ID   HEPC2_DANRE             Reviewed;          91 AA.
AC   Q7T273; A7UDN3;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 3.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Hepcidin-2;
DE   Flags: Precursor;
GN   Name=hamp2; Synonyms=hamp;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15043943; DOI=10.1016/j.dci.2003.11.009;
RA   Shike H., Shimizu C., Lauth X., Burns J.C.;
RT   "Organization and expression analysis of the zebrafish hepcidin gene, an
RT   antimicrobial peptide gene conserved among vertebrates.";
RL   Dev. Comp. Immunol. 28:747-754(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Liver;
RA   Gong H.Y., Wu J.L.;
RT   "Zebrafish hepcidin antimicrobial peptide expressed in the liver and
RT   regulated by HNF1.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Jeffy G., Sanath K., Karunasagar I., Karunasagar I.;
RT   "cDNA cloning and expression of antimicrobial peptide hepcidin from Danio
RT   rerio.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; AY363453; AAR18593.1; -; Genomic_DNA.
DR   EMBL; AY130989; AAN10302.1; -; mRNA.
DR   EMBL; AY258137; AAP80240.1; -; Genomic_DNA.
DR   EMBL; EU047750; ABU23729.1; -; mRNA.
DR   EMBL; BC162314; AAI62314.1; -; mRNA.
DR   EMBL; BC162321; AAI62321.1; -; mRNA.
DR   EMBL; BC163916; AAI63916.1; -; mRNA.
DR   RefSeq; NP_991146.1; NM_205583.2.
DR   RefSeq; XP_005170823.1; XM_005170766.3.
DR   AlphaFoldDB; Q7T273; -.
DR   SMR; Q7T273; -.
DR   STRING; 7955.ENSDARP00000069720; -.
DR   PaxDb; Q7T273; -.
DR   Ensembl; ENSDART00000167332; ENSDARP00000131567; ENSDARG00000102175.
DR   GeneID; 402837; -.
DR   KEGG; dre:402837; -.
DR   CTD; 57817; -.
DR   ZFIN; ZDB-GENE-050726-1; hamp.
DR   eggNOG; ENOG502SA4E; Eukaryota.
DR   GeneTree; ENSGT00390000003154; -.
DR   HOGENOM; CLU_2426380_0_0_1; -.
DR   InParanoid; Q7T273; -.
DR   OMA; PPEHFRF; -.
DR   OrthoDB; 1578654at2759; -.
DR   TreeFam; TF330932; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 16.
DR   Bgee; ENSDARG00000102175; Expressed in spleen and 16 other tissues.
DR   ExpressionAtlas; Q7T273; baseline.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0001530; F:lipopolysaccharide binding; IDA:ZFIN.
DR   GO; GO:0070891; F:lipoteichoic acid binding; IDA:ZFIN.
DR   GO; GO:0042834; F:peptidoglycan binding; IDA:ZFIN.
DR   GO; GO:0140367; P:antibacterial innate immune response; IDA:ZFIN.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
DR   GO; GO:0071393; P:cellular response to progesterone stimulus; IMP:ZFIN.
DR   GO; GO:0071383; P:cellular response to steroid hormone stimulus; IMP:ZFIN.
DR   GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:ZFIN.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:ZFIN.
DR   GO; GO:0055072; P:iron ion homeostasis; IMP:ZFIN.
DR   GO; GO:0009617; P:response to bacterium; IDA:ZFIN.
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..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..64
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000013389"
FT   PEPTIDE         67..91
FT                   /note="Hepcidin-2"
FT                   /id="PRO_0000013390"
FT   DISULFID        73..89
FT                   /evidence="ECO:0000250"
FT   DISULFID        76..79
FT                   /evidence="ECO:0000250"
FT   DISULFID        77..85
FT                   /evidence="ECO:0000250"
FT   DISULFID        80..88
FT                   /evidence="ECO:0000250"
FT   CONFLICT        56
FT                   /note="T -> A (in Ref. 1; AAR18593)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   91 AA;  10517 MW;  2602EAD89C31CE53 CRC64;
     MKLSNVFLAA VVILTCVCVF QITAVPFIQQ VQDEHHVESE ELQENQHLTE AEHRLTDPLV
     LFRTKRQSHL SLCRFCCKCC RNKGCGYCCK F