ID   HEPC_LARCR              Reviewed;          85 AA.
AC   A1Z0M0;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Hepcidin {ECO:0000312|EMBL:ABL96317.2};
DE   Flags: Precursor;
GN   Name=hamp {ECO:0000250|UniProtKB:P81172};
OS   Larimichthys crocea (Large yellow croaker) (Pseudosciaena crocea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Sciaenidae; Larimichthys.
OX   NCBI_TaxID=215358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=19150638; DOI=10.1016/j.peptides.2008.12.014;
RA   Wang K.-J., Cai J.-J., Cai L., Qu H.-D., Yang M., Zhang M.;
RT   "Cloning and expression of a hepcidin gene from a marine fish
RT   (Pseudosciaena crocea) and the antimicrobial activity of its synthetic
RT   peptide.";
RL   Peptides 30:638-646(2009).
RN   [2]
RP   PROTEIN SEQUENCE OF 65-85, FUNCTION, SUBUNIT, AND MASS SPECTROMETRY.
RC   TISSUE=Head kidney;
RX   PubMed=19344770; DOI=10.1016/j.fsi.2009.03.014;
RA   Zhang J., Yan Q., Ji R., Zou W., Guo G.;
RT   "Isolation and characterization of a hepcidin peptide from the head kidney
RT   of large yellow croaker, Pseudosciaena crocea.";
RL   Fish Shellfish Immunol. 26:864-870(2009).
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 (By similarity). {ECO:0000250|UniProtKB:Q9EQ21}.
CC   -!- FUNCTION: Has very strong antibacterial activity against the marine
CC       Gram-negative bacteria V.alginolyticus (MIC=24 uM), V.fluvialis,
CC       V.harveyis (MIC=12 uM) and V.parahaemolyticus (MIC=6 uM). Has
CC       antibacterial activity against the Gram-negative bacteria A.hydrophila
CC       (MIC=6 uM), E.coli (MIC=24 uM), and E.coli BL21(DE3)plysS (MIC=6 uM),
CC       and the Gram-positive bacteria B.cereus (MIC=24 uM), B.subtilis (MIC=6
CC       uM), C.glutamicum (MIC=3 uM), M.luteus (MIC=3 uM), M.lysodeikticus,
CC       S.aureus (MIC=6 uM) and S.epidermis (MIC=12 uM). Possesses antifungal
CC       activity against A.niger (MIC=24 uM), F.graminearum (MIC24 uM) and
CC       F.solani (MIC=24 uM), but lacks antifungal activity against the yeasts
CC       P.pastoris GS115 and C.albicans. {ECO:0000269|PubMed:19150638,
CC       ECO:0000269|PubMed:19344770}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19344770}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9EQ21}.
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues tested, with highest
CC       levels of expression in kidney and lowest levels in liver. Intra-
CC       peritoneal injection of lipopolysaccharide results in increased
CC       expression in heart, spleen and stomach, but not in kidney or liver.
CC       {ECO:0000269|PubMed:19150638}.
CC   -!- MASS SPECTROMETRY: Mass=2524.2; Mass_error=2; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19344770};
CC   -!- SIMILARITY: Belongs to the hepcidin family. {ECO:0000255}.
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DR   EMBL; EF156401; ABL96317.2; -; mRNA.
DR   EMBL; EU443735; ACB98724.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1Z0M0; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IDA:UniProtKB.
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   InterPro; IPR010500; Hepcidin.
DR   PANTHER; PTHR16877; PTHR16877; 1.
DR   Pfam; PF06446; Hepcidin; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Hormone; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..64
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000363724"
FT   PEPTIDE         65..85
FT                   /note="Hepcidin"
FT                   /id="PRO_0000363725"
FT   DISULFID        66..83
FT                   /evidence="ECO:0000250"
FT   DISULFID        69..72
FT                   /evidence="ECO:0000250"
FT   DISULFID        70..79
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..82
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   85 AA;  9685 MW;  31060E56659EE61F CRC64;
     MKTFSVAVAV AVVLAFICLQ ESSAVPANEE QELEQQIYFA DPEMPVESCK MPYYMRENRQ
     GSPARCRFCC RCCPRMRGCG ICCRF