ID   HEPC_CANLF              Reviewed;          85 AA.
AC   Q5U9D2; Q5EES0;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Hepcidin;
DE   Flags: Precursor;
GN   Name=HAMP;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Shi J., Wei Y., Boothe D.;
RT   "Identification of dog hepcidin.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Li X.D., Zhao T.Z., Sun M., Tian K.G., Chen X.Z.;
RT   "Identification of dog hepcidin in China.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
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. Controls the major flows of iron into plasma:
CC       absorption of dietary iron in the intestine, recycling of iron by
CC       macrophages, which phagocytose old erythrocytes and other cells, and
CC       mobilization of stored iron from hepatocytes.
CC       {ECO:0000250|UniProtKB:P81172}.
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. {ECO:0000250|UniProtKB:P81172}.
CC   -!- SUBUNIT: Interacts with SLC40A1; this interaction promotes SLC40A1
CC       rapid ubiquitination. {ECO:0000250|UniProtKB:P81172}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the hepcidin family. {ECO:0000305}.
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DR   EMBL; AY772532; AAV40979.1; -; mRNA.
DR   EMBL; AY899807; AAW82336.1; -; mRNA.
DR   RefSeq; NP_001007141.1; NM_001007140.1.
DR   AlphaFoldDB; Q5U9D2; -.
DR   SMR; Q5U9D2; -.
DR   STRING; 9615.ENSCAFP00000010474; -.
DR   PaxDb; Q5U9D2; -.
DR   GeneID; 492281; -.
DR   KEGG; cfa:492281; -.
DR   CTD; 57817; -.
DR   eggNOG; ENOG502T0FU; Eukaryota.
DR   InParanoid; Q5U9D2; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR   GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR   GO; GO:0034760; P:negative regulation of iron ion transmembrane transport; IBA:GO_Central.
DR   InterPro; IPR010500; Hepcidin.
DR   PANTHER; PTHR16877; PTHR16877; 1.
DR   Pfam; PF06446; Hepcidin; 1.
PE   3: Inferred from homology;
KW   Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW   Disulfide bond; Hormone; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..54
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000013376"
FT   PEPTIDE         61..85
FT                   /note="Hepcidin"
FT                   /id="PRO_0000013377"
FT   DISULFID        67..83
FT                   /evidence="ECO:0000250"
FT   DISULFID        70..73
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..79
FT                   /evidence="ECO:0000250"
FT   DISULFID        74..82
FT                   /evidence="ECO:0000250"
FT   CONFLICT        81
FT                   /note="L -> F (in Ref. 2; AAW82336)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   85 AA;  9172 MW;  39C3114830CED31B CRC64;
     MALSTRIQAA CLLLLLLASV ASVSVLPHQT GQLTDLRAQD TAGAEAGLQP TLQLRRLRRR
     DTHFPICIFC CGCCKTPKCG LCCKT