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hephaestin (HEPH, KIAA0698, UNQ2562/PRO6242)
Function:
1) ferroxidase for Fe+2 to Fe+3 conversion
2) copper transport & homeostasis
3) iron homeostasis
- may mediate iron efflux associated to ferroportin 1
Cofactor: binds 6 Cu+/Cu+2 per monomer
Structure:
- belongs to the multicopper oxidase family
- contains 6 plastocyanin-like domains
Compartment: membrane
Alternative splicing: named isoforms=2
Expression:
- detected in breast, colon, bone trabecural cells, fibroblasts
General
carrier protein (transporter)
glycoprotein
membrane protein
metalloprotein
oxidoreductase
Properties
SIZE: MW = 130 kD
entity length = 1158 aa
COMPARTMENT: cellular membrane
MOTIF: signal sequence {1-23}
Plastocyanin-like 1 {24-206}
MOTIF: copper [Cu]-binding site
SITE: 126-126
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 128-128
MOTIF: histidine residue (3)
N-glycosylation site {N164}
cysteine residue {C180}
MODIFICATION: cysteine residue {C206}
copper [Cu]-binding site
SITE: 186-186
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 188-188
MOTIF: histidine residue (3)
cysteine residue {C206}
MODIFICATION: cysteine residue {C180}
Plastocyanin-like 2 {218-366}
MOTIF: N-glycosylation site {N236}
cysteine residue {C285}
MODIFICATION: cysteine residue {C366}
copper [Cu]-binding site
SITE: 304-304
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 347-347
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 352-352
MOTIF: histidine residue (3)
cysteine residue {C366}
MODIFICATION: cysteine residue {C285}
Plastocyanin-like 3 {379-560}
MOTIF: cysteine residue {C534}
MODIFICATION: cysteine residue {C560}
cysteine residue {C560}
MODIFICATION: cysteine residue {C534}
Plastocyanin-like 4 {570-718}
MOTIF: N-glycosylation site {N588}
cysteine residue {C637}
MODIFICATION: cysteine residue {C718}
copper [Cu]-binding site
SITE: 656-656
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 699-699
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 704-704
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 709-709
MOTIF: histidine residue (3)
N-glycosylation site {N714}
cysteine residue {C718}
MODIFICATION: cysteine residue {C637}
Plastocyanin-like 5 {731-903}
MOTIF: N-glycosylation site {N758}
N-glycosylation site {N829}
N-glycosylation site {N873}
cysteine residue {C877}
MODIFICATION: cysteine residue {C903}
cysteine residue {C903}
MODIFICATION: cysteine residue {C877}
Plastocyanin-like 6 {911-1087}
MOTIF: N-glycosylation site {N931}
copper [Cu]-binding site
SITE: 999-999
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 1000-1000
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 1003-1003
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 1005-1005
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 1045-1045
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 1046-1046
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 1047-1047
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 1051-1051
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 1056-1056
MOTIF: histidine residue (3)
transmembrane domain {1111-1131}
Database Correlations
OMIM 300167
UniProt Q9BQS7
PFAM correlations
References
UniProt :accession Q9BQS7