A0A804HKV8 · A0A804HKV8_HUMAN
- ProteinPeptidylglycine alpha-amidating monooxygenase
- GenePAM
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids798 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
Catalytic activity
- a [peptide]-C-terminal (2S)-2-hydroxyglycine = a [peptide]-C-terminal amide + glyoxylate
Cofactor
Protein has several cofactor binding sites:
Note: Binds 2 Cu2+ ions per subunit.
Note: Binds one Zn2+ ion per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 102 | Cu2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 103 | Cu2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 167 | Cu2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 237 | Cu2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 239 | Cu2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 309 | Cu2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: M | ||||||
Binding site | 410 | Ca2+ (UniProtKB | ChEBI); structural | ||||
Sequence: V | ||||||
Binding site | 423 | C-terminal Xaa-(2S)-2-hydroxyglycine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 475 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 477 | Ca2+ (UniProtKB | ChEBI); structural | ||||
Sequence: L | ||||||
Binding site | 544 | C-terminal Xaa-(2S)-2-hydroxyglycine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 580 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 596 | C-terminal Xaa-(2S)-2-hydroxyglycine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 676 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 677 | Ca2+ (UniProtKB | ChEBI); structural | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | transport vesicle membrane | |
Molecular Function | copper ion binding | |
Molecular Function | L-ascorbic acid binding | |
Molecular Function | lyase activity | |
Molecular Function | oxidoreductase 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 Process | peptide metabolic process |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A804HKV8
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cytoplasmic vesicle, secretory vesicle membrane ; Single-pass membrane protein
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-20 | UniProt | |||||
Sequence: MAGRVPSLLVLLVFPSSCLA | |||||||
Chain | PRO_5032475910 | 21-798 | UniProt | ||||
Sequence: FRSPLSVFKRFKETTRPFSNECLGTTRPVVPIDSSDFALDIRMPGVTPKQSDTYFCMSMRIPVDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNNKDCSGVSLHLTRLPQPLIAGMYLMMSVDTVIPAGEKVVNSDISCHYKNYPMHVFAYRVHTHHLGKVVSGYRVRNGQWTLIGRQSPQLPQAFYPVGHPVDVSFGDLLAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYMEAKHAVSFMTCTQNVAPDMFRTIPPEANIPIPVKSDMVMMHEHHKETEYKDKIPLLQQPKREEEEVLDQDFHMEEALDWPGVYLLPGQVSGVALDPKNNLVIFHRGDHVWDGNSFDSKFVYQQIGLGPIEEDTILVIDPNNAAVLQSSGKNLFYLPHGLSIDKDGNYWVTDVALHQVFKLDPNNKEGPVLILGRSMQPGSDQNHFCQPTDVAVDPGTGAIYVSDGYCNSRIVQFSPSGKFITQWGEESSGSSPLPGQFTVPHSLALVPLLGQLCVADRENGRIQCFKTDTKEFVREIKHSSFGRNVFAISYIPGLLFAVNGKPHFGDQEPVQGFVMNFSNGEIIDIFKPVRKHFDMPHDIVASEDGTVYIGDAHTNTVWKFTLTEKLEHRSVKKAGIEVQEIKDSEHKLETSSGRVLGRFRGKGSGGLNLGNFFASRKGYSRKGFDRLSTEGSDQEKEDDGSESEEEYSAPLPALAPSSS | |||||||
Disulfide bond | 42↔181 | UniProt | |||||
Sequence: CLGTTRPVVPIDSSDFALDIRMPGVTPKQSDTYFCMSMRIPVDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNNKDC | |||||||
Disulfide bond | 76↔121 | UniProt | |||||
Sequence: CMSMRIPVDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTGSYWFC | |||||||
Disulfide bond | 109↔126 | UniProt | |||||
Sequence: CNMPSSTGSYWFCDEGTC | |||||||
Disulfide bond | 222↔329 | UniProt | |||||
Sequence: CHYKNYPMHVFAYRVHTHHLGKVVSGYRVRNGQWTLIGRQSPQLPQAFYPVGHPVDVSFGDLLAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYMEAKHAVSFMTC | |||||||
Disulfide bond | 288↔310 | UniProt | |||||
Sequence: CVFTGEGRTEATHIGGTSSDEMC | |||||||
Disulfide bond | 524↔545 | UniProt | |||||
Sequence: CQPTDVAVDPGTGAIYVSDGYC | |||||||
Disulfide bond | 592↔603 | UniProt | |||||
Sequence: CVADRENGRIQC | |||||||
Glycosylation | 655 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 743 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 754 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 767 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 768 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 771 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 780 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 782 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, repeat, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 60-171 | Copper type II ascorbate-dependent monooxygenase N-terminal | ||||
Sequence: DIRMPGVTPKQSDTYFCMSMRIPVDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDI | ||||||
Domain | 196-340 | Copper type II ascorbate-dependent monooxygenase C-terminal | ||||
Sequence: IAGMYLMMSVDTVIPAGEKVVNSDISCHYKNYPMHVFAYRVHTHHLGKVVSGYRVRNGQWTLIGRQSPQLPQAFYPVGHPVDVSFGDLLAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYMEAKHAVSFMTCTQNVAPDMFRT | ||||||
Repeat | 460-501 | NHL | ||||
Sequence: AAVLQSSGKNLFYLPHGLSIDKDGNYWVTDVALHQVFKLDPN | ||||||
Repeat | 510-555 | NHL | ||||
Sequence: LGRSMQPGSDQNHFCQPTDVAVDPGTGAIYVSDGYCNSRIVQFSPS | ||||||
Repeat | 563-607 | NHL | ||||
Sequence: GEESSGSSPLPGQFTVPHSLALVPLLGQLCVADRENGRIQCFKTD | ||||||
Repeat | 659-702 | NHL | ||||
Sequence: GEIIDIFKPVRKHFDMPHDIVASEDGTVYIGDAHTNTVWKFTLT | ||||||
Region | 762-798 | Disordered | ||||
Sequence: GFDRLSTEGSDQEKEDDGSESEEEYSAPLPALAPSSS |
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length798
- Mass (Da)88,744
- Last updated2021-09-29 v1
- Checksum3B4AEDA2D5CD7BDB
Computationally mapped potential isoform sequences
There are 18 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
P19021 | AMD_HUMAN | PAM | 973 | ||
D6RG20 | D6RG20_HUMAN | PAM | 68 | ||
D6RF09 | D6RF09_HUMAN | PAM | 29 | ||
D6RAQ2 | D6RAQ2_HUMAN | PAM | 42 | ||
D6RDU2 | D6RDU2_HUMAN | PAM | 25 | ||
F8W8D9 | F8W8D9_HUMAN | PAM | 175 | ||
D6RCD5 | D6RCD5_HUMAN | PAM | 53 | ||
H0Y9I4 | H0Y9I4_HUMAN | PAM | 250 | ||
D6R961 | D6R961_HUMAN | PAM | 28 | ||
A0A8C8KD64 | A0A8C8KD64_HUMAN | PAM | 973 | ||
A0A804HI59 | A0A804HI59_HUMAN | PAM | 897 | ||
A0A804HIQ0 | A0A804HIQ0_HUMAN | PAM | 867 | ||
H7BYD9 | H7BYD9_HUMAN | PAM | 679 | ||
A0A804HLE0 | A0A804HLE0_HUMAN | PAM | 265 | ||
A0A804HLJ2 | A0A804HLJ2_HUMAN | PAM | 71 | ||
A0A804HK31 | A0A804HK31_HUMAN | PAM | 83 | ||
A0A804HJJ2 | A0A804HJJ2_HUMAN | PAM | 150 | ||
A0A804HKM7 | A0A804HKM7_HUMAN | PAM | 830 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC008501 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC008779 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC010250 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC113373 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |