ID   HEPC1_SALSA             Reviewed;          86 AA.
AC   Q801Y3;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Hepcidin-1;
DE   Flags: Precursor;
GN   Name=hamp1; Synonyms=hep1;
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12697315; DOI=10.1016/s0145-305x(03)00036-3;
RA   Douglas S.E., Gallant J.W., Liebscher R.S., Dacanay A., Tsoi S.C.M.;
RT   "Identification and expression analysis of hepcidin-like antimicrobial
RT   peptides in bony fish.";
RL   Dev. Comp. Immunol. 27:589-601(2003).
CC   -!- FUNCTION: Seems to act as a signaling molecule involved in the
CC       maintenance of iron homeostasis. Seems to be required in conjunction
CC       with HFE to regulate both intestinal iron absorption and iron storage
CC       in macrophages. May also have antimicrobial activity (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the hepcidin family. {ECO:0000305}.
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DR   EMBL; AF542965; AAO85553.1; -; Transcribed_RNA.
DR   RefSeq; XP_014025519.1; XM_014170044.1.
DR   AlphaFoldDB; Q801Y3; -.
DR   STRING; 8030.ENSSSAP00000083302; -.
DR   GeneID; 106584587; -.
DR   KEGG; sasa:106584587; -.
DR   OrthoDB; 1623838at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa02.
DR   Bgee; ENSSSAG00000068171; Expressed in liver and 16 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
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..59
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000013395"
FT   PEPTIDE         62..86
FT                   /note="Hepcidin-1"
FT                   /id="PRO_0000013396"
FT   DISULFID        68..84
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..74
FT                   /evidence="ECO:0000250"
FT   DISULFID        72..80
FT                   /evidence="ECO:0000250"
FT   DISULFID        75..83
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   86 AA;  9456 MW;  B3F5A2010CB05E31 CRC64;
     MKAFSVAVVL VIACMFILES TAVPFSEVRT EEVGSFDSPV GEHQQPGGES MHLPEPFRFK
     RQIHLSLCGL CCNCCHNIGC GFCCKF