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A0A8C0RGS4 · A0A8C0RGS4_CANLF

Function

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Cu2+ (UniProtKB | Rhea| CHEBI:29036 )

Note: Binds 2 Cu2+ ions per subunit.
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds one Zn2+ ion per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site108Cu2+ 1 (UniProtKB | ChEBI); catalytic
Binding site109Cu2+ 1 (UniProtKB | ChEBI); catalytic
Binding site173Cu2+ 1 (UniProtKB | ChEBI); catalytic
Binding site243Cu2+ 1 (UniProtKB | ChEBI); catalytic
Binding site245Cu2+ 1 (UniProtKB | ChEBI); catalytic
Binding site315Cu2+ 1 (UniProtKB | ChEBI); catalytic
Binding site523Ca2+ (UniProtKB | ChEBI); structural
Binding site536C-terminal Xaa-(2S)-2-hydroxyglycine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI)
Binding site588Zn2+ (UniProtKB | ChEBI); catalytic
Binding site590Ca2+ (UniProtKB | ChEBI); structural
Binding site657C-terminal Xaa-(2S)-2-hydroxyglycine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI)
Binding site693Zn2+ (UniProtKB | ChEBI); catalytic
Binding site709C-terminal Xaa-(2S)-2-hydroxyglycine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI)
Binding site789Zn2+ (UniProtKB | ChEBI); catalytic
Binding site790Ca2+ (UniProtKB | ChEBI); structural

GO annotations

AspectTerm
Cellular Componenttransport vesicle membrane
Molecular Functioncopper ion binding
Molecular FunctionL-ascorbic acid binding
Molecular Functionlyase activity
Molecular Functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen
Biological Processpeptide metabolic process

Keywords

Names & Taxonomy

Protein names

  • Submitted names
    • Peptidylglycine alpha-amidating monooxygenase

Gene names

    • Name
      PAM

Organism names

Accessions

  • Primary accession
    A0A8C0RGS4
  • Secondary accessions
    • A0A8P0NA39

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasmic vesicle, secretory vesicle membrane
; Single-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane868-893Helical

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation.

Type
IDPosition(s)Description
Signal1-24
ChainPRO_504063604225-962
Disulfide bond48↔187
Disulfide bond82↔127
Disulfide bond115↔132
Disulfide bond228↔335
Disulfide bond294↔316
Disulfide bond637↔658
Disulfide bond705↔716
Glycosylation768N-linked (GlcNAc...) asparagine

Keywords

Family & Domains

Features

Showing features for domain, repeat, region.

Type
IDPosition(s)Description
Domain66-177Copper type II ascorbate-dependent monooxygenase N-terminal
Domain202-346Copper type II ascorbate-dependent monooxygenase C-terminal
Repeat573-614NHL
Repeat623-668NHL
Repeat676-720NHL
Repeat772-815NHL
Region925-962Disordered

Sequence similarities

In the C-terminal section; belongs to the peptidyl-alpha-hydroxyglycine alpha-amidating lyase family.
In the N-terminal section; belongs to the copper type II ascorbate-dependent monooxygenase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    962
  • Mass (Da)
    106,864
  • Last updated
    2022-01-19 v1
  • MD5 Checksum
    8818E6FCFEBBB9BB8E0F222C9DC1BAF6
MGRPPRPLLLLLLLLLLLLGLARALGFRGPLSVWKRFKENTRSFSNECLGTTRPVIPIDSSDFALDIHMPGVTPKQSDTYLCMSMRLPVDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSLHLTRLPQPLIAGMYLMMSVDTVIPPGEKVVNSDISCHYKKYPMHVFAYRVHTHHLGKVVSGYRVRNGQWALIGRQSPQLPQAFYPVEHPVDVSFGDILAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYMEAKHAVSFMTCTQNVAPDVFRTIPPEANIPIPVKPDMVMMHGHHKETENKEKTSLLQQPKGEEEMLEQGDFYSLLSKLLGEREDVVHVHKYNPTEKAESESDLVAEIANVVQKKDVGPPDARGSAEREDRGNAVLVRDRIHKFHRLESTLRPAESRVLSLQQPLPAEGTWEPDRSGDFHVEEALDWPGVYLLPGQVSGVALDAKNNLVIFHRGDHVWDGNSFDSMFVYQQRGLGPIEEDTILVIDPNNAAVLQSSGKNLFYLPHGLSVDKDGNYWVTDVALHQVFKLDPNSKGGPLLTLGRSMQPGSDQNHFCQPTDVAVDPDTGTIYVSDGYCNSRIVQFSPTGNFITQWGEESSRSNPKPGQFSVPHSLALVPHLGQLCVADRENGRIQCFKTDTKEFVREIKHASFGRNVFAISYIPGLLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVRKHFDMPHDIAASEDGTVYVGDAHTNTVWKFALTEKIEHRSVKKAGIEVQEIKESEAVVETKMENKPASTELQKMQEKQKLIKEPGLGVPIVLITTLLVIPVVVLLAIALYIRWKKSKAFGGKGSGGLNLGNFFASRKGYSRKGFDRLSTEGSDQEKDEDDGSESEEEYSAPLPAASASSS

Genome annotation databases

Similar Proteins

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