Highest expression in liver and to a lesser extent
CC in heart and brain. Low levels in lung, tonsils, salivary gland,
CC trachea, prostate gland, adrenal gland and thyroid gland. Secreted into
CC the urine and blood (PubMed:11034317). Expressed by hepatocytes
CC (PubMed:15124018). {ECO:0000269|PubMed:11034317,
CC ECO:0000269|PubMed:15124018}.
CC -!- INDUCTION: Expression in hepatocytes is induced by LPS stimulus and the
CC induction is mediated by IL6 (PubMed:15124018). Expression is inhibited
CC in presence of TNF (PubMed:15124018). {ECO:0000269|PubMed:15124018}.
CC -!- MASS SPECTROMETRY: [Hepcidin-25]: Mass=2789.8; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11034317};
CC -!- DISEASE: Hemochromatosis 2B (HFE2B) [MIM:613313]: A juvenile form of
CC hemochromatosis, a disorder of iron metabolism with excess deposition
CC of iron in a variety of organs leading to their failure, bronze skin
CC pigmentation, hepatic cirrhosis, arthropathy and diabetes. The most
CC common symptoms of juvenile hemochromatosis at presentation are
CC hypogonadism and cardiomyopathy. {ECO:0000269|PubMed:12915468,
CC ECO:0000269|PubMed:14630809, ECO:0000269|PubMed:14633868,
CC ECO:0000269|PubMed:14670915, ECO:0000269|PubMed:15099344}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the hepcidin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Hepcidin entry;
CC URL="https://en.wikipedia.org/wiki/Hepcidin";
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DR EMBL; AF309489; AAG23966.1; -; mRNA.
DR EMBL; AJ277280; CAC09419.1; -; mRNA.
DR EMBL; AF131292; AAK14912.1; -; mRNA.
DR EMBL; AY358669; AAQ89032.1; -; mRNA.
DR EMBL; DQ496109; ABF47098.1; -; Genomic_DNA.
DR EMBL; AD000684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020612; AAH20612.1; -; mRNA.
DR CCDS; CCDS12454.1; -.
DR RefSeq; NP_066998.1; NM_021175.3.
DR PDB; 1M4E; NMR; -; A=65-84.
DR PDB; 1M4F; NMR; -; A=60-84.
DR PDB; 2KEF; NMR; -; A=60-84.
DR PDB; 3H0T; X-ray; 1.89 A; C=60-84.
DR PDB; 4QAE; X-ray; 2.10 A; P/Q/R/S/T/U=60-84.
DR PDB; 6WBV; EM; 2.50 A; B=60-84.
DR PDBsum; 1M4E; -.
DR PDBsum; 1M4F; -.
DR PDBsum; 2KEF; -.
DR PDBsum; 3H0T; -.
DR PDBsum; 4QAE; -.
DR PDBsum; 6WBV; -.
DR AlphaFoldDB; P81172; -.
DR SMR; P81172; -.
DR BioGRID; 121776; 3.
DR IntAct; P81172; 2.
DR STRING; 9606.ENSP00000471894; -.
DR ChEMBL; CHEMBL3989381; -.
DR DrugBank; DB13257; Ferrous sulfate anhydrous.
DR TCDB; 8.A.37.1.2; the hepcidin (hepcidin) family.
DR PhosphoSitePlus; P81172; -.
DR BioMuta; HAMP; -.
DR DMDM; 10720397; -.
DR jPOST; P81172; -.
DR MassIVE; P81172; -.
DR PaxDb; P81172; -.
DR PeptideAtlas; P81172; -.
DR PRIDE; P81172; -.
DR ProteomicsDB; 57692; -.
DR ABCD; P81172; 4 sequenced antibodies.
DR Antibodypedia; 29325; 388 antibodies from 30 providers.
DR DNASU; 57817; -.
DR Ensembl; ENST00000222304.5; ENSP00000222304.2; ENSG00000105697.9.
DR Ensembl; ENST00000598398.5; ENSP00000471894.1; ENSG00000105697.9.
DR GeneID; 57817; -.
DR KEGG; hsa:57817; -.
DR MANE-Select; ENST00000222304.5; ENSP00000222304.2; NM_021175.4; NP_066998.1.
DR UCSC; uc002nyw.4; human.
DR CTD; 57817; -.
DR DisGeNET; 57817; -.
DR GeneCards; HAMP; -.
DR GeneReviews; HAMP; -.
DR HGNC; HGNC:15598; HAMP.
DR HPA; ENSG00000105697; Tissue enriched (liver).
DR MalaCards; HAMP; -.
DR MIM; 606464; gene.
DR MIM; 613313; phenotype.
DR neXtProt; NX_P81172; -.
DR OpenTargets; ENSG00000105697; -.
DR Orphanet; 79230; Hemochromatosis type 2.
DR PharmGKB; PA29182; -.
DR VEuPathDB; HostDB:ENSG00000105697; -.
DR eggNOG; ENOG502T0FU; Eukaryota.
DR GeneTree; ENSGT00390000003154; -.
DR HOGENOM; CLU_2557737_0_0_1; -.
DR InParanoid; P81172; -.
DR OMA; PICLFCC; -.
DR OrthoDB; 1623838at2759; -.
DR PhylomeDB; P81172; -.
DR TreeFam; TF330932; -.
DR PathwayCommons; P81172; -.
DR SignaLink; P81172; -.
DR SIGNOR; P81172; -.
DR BioGRID-ORCS; 57817; 313 hits in 1077 CRISPR screens.
DR EvolutionaryTrace; P81172; -.
DR GeneWiki; HAMP; -.
DR GenomeRNAi; 57817; -.
DR Pharos; P81172; Tbio.
DR PRO; PR:P81172; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P81172; protein.
DR Bgee; ENSG00000105697; Expressed in right lobe of liver and 164 other tissues.
DR Genevisible; P81172; HS.
DR GO; GO:0045179; C:apical cortex; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005507; F:copper ion binding; IEA:Ensembl.
DR GO; GO:0005179; F:hormone activity; IDA:BHF-UCL.
DR GO; GO:0097690; F:iron ion transmembrane transporter inhibitor activity; IDA:BHF-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR GO; GO:0006953; P:acute-phase response; IEA:Ensembl.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IDA:BHF-UCL.
DR GO; GO:1903413; P:cellular response to bile acid; IEA:Ensembl.
DR GO; GO:0071354; P:cellular response to interleukin-6; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0071481; P:cellular response to X-ray; IEA:Ensembl.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; TAS:UniProtKB.
DR GO; GO:0034755; P:iron ion transmembrane transport; IEA:Ensembl.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR GO; GO:0042116; P:macrophage activation; IEA:Ensembl.
DR GO; GO:0060586; P:multicellular organismal iron ion homeostasis; IMP:BHF-UCL.
DR GO; GO:0002262; P:myeloid cell homeostasis; IEA:Ensembl.
DR GO; GO:0045779; P:negative regulation of bone resorption; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:1904479; P:negative regulation of intestinal absorption; IMP:BHF-UCL.
DR GO; GO:0032413; P:negative regulation of ion transmembrane transporter activity; IDA:BHF-UCL.
DR GO; GO:1904039; P:negative regulation of iron export across plasma membrane; IDA:BHF-UCL.
DR GO; GO:0034760; P:negative regulation of iron ion transmembrane transport; IBA:GO_Central.
DR GO; GO:1904255; P:negative regulation of iron ion transmembrane transporter activity; IDA:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; IEA:Ensembl.
DR GO; GO:0043032; P:positive regulation of macrophage activation; IEA:Ensembl.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:1902916; P:positive regulation of protein polyubiquitination; IDA:BHF-UCL.
DR GO; GO:2000646; P:positive regulation of receptor catabolic process; IDA:BHF-UCL.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR GO; GO:0036017; P:response to erythropoietin; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0010039; P:response to iron ion; IMP:BHF-UCL.
DR GO; GO:1990641; P:response to iron ion starvation; IEA:Ensembl.
DR GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
DR GO; GO:0010043; P:response to zinc ion; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR InterPro; IPR010500; Hepcidin.
DR PANTHER; PTHR16877; PTHR16877; 1.
DR Pfam; PF06446; Hepcidin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disease variant; Disulfide bond; Fungicide; Hormone; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..54
FT /id="PRO_0000013378"
FT PEPTIDE 60..84
FT /note="Hepcidin-25"
FT /id="PRO_0000013379"
FT PEPTIDE 65..84
FT /note="Hepcidin-20"
FT /id="PRO_0000013380"
FT DISULFID 66..82
FT /evidence="ECO:0000269|PubMed:19553669"
FT DISULFID 69..72
FT /evidence="ECO:0000269|PubMed:19553669"
FT DISULFID 70..78
FT /evidence="ECO:0000269|PubMed:19553669"
FT DISULFID 73..81
FT /evidence="ECO:0000269|PubMed:19553669"
FT VARIANT 59
FT /note="R -> G (in HFE2B; dbSNP:rs779021719)"
FT /evidence="ECO:0000269|PubMed:14670915"
FT /id="VAR_042512"
FT VARIANT 70
FT /note="C -> R (in HFE2B; dbSNP:rs1374259518)"
FT /evidence="ECO:0000269|PubMed:14630809"
FT /id="VAR_042513"
FT VARIANT 71
FT /note="G -> D (in HFE2B; dbSNP:rs104894696)"
FT /evidence="ECO:0000269|PubMed:12915468,
FT ECO:0000269|PubMed:14633868, ECO:0000269|PubMed:14670915"
FT /id="VAR_026648"
FT VARIANT 78
FT /note="C -> Y (in HFE2B; dbSNP:rs1462013476)"
FT /evidence="ECO:0000269|PubMed:15099344"
FT /id="VAR_042514"
FT CONFLICT 31
FT /note="T -> M (in Ref. 3; AAK14912)"
FT /evidence="ECO:0000305"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:3H0T"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:3H0T"
SQ SEQUENCE 84 AA; 9408 MW; 5F8DCA23D19D29F7 CRC64;
MALSSQIWAA CLLLLLLLAS LTSGSVFPQQ TGQLAELQPQ DRAGARASWM PMFQRRRRRD
THFPICIFCC GCCHRSKCGM CCKT
