HEPC2_MOUSE
ID HEPC2_MOUSE Reviewed; 83 AA.
AC Q80T19; Q8BFW2;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Hepcidin-2;
DE Flags: Precursor;
GN Name=Hamp2; Synonyms=Hepc2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=12729891; DOI=10.1016/s0014-5793(03)00329-6;
RA Ilyin G., Courselaud B., Troadec M.-B., Pigeon C., Alizadeh M., Leroyer P.,
RA Brissot P., Loreal O.;
RT "Comparative analysis of mouse hepcidin 1 and 2 genes: evidence for
RT different patterns of expression and co-inducibility during iron
RT overload.";
RL FEBS Lett. 542:22-26(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Seems to act as a signaling molecule involved in the
CC maintenance of iron homeostasis. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Highly expressed in the liver and to a much lesser
CC extent in the heart. Also expressed in pancreas.
CC {ECO:0000269|PubMed:12729891}.
CC -!- SIMILARITY: Belongs to the hepcidin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC25194.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC25234.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY232841; AAO73588.1; -; mRNA.
DR EMBL; AK007975; BAC25194.1; ALT_INIT; mRNA.
DR EMBL; AK008993; BAC25234.1; ALT_INIT; mRNA.
DR CCDS; CCDS39894.2; -.
DR RefSeq; NP_899080.2; NM_183257.4.
DR AlphaFoldDB; Q80T19; -.
DR BioGRID; 211473; 2.
DR STRING; 10090.ENSMUSP00000074240; -.
DR MaxQB; Q80T19; -.
DR PaxDb; Q80T19; -.
DR PRIDE; Q80T19; -.
DR ProteomicsDB; 269734; -.
DR DNASU; 66438; -.
DR Ensembl; ENSMUST00000074671; ENSMUSP00000074240; ENSMUSG00000056978.
DR GeneID; 66438; -.
DR KEGG; mmu:66438; -.
DR CTD; 66438; -.
DR MGI; MGI:2153530; Hamp2.
DR VEuPathDB; HostDB:ENSMUSG00000056978; -.
DR eggNOG; ENOG502T0FU; Eukaryota.
DR GeneTree; ENSGT01030000240372; -.
DR InParanoid; Q80T19; -.
DR OMA; NCCRNAK; -.
DR OrthoDB; 1623838at2759; -.
DR PhylomeDB; Q80T19; -.
DR BioGRID-ORCS; 66438; 2 hits in 70 CRISPR screens.
DR PRO; PR:Q80T19; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q80T19; protein.
DR Bgee; ENSMUSG00000056978; Expressed in epithelium of stomach and 52 other tissues.
DR ExpressionAtlas; Q80T19; baseline and differential.
DR GO; GO:0045179; C:apical cortex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0014704; C:intercalated disc; ISO:MGI.
DR GO; GO:0005179; F:hormone activity; ISO:MGI.
DR GO; GO:0097690; F:iron ion transmembrane transporter inhibitor activity; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR GO; GO:0006879; P:cellular iron ion homeostasis; ISO:MGI.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; ISO:MGI.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:MGI.
DR GO; GO:0031640; P:killing of cells of another organism; ISO:MGI.
DR GO; GO:0060586; P:multicellular organismal iron ion homeostasis; ISO:MGI.
DR GO; GO:1904479; P:negative regulation of intestinal absorption; ISO:MGI.
DR GO; GO:0032413; P:negative regulation of ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:1904039; P:negative regulation of iron export across plasma membrane; ISO:MGI.
DR GO; GO:0034760; P:negative regulation of iron ion transmembrane transport; IBA:GO_Central.
DR GO; GO:1904255; P:negative regulation of iron ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; ISO:MGI.
DR GO; GO:1902916; P:positive regulation of protein polyubiquitination; ISO:MGI.
DR GO; GO:2000646; P:positive regulation of receptor catabolic process; ISO:MGI.
DR GO; GO:0002092; P:positive regulation of receptor internalization; ISO:MGI.
DR GO; GO:0010039; P:response to iron ion; ISO:MGI.
DR InterPro; IPR010500; Hepcidin.
DR PANTHER; PTHR16877; PTHR16877; 1.
DR Pfam; PF06446; Hepcidin; 1.
PE 2: Evidence at transcript level;
KW Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW Disulfide bond; Fungicide; Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..53
FT /evidence="ECO:0000250"
FT /id="PRO_0000013397"
FT PEPTIDE 59..83
FT /note="Hepcidin-2"
FT /id="PRO_0000013398"
FT DISULFID 65..81
FT /evidence="ECO:0000250"
FT DISULFID 68..71
FT /evidence="ECO:0000250"
FT DISULFID 69..77
FT /evidence="ECO:0000250"
FT DISULFID 72..80
FT /evidence="ECO:0000250"
SQ SEQUENCE 83 AA; 9410 MW; 3CD253E35F3AF90E CRC64;
MALSTRTQAA CLLLLLLASL SSTTYLQQQM RQTTELQPLH GEESRADIAI PMQKRRKRDI
NFPICRFCCQ CCNKPSCGIC CEE
