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Hepcidin (Liver-expressed antimicrobial peptide 1) (LEAP-1) (Putative liver tumor regressor) (PLTR) [Cleaved into: Hepcidin-25 (Hepc25); Hepcidin-20 (Hepc20)]

 HEPC_HUMAN              Reviewed;          84 AA.
P81172; Q1HE14; Q9BY68;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
12-SEP-2018, entry version 168.
RecName: Full=Hepcidin;
AltName: Full=Liver-expressed antimicrobial peptide 1;
Short=LEAP-1;
AltName: Full=Putative liver tumor regressor;
Short=PLTR;
Contains:
RecName: Full=Hepcidin-25;
Short=Hepc25;
Contains:
RecName: Full=Hepcidin-20;
Short=Hepc20;
Flags: Precursor;
Name=HAMP; Synonyms=HEPC, LEAP1; ORFNames=UNQ487/PRO1003;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 60-84.
TISSUE=Liver, and Urine;
PubMed=11113131; DOI=10.1074/jbc.M008922200;
Park C.H., Valore E.V., Waring A.J., Ganz T.;
"Hepcidin: a urinary antimicrobial peptide synthesized in the liver.";
J. Biol. Chem. 276:7806-7810(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 60-84, TISSUE
SPECIFICITY, AND MASS SPECTROMETRY.
TISSUE=Blood, and Liver;
PubMed=11034317; DOI=10.1016/S0014-5793(00)01920-7;
Krause A., Neitz S., Maegert H.-J., Schulz A., Forssmann W.-G.,
Schulz-Knappe P., Adermann K.;
"LEAP-1, a novel highly disulfide-bonded human peptide exhibits
antimicrobial activity.";
FEBS Lett. 480:147-150(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Jung J.-W., Shin W.-S., Yoon Y., Lee S.-T.;
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
SYNTHESIS OF 60-84.
PubMed=12010514; DOI=10.1034/j.1399-3011.2002.00980.x;
Kluever E., Schulz A., Forssmann W.-G., Adermann K.;
"Chemical synthesis of beta-defensins and LEAP-1/hepcidin.";
J. Pept. Res. 59:241-248(2002).
[9]
REVIEW.
PubMed=22306005; DOI=10.1016/j.bbamcr.2012.01.014;
Ganz T., Nemeth E.;
"Hepcidin and iron homeostasis.";
Biochim. Biophys. Acta 1823:1434-1443(2012).
[10]
STRUCTURE BY NMR OF 60-84, AND PRELIMINARY DISULFIDE BONDS.
PubMed=12138110; DOI=10.1074/jbc.M205305200;
Hunter H.N., Fulton D.B., Ganz T., Vogel H.J.;
"The solution structure of human hepcidin, a peptide hormone with
antimicrobial activity that is involved in iron uptake and hereditary
hemochromatosis.";
J. Biol. Chem. 277:37597-37603(2002).
[11]
X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 60-84, AND DISULFIDE BONDS.
PubMed=19553669; DOI=10.1074/jbc.M109.017764;
Jordan J.B., Poppe L., Haniu M., Arvedson T., Syed R., Li V.,
Kohno H., Kim H., Schnier P.D., Harvey T.S., Miranda L.P.,
Cheetham J., Sasu B.J.;
"Hepcidin revisited, disulfide connectivity, dynamics, and
structure.";
J. Biol. Chem. 284:24155-24167(2009).
[12]
VARIANT HFE2B ASP-71.
PubMed=14633868; DOI=10.1373/clinchem.2003.023440;
Biasiotto G., Belloli S., Ruggeri G., Zanella I., Gerardi G.,
Corrado M., Gobbi E., Albertini A., Arosio P.;
"Identification of new mutations of the HFE, hepcidin, and transferrin
receptor 2 genes by denaturing HPLC analysis of individuals with
biochemical indications of iron overload.";
Clin. Chem. 49:1981-1988(2003).
[13]
VARIANT HFE2B ASP-71.
PubMed=12915468; DOI=10.1093/hmg/ddg225;
Merryweather-Clarke A.T., Cadet E., Bomford A., Capron D.,
Viprakasit V., Miller A., McHugh P.J., Chapman R.W., Pointon J.J.,
Wimhurst V.L., Livesey K.J., Tanphaichitr V., Rochette J.,
Robson K.J.;
"Digenic inheritance of mutations in HAMP and HFE results in different
types of haemochromatosis.";
Hum. Mol. Genet. 12:2241-2247(2003).
[14]
VARIANT HFE2B ARG-70.
PubMed=14630809; DOI=10.1182/blood-2003-10-3390;
Roetto A., Daraio F., Porporato P., Caruso R., Cox T.M., Cazzola M.,
Gasparini P., Piperno A., Camaschella C.;
"Screening hepcidin for mutations in juvenile hemochromatosis:
identification of a new mutation (C70R).";
Blood 103:2407-2409(2004).
[15]
VARIANTS HFE2B GLY-59 AND ASP-71.
PubMed=14670915; DOI=10.1182/blood-2003-10-3366;
Jacolot S., Le Gac G., Scotet V., Quere I., Mura C., Ferec C.;
"HAMP as a modifier gene that increases the phenotypic expression of
the HFE pC282Y homozygous genotype.";
Blood 103:2835-2840(2004).
[16]
VARIANT HFE2B TYR-78.
PubMed=15099344; DOI=10.1111/j.0009-9163.2004.00254.x;
Delatycki M.B., Allen K.J., Gow P., MacFarlane J., Radomski C.,
Thompson J., Hayden M.R., Goldberg Y.P., Samuels M.E.;
"A homozygous HAMP mutation in a multiply consanguineous family with
pseudo-dominant juvenile hemochromatosis.";
Clin. Genet. 65:378-383(2004).
-!- FUNCTION: Liver-produced hormone that constitutes the main
circulating regulator of iron absorption and distribution across
tissues. Acts by promoting endocytosis and degradation of
ferroportin, leading to the retention of iron in iron-exporting
cells and decreased flow of iron into plasma. Controls the major
flows of iron into plasma: absorption of dietary iron in the
intestine, recycling of iron by macrophages, which phagocytose old
erythrocytes and other cells, and mobilization of stored iron from
hepatocytes (PubMed:22306005). {ECO:0000269|PubMed:22306005}.
-!- FUNCTION: Has strong antimicrobial activity against E.coli ML35P
N.cinerea and weaker against S.epidermidis, S.aureus and group b
streptococcus bacteria. Active against the fungus C.albicans. No
activity against P.aeruginosa (PubMed:11113131, PubMed:11034317).
{ECO:0000269|PubMed:11034317, ECO:0000269|PubMed:11113131}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Highest expression in liver and to a lesser
extent in heart and brain. Low levels in lung, tonsils, salivary
gland, trachea, prostate gland, adrenal gland and thyroid gland.
Secreted into the urine. {ECO:0000269|PubMed:11034317}.
-!- MASS SPECTROMETRY: Mass=2789.8; Method=MALDI; Range=60-84;
Evidence={ECO:0000269|PubMed:11034317};
-!- DISEASE: Hemochromatosis 2B (HFE2B) [MIM:613313]: A juvenile form
of hemochromatosis, a disorder of iron metabolism with excess
deposition of iron in a variety of organs leading to their
failure, bronze skin pigmentation, hepatic cirrhosis, arthropathy
and diabetes. The most common symptoms of juvenile hemochromatosis
at presentation are hypogonadism and cardiomyopathy.
{ECO:0000269|PubMed:12915468, ECO:0000269|PubMed:14630809,
ECO:0000269|PubMed:14633868, ECO:0000269|PubMed:14670915,
ECO:0000269|PubMed:15099344}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the hepcidin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Hepcidin entry;
URL="https://en.wikipedia.org/wiki/Hepcidin";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF309489; AAG23966.1; -; mRNA.
EMBL; AJ277280; CAC09419.1; -; mRNA.
EMBL; AF131292; AAK14912.1; -; mRNA.
EMBL; AY358669; AAQ89032.1; -; mRNA.
EMBL; DQ496109; ABF47098.1; -; Genomic_DNA.
EMBL; AD000684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC020612; AAH20612.1; -; mRNA.
CCDS; CCDS12454.1; -.
RefSeq; NP_066998.1; NM_021175.3.
UniGene; Hs.8821; -.
PDB; 1M4E; NMR; -; A=65-84.
PDB; 1M4F; NMR; -; A=60-84.
PDB; 2KEF; NMR; -; A=60-84.
PDB; 3H0T; X-ray; 1.89 A; C=60-84.
PDB; 4QAE; X-ray; 2.10 A; P/Q/R/S/T/U=60-84.
PDBsum; 1M4E; -.
PDBsum; 1M4F; -.
PDBsum; 2KEF; -.
PDBsum; 3H0T; -.
PDBsum; 4QAE; -.
ProteinModelPortal; P81172; -.
SMR; P81172; -.
BioGrid; 121776; 2.
IntAct; P81172; 2.
STRING; 9606.ENSP00000222304; -.
ChEMBL; CHEMBL3989381; -.
TCDB; 8.A.37.1.2; the hepcidin (hepcidin) family.
BioMuta; HAMP; -.
DMDM; 10720397; -.
PaxDb; P81172; -.
PeptideAtlas; P81172; -.
PRIDE; P81172; -.
ProteomicsDB; 57692; -.
Ensembl; ENST00000222304; ENSP00000222304; ENSG00000105697.
Ensembl; ENST00000598398; ENSP00000471894; ENSG00000105697.
GeneID; 57817; -.
KEGG; hsa:57817; -.
UCSC; uc002nyw.4; human.
CTD; 57817; -.
DisGeNET; 57817; -.
EuPathDB; HostDB:ENSG00000105697.7; -.
GeneCards; HAMP; -.
GeneReviews; HAMP; -.
HGNC; HGNC:15598; HAMP.
MalaCards; HAMP; -.
MIM; 606464; gene.
MIM; 613313; phenotype.
neXtProt; NX_P81172; -.
OpenTargets; ENSG00000105697; -.
Orphanet; 79230; Hemochromatosis type 2.
PharmGKB; PA29182; -.
eggNOG; ENOG410J3JD; Eukaryota.
eggNOG; ENOG4111C2J; LUCA.
GeneTree; ENSGT00390000003154; -.
HOGENOM; HOG000008666; -.
HOVERGEN; HBG003716; -.
InParanoid; P81172; -.
OMA; CGICCKT; -.
OrthoDB; EOG091G1A4A; -.
PhylomeDB; P81172; -.
TreeFam; TF330932; -.
SIGNOR; P81172; -.
EvolutionaryTrace; P81172; -.
GeneWiki; HAMP; -.
GenomeRNAi; 57817; -.
PRO; PR:P81172; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105697; Expressed in 200 organ(s), highest expression level in liver.
CleanEx; HS_HAMP; -.
Genevisible; P81172; HS.
GO; GO:0045179; C:apical cortex; IEA:Ensembl.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
GO; GO:0005179; F:hormone activity; IDA:BHF-UCL.
GO; GO:0097690; F:iron channel inhibitor activity; IDA:BHF-UCL.
GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
GO; GO:0006953; P:acute-phase response; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
GO; GO:0006879; P:cellular iron ion homeostasis; IDA:BHF-UCL.
GO; GO:1903413; P:cellular response to bile acid; IEA:Ensembl.
GO; GO:0071354; P:cellular response to interleukin-6; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0071481; P:cellular response to X-ray; IEA:Ensembl.
GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
GO; GO:0006955; P:immune response; TAS:UniProtKB.
GO; GO:0031640; P:killing of cells of other organism; IDA:UniProtKB.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0060586; P:multicellular organismal iron ion homeostasis; IMP:BHF-UCL.
GO; GO:1904039; P:negative regulation of ferrous iron export; IDA:BHF-UCL.
GO; GO:1904479; P:negative regulation of intestinal absorption; IMP:BHF-UCL.
GO; GO:0032413; P:negative regulation of ion transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:1904255; P:negative regulation of iron channel activity; IDA:BHF-UCL.
GO; GO:0034760; P:negative regulation of iron ion transmembrane transport; IBA:GO_Central.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; IEA:Ensembl.
GO; GO:1902916; P:positive regulation of protein polyubiquitination; IDA:BHF-UCL.
GO; GO:2000646; P:positive regulation of receptor catabolic process; IDA:BHF-UCL.
GO; GO:0002092; P:positive regulation of receptor internalization; IDA:BHF-UCL.
GO; GO:0036017; P:response to erythropoietin; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0010039; P:response to iron ion; IMP:BHF-UCL.
GO; GO:1990641; P:response to iron ion starvation; IEA:Ensembl.
GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
GO; GO:0010043; P:response to zinc ion; IEA:Ensembl.
InterPro; IPR010500; Hepcidin.
PANTHER; PTHR16877; PTHR16877; 1.
Pfam; PF06446; Hepcidin; 1.
1: Evidence at protein level;
3D-structure; Antibiotic; Antimicrobial;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Fungicide; Hormone; Reference proteome; Secreted; Signal.
SIGNAL 1 24 {ECO:0000255}.
PROPEP 25 54
/FTId=PRO_0000013378.
PEPTIDE 60 84 Hepcidin-25.
/FTId=PRO_0000013379.
PEPTIDE 65 84 Hepcidin-20.
/FTId=PRO_0000013380.
DISULFID 66 82 {ECO:0000269|PubMed:19553669}.
DISULFID 69 72 {ECO:0000269|PubMed:19553669}.
DISULFID 70 78 {ECO:0000269|PubMed:19553669}.
DISULFID 73 81 {ECO:0000269|PubMed:19553669}.
VARIANT 59 59 R -> G (in HFE2B; dbSNP:rs779021719).
{ECO:0000269|PubMed:14670915}.
/FTId=VAR_042512.
VARIANT 70 70 C -> R (in HFE2B).
{ECO:0000269|PubMed:14630809}.
/FTId=VAR_042513.
VARIANT 71 71 G -> D (in HFE2B; dbSNP:rs104894696).
{ECO:0000269|PubMed:12915468,
ECO:0000269|PubMed:14633868,
ECO:0000269|PubMed:14670915}.
/FTId=VAR_026648.
VARIANT 78 78 C -> Y (in HFE2B).
{ECO:0000269|PubMed:15099344}.
/FTId=VAR_042514.
CONFLICT 31 31 T -> M (in Ref. 3; AAK14912).
{ECO:0000305}.
STRAND 66 71 {ECO:0000244|PDB:3H0T}.
STRAND 76 82 {ECO:0000244|PDB:3H0T}.
SEQUENCE 84 AA; 9408 MW; 5F8DCA23D19D29F7 CRC64;
MALSSQIWAA CLLLLLLLAS LTSGSVFPQQ TGQLAELQPQ DRAGARASWM PMFQRRRRRD
THFPICIFCC GCCHRSKCGM CCKT


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