HEPC_MORCS
ID HEPC_MORCS Reviewed; 85 AA.
AC P82951;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Hepcidin;
DE Flags: Precursor;
GN Name=hamp;
OS Morone chrysops x Morone saxatilis (White bass x Striped bass).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Moronidae; Morone.
OX NCBI_TaxID=45352;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 65-85, TISSUE
RP SPECIFICITY, ANTIBACTERIAL ACTIVITY, AND MASS SPECTROMETRY.
RC TISSUE=Gill, and Skin;
RX PubMed=11985602; DOI=10.1046/j.1432-1033.2002.02881.x;
RA Shike H., Lauth X., Westerman M.E., Ostland V.E., Carlberg J.M.,
RA Van Olst J.C., Shimizu C., Bulet P., Burns J.C.;
RT "Bass hepcidin is a novel antimicrobial peptide induced by bacterial
RT challenge.";
RL Eur. J. Biochem. 269:2232-2237(2002).
RN [2]
RP STRUCTURE BY NMR OF 65-85, AND DISULFIDE BONDS.
RX PubMed=15546886; DOI=10.1074/jbc.m411154200;
RA Lauth X., Babon J.J., Stannard J.A., Singh S., Nizet V., Carlberg J.M.,
RA Ostland V.E., Pennington M.W., Norton R.S., Westerman M.E.;
RT "Bass hepcidin synthesis, solution structure, antimicrobial activities and
RT synergism, and in vivo hepatic response to bacterial infections.";
RL J. Biol. Chem. 280:9272-9282(2005).
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}.
CC -!- FUNCTION: Antimicrobial activity against Gram-negative bacteria such as
CC E.coli.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in liver.
CC {ECO:0000269|PubMed:11985602}.
CC -!- INDUCTION: By bacterial challenge.
CC -!- MASS SPECTROMETRY: Mass=2255.97; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11985602};
CC -!- SIMILARITY: Belongs to the hepcidin family. {ECO:0000305}.
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DR EMBL; AF394245; AAM28439.1; -; Genomic_DNA.
DR EMBL; AF394246; AAM28440.1; -; mRNA.
DR PDB; 1S6W; NMR; -; A=65-85.
DR PDBsum; 1S6W; -.
DR AlphaFoldDB; P82951; -.
DR SMR; P82951; -.
DR EvolutionaryTrace; P82951; -.
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 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW Disulfide bond; Hormone; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..64
FT /evidence="ECO:0000269|PubMed:11985602"
FT /id="PRO_0000013391"
FT PEPTIDE 65..85
FT /note="Hepcidin"
FT /id="PRO_0000013392"
FT DISULFID 66..83
FT /evidence="ECO:0000269|PubMed:15546886"
FT DISULFID 69..72
FT /evidence="ECO:0000269|PubMed:15546886"
FT DISULFID 70..79
FT /evidence="ECO:0000269|PubMed:15546886"
FT DISULFID 73..82
FT /evidence="ECO:0000269|PubMed:15546886"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1S6W"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1S6W"
SQ SEQUENCE 85 AA; 9484 MW; 0FEA55CF0A522C84 CRC64;
MKTFSVAVAV AVVLAFICLQ ESSAVPVTEV QELEEPMSNE YQEMPVESWK MPYNNRHKRH
SSPGGCRFCC NCCPNMSGCG VCCRF
