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hephaestin-like protein 1 (HEPHL1)
Function:
- may function as a ferroxidase & may be involved in copper transport & homeostasis (putative)
Cofactor: binds 6 copper ions per monomer (putative)
Structure:
- belongs to the multicopper oxidase family
- contains 6 plastocyanin-like domains
Compartment: membrane (putative)
General
glycoprotein
membrane protein
metalloprotein
oxidoreductase
Properties
SIZE: entity length = 1159 aa
MW = 132 kD
COMPARTMENT: cellular membrane
MOTIF: signal sequence {1-24}
Plastocyanin-like 1 {25-207}
MOTIF: copper [Cu]-binding site
SITE: 127-127
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 129-129
MOTIF: histidine residue (3)
N-glycosylation site {N161}
cysteine residue {C181}
MODIFICATION: cysteine residue {C207}
copper [Cu]-binding site
SITE: 187-187
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 189-189
MOTIF: histidine residue (3)
cysteine residue {C207}
MODIFICATION: cysteine residue {C181}
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 {379-561}
MOTIF: N-glycosylation site {N407}
cysteine residue {C535}
MODIFICATION: cysteine residue {C561}
cysteine residue {C561}
MODIFICATION: cysteine residue {C535}
Plastocyanin-like 4 {571-719}
MOTIF: N-glycosylation site {N589}
cysteine residue {C638}
MODIFICATION: cysteine residue {C719}
copper [Cu]-binding site
SITE: 657-657
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 700-700
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 705-705
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 710-710
MOTIF: histidine residue (3)
cysteine residue {C719}
MODIFICATION: cysteine residue {C638}
Plastocyanin-like 5 {731-907}
MOTIF: N-glycosylation site {N772}
cysteine residue {C881}
MODIFICATION: cysteine residue {C907}
cysteine residue {C907}
MODIFICATION: cysteine residue {C881}
Plastocyanin-like 6 {915-1092}
MOTIF: N-glycosylation site {N935}
copper [Cu]-binding site
SITE: 1002-1002
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 1003-1003
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 1006-1006
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 1008-1008
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 1048-1048
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 1049-1049
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 1050-1050
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 1054-1054
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 1059-1059
MOTIF: histidine residue (3)
transmembrane domain {1115-1135}
Database Correlations
UniProt Q6MZM0
Pfam PF07731
Kegg hsa:3412
References
UniProt :accession Q6MZM0