H2A0M3 · AMO_PINMG

Function

Cofactor

Protein has several cofactor binding sites:
Cu cation (UniProtKB | Rhea| CHEBI:23378 )

Note: Binds 1 copper ion per subunit.
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Binds 2 calcium ions per subunit.
L-topaquinone (UniProtKB | Rhea| CHEBI:79027 )

Note: Contains 1 topaquinone per subunit.
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 1 Mn2+ ion per subunit.

Features

Showing features for binding site, active site.

1781100200300400500600700
TypeIDPosition(s)Description
Binding site385-395substrate
Active site387Proton acceptor
Binding site472-477substrate
Active site475Schiff-base intermediate with substrate; via topaquinone
Binding site525Cu cation (UniProtKB | ChEBI)
Binding site527Cu cation (UniProtKB | ChEBI)
Binding site534Ca2+ 1 (UniProtKB | ChEBI)
Binding site534Mn2+ (UniProtKB | ChEBI)
Binding site536Ca2+ 1 (UniProtKB | ChEBI)
Binding site536Mn2+ (UniProtKB | ChEBI)
Binding site579Ca2+ 2 (UniProtKB | ChEBI)
Binding site671Ca2+ 2 (UniProtKB | ChEBI)
Binding site674Ca2+ 2 (UniProtKB | ChEBI)
Binding site676Ca2+ 2 (UniProtKB | ChEBI)
Binding site682Ca2+ 1 (UniProtKB | ChEBI)
Binding site682Mn2+ (UniProtKB | ChEBI)
Binding site683Ca2+ 1 (UniProtKB | ChEBI)
Binding site693Cu cation (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
Cellular Componentplasma membrane
Molecular Functioncopper ion binding
Molecular Functionprimary amine oxidase activity
Molecular Functionquinone binding
Biological Processamine metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Putative amine oxidase [copper-containing]
  • EC number

Organism names

Accessions

  • Primary accession
    H2A0M3

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, modified residue.

TypeIDPosition(s)Description
Signal1-34
ChainPRO_000041801835-781Putative amine oxidase [copper-containing]
Disulfide bond199↔203
Disulfide bond405↔432
Modified residue4752',4',5'-topaquinone

Post-translational modification

Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.

Keywords

Expression

Tissue specificity

Prismatic layer of shell (at protein level). Expressed primarily in the mantle with highest level in the mantle edge and lower level in the mantle pallium.

Interaction

Subunit

Homodimer.

Structure

Family & Domains

Sequence similarities

Belongs to the copper/topaquinone oxidase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    781
  • Mass (Da)
    89,950
  • Last updated
    2012-03-21 v1
  • Checksum
    49A8CBC587935AF0
MSLPKTANGMDKLKLCYLLLFYLGSSSLTEVSGAQTCEIDSVLCTSDLSEPDDPPIFHDLTTKEIKSVQTYLYHQRDLRLLRPGLAKINTSFIQGMELYLPNKKDVIHYLQSKVPTPKPPRAAVVTIFRGDCDPAVVEEYIVFPLPWPTQHRLHRKVPYYLRPFNDVEFATISDFLTKQVDGVLRQFLEESFGGRLINCGNRCLNFQFASPVGPSVSNEPGARKSWYWLHQLVEYSALHPVDFAVLMKIVGCVYTIEKVYFNNMYFNSLQEVALHYRNPSFPRLRIPYPVDSKQLFSKMERRGILFPEKPVSPPRQVEPEGKRYSVKYQEVKYMNWKFNFRLSPGLGPRLHNIRYHDRLIVYELALQDIVVFYSGAEPPHQYANFFDSSYMIGMNLQGMVPGVDCPTGATFIDSHILTESSLKPAKLINAFCVFEQNTGDFLRRHISKTSPDGPFYEGVPSIVLVLRAITTIANYDYTIDFIFHHNGVLQTKVVPTGYILPSLYTKQNENKYGFRLNNKLIGNLHHHLFNFKVDIDINGQHNRYETLDIVLDKTSHPVSKKPYDVWYQNKIKHNLRKTEMEALFKYDFDKPMHHIFYNNNLKSPEGNNMAYRLVNRGMSKSLLPECSGNEGTGAWMRHQIAVTKRKETELTSSSVYSAFGTKNPVVNFRNFYADNENIVDEDLVAWVTMGTYHIPHTEDLPVTHTPGLDLSFFLSPFNYFPEDPAMGSRDSVRIEAVDKNNLKRGIKIDKQTFPEKMTCKAPIGNYFEYILKRPNVIFDIQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HE610390
EMBL· GenBank· DDBJ
CCE46164.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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