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A0A5F8H1V1 · A0A5F8H1V1_MONDO

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 site103Cu2+ 1 (UniProtKB | ChEBI); catalytic
Binding site104Cu2+ 1 (UniProtKB | ChEBI); catalytic
Binding site168Cu2+ 1 (UniProtKB | ChEBI); catalytic
Binding site238Cu2+ 1 (UniProtKB | ChEBI); catalytic
Binding site240Cu2+ 1 (UniProtKB | ChEBI); catalytic
Binding site310Cu2+ 1 (UniProtKB | ChEBI); catalytic
Binding site517Ca2+ (UniProtKB | ChEBI); structural
Binding site530C-terminal Xaa-(2S)-2-hydroxyglycine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI)
Binding site582Zn2+ (UniProtKB | ChEBI); catalytic
Binding site584Ca2+ (UniProtKB | ChEBI); structural
Binding site651C-terminal Xaa-(2S)-2-hydroxyglycine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI)
Binding site687Zn2+ (UniProtKB | ChEBI); catalytic
Binding site703C-terminal Xaa-(2S)-2-hydroxyglycine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI)
Binding site783Zn2+ (UniProtKB | ChEBI); catalytic
Binding site784Ca2+ (UniProtKB | ChEBI); structural

GO annotations

AspectTerm
Cellular Componenttransport vesicle membrane
Molecular Functioncopper ion binding
Molecular FunctionL-ascorbic acid binding
Molecular Functionpeptidylamidoglycolate lyase activity
Molecular Functionpeptidylglycine monooxygenase activity
Biological Processpeptide metabolic process

Keywords

Names & Taxonomy

Protein names

  • Submitted names
    • Peptidylglycine alpha-amidating monooxygenase

Gene names

    • Name
      PAM

Organism names

Accessions

  • Primary accession
    A0A5F8H1V1

Proteomes

Subcellular Location

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

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

Type
IDPosition(s)Description
Signal1-21
ChainPRO_502388942022-908
Disulfide bond43↔182
Disulfide bond77↔122
Disulfide bond110↔127
Disulfide bond223↔330
Disulfide bond289↔311
Disulfide bond631↔652
Disulfide bond699↔710

Keywords

Expression

Gene expression databases

Family & Domains

Features

Showing features for domain, region, compositional bias, repeat.

Type
IDPosition(s)Description
Domain61-172Copper type II ascorbate-dependent monooxygenase N-terminal
Domain197-341Copper type II ascorbate-dependent monooxygenase C-terminal
Region466-491Disordered
Compositional bias472-487Polar residues
Repeat567-608NHL
Repeat617-662NHL
Repeat680-714NHL
Repeat766-809NHL
Region869-908Disordered

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    908
  • Mass (Da)
    101,323
  • Last updated
    2019-12-11 v1
  • MD5 Checksum
    886DB2D265942E163D03090F9A1F1CE4
MAGLVNNLLILFLGLQSSCLAFRSPLSVFKRYKESTRSFSNECLGTSRPIIPIDSSDFALDIRMPGVTPKQSDTYLCMSLRLPMDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTESYWDCDEGTCSDKVNILYAWARNAPPTRLPKGVGFRVGGAMGSKYFVLQVHYGDISAFRDNHKDCSGVTLHLTRLQQPLIAGMYLMMSVDTVIPPGEKVVNADISCHYKKYPMHLFAYRVHTHHLGKVVSGYRVRNGQWTLIGRQSPQLPQAFYPVEHPVDVSFGDILAARCVFSGEGRTEETHIGGTSSDEMCNLYIMYYMEAKHAVSFMTCTQNVDPAMFATIPAEANIPIPVKSDLVMMHGHHKETENKDHLPLLQQPKREEEEVLDQGDFYSLISKLLGEREDVVHVHKYNPTEKAESDLVAEIANVVQKKDLDWSGTREGADHNVRGNAILVRDRIHKFHRLESTLKPPDNKHFSLQQPPQDEGTQETEHTGDFHVEEALDWPGVYLLPGQVSGVALDSDGNLVIFHRGDHIWDGNSFDSKFVYQQRGLGPIEEDTILVIDPNNAAVLQSTGKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLDPRNKGSPLLILGRSMQPGSDKSHFCQPTDVAVDPVTGTIYVSDGYCNSRIVQFSKDGVFMSQWGEESSGDNPKPGQFQVPHSLTLVPHFGQLCVADRENGRIQCFKTETKEFVREIKHTAFGRNVFAISYTPGLLFAVNGKPQLGDKQPLQGFVMNFTSGEILDTFTPVRKRFDMPHDLVASEDGTVYVGDAHADTVWKFTTAEKMEHRSVKKAGIEVHEVKADSEHKLETSSGRILGRLRGKGSGGLNLGNFFANRKGYSRKGFDRLSTEGSDQEKDDEGSDSEEEYSAPPPRPASVSSLN

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
F6SHA5F6SHA5_MONDOPAM976
A0A5F8G7D0A0A5F8G7D0_MONDOPAM818
A0A5F8G7W8A0A5F8G7W8_MONDOPAM870

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias472-487Polar residues

Keywords

Sequence databases

Genome annotation databases

Similar Proteins

Disclaimer

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