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Pam peptidylglycine alpha-amidating monooxygenase [ Rattus norvegicus (Norway rat) ]

Gene ID: 25508, updated on 13-Apr-2024

Summary

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Symbol
Pamprovided by RGD
Full Name
peptidylglycine alpha-amidating monooxygenaseprovided by RGD
Primary source
RGD:3252
See related
Ensembl:ENSRNOG00000033280 AllianceGenome:RGD:3252
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Rattus norvegicus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Also known as
PHM
Summary
Enables several functions, including metal ion binding activity; peptidylamidoglycolate lyase activity; and peptidylglycine monooxygenase activity. Involved in several processes, including animal organ development; fatty acid primary amide biosynthetic process; and peptide amidation. Located in several cellular components, including perikaryon; secretory granule membrane; and trans-Golgi network. Biomarker of hypothyroidism. Orthologous to human PAM (peptidylglycine alpha-amidating monooxygenase). [provided by Alliance of Genome Resources, Apr 2022]
Expression
Biased expression in Heart (RPKM 2320.3), Lung (RPKM 427.0) and 5 other tissues See more
Orthologs
human mouse all
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Genomic context

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Location:
9q36
Exon count:
31
Annotation release Status Assembly Chr Location
RS_2024_02 current GRCr8 (GCF_036323735.1) 9 NC_086027.1 (105445812..105719287)
RS_2023_06 previous assembly mRatBN7.2 (GCF_015227675.2) 9 NC_051344.1 (97998581..98271966)
106 previous assembly Rnor_6.0 (GCF_000001895.5) 9 NC_005108.4 (111028543..111177588)

Chromosome 9 - NC_086027.1Genomic Context describing neighboring genes Neighboring gene solute carrier organic anion transporter family, member 6d1 Neighboring gene tumor protein, translationally-controlled 1 pseudogene 6 Neighboring gene potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2-like Neighboring gene diphosphoinositol pentakisphosphate kinase 2 Neighboring gene gypsy retrotransposon integrase 1 Neighboring gene transfer RNA proline (anticodon AGG) 31

Genomic regions, transcripts, and products

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Go to nucleotide: Graphics FASTA GenBank

Expression

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  • Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
  • Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
  • BioProject: PRJNA238328
  • Publication: PMID 24510058
  • Analysis date: Mon Jun 6 17:44:12 2016

Bibliography

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Related articles in PubMed

  1. Multiple roles for peptidylglycine α-amidating monooxygenase in the response to hypoxia. Rao VKS, et al. J Cell Physiol, 2021 Nov. PMID 34061983
  2. A histidine-rich linker region in peptidylglycine α-amidating monooxygenase has the properties of a pH sensor. Vishwanatha K, et al. J Biol Chem, 2014 May 2. PMID 24627494, Free PMC Article
  3. Coordination of peroxide to the Cu(M) center of peptidylglycine α-hydroxylating monooxygenase (PHM): structural and computational study. Rudzka K, et al. J Biol Inorg Chem, 2013 Feb. PMID 23247335, Free PMC Article
  4. Dynamics of peptidergic secretory granule transport are regulated by neuronal stimulation. Sobota JA, et al. BMC Neurosci, 2010 Mar 4. PMID 20202202, Free PMC Article
  5. Amidation of bioactive peptides: the structure of the lyase domain of the amidating enzyme. Chufán EE, et al. Structure, 2009 Jul 15. PMID 19604476, Free PMC Article

See all (65) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Multiple roles for peptidylglycine alpha-amidating monooxygenase in the response to hypoxia.
    Title: Multiple roles for peptidylglycine α-amidating monooxygenase in the response to hypoxia.
  2. Disruption of AP-1-dependent late endosomal trafficking diminishes the ability of PAM to retain copper and produce amidated peptides.
    Title: Adaptor Protein-1 Complex Affects the Endocytic Trafficking and Function of Peptidylglycine α-Amidating Monooxygenase, a Luminal Cuproenzyme.
  3. Data indicate that H3A mutation eliminates the ability of internalized peptidylglycine alpha-amidating monooxygenase PAM-1 to return to secretory granules.
    Title: A histidine-rich linker region in peptidylglycine α-amidating monooxygenase has the properties of a pH sensor.
  4. The crystal structure of the oxidized form of PHM complexed with hydrogen peroxide.
    Title: Coordination of peroxide to the Cu(M) center of peptidylglycine α-hydroxylating monooxygenase (PHM): structural and computational study.
  5. Intermittent hypoxia activates peptidylglycine alpha-amidating monooxygenase in rat brain stem via reactive oxygen species-mediated proteolytic processing.
    Title: Intermittent hypoxia activates peptidylglycine alpha-amidating monooxygenase in rat brain stem via reactive oxygen species-mediated proteolytic processing.
  6. Recruitment of PAM-1 to secretory vesicles depends on intact N-terminal proANP and on the lumenal domain of PAM-1. Conversely, PAM-1 participates in shaping the proANP-secretory vesicles.
    Title: Peptidyl-glycine alpha-amidating monooxygenase targeting and shaping of atrial secretory vesicles: inhibition by mutated N-terminal ProANP and PBA.
  7. expression analysis of PHM in rats and in mouse cells
    Title: Murine atrial HL-1 cells express highly active peptidylglycine alpha-amidating enzyme.
  8. Data show that ubiquitin is a peptidylglycine alpha-amidating monooxygenase substrate with a (V/K)(amidation) that is similar to other known peptide substrates.
    Title: Ubiquitin and ubiquitin-derived peptides as substrates for peptidylglycine alpha-amidating monooxygenase.
  9. PAM activity was lower in cardiac atria of Cu- rats than Cu-adequate (Cu+) rats
    Title: Peptidylglycine-alpha-amidating monooxygenase activity and protein are lower in copper-deficient rats and suckling copper-deficient mice.
  10. the structure of the ternary complex of the peptidylglycine-alphahydroxylating monooxygenase (PHM) domain of PAM with molecular oxygen and a peptide that contains a D-amino acid designed to trap the precatalytic complex is presented
    Title: Dioxygen binds end-on to mononuclear copper in a precatalytic enzyme complex.
Submit: New GeneRIF Correction See all GeneRIFs (12)

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Markers

Homology

Gene Ontology Provided by RGD

Function Evidence Code Pubs
enables L-ascorbic acid binding IEA
Inferred from Electronic Annotation
more info
  
enables calcium ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables chromatin binding ISO
Inferred from Sequence Orthology
more info
  
enables copper ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables copper ion binding IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables lyase activity IEA
Inferred from Electronic Annotation
more info
  
enables peptidylamidoglycolate lyase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables peptidylamidoglycolate lyase activity IEA
Inferred from Electronic Annotation
more info
  
enables peptidylamidoglycolate lyase activity ISO
Inferred from Sequence Orthology
more info
  
enables peptidylglycine monooxygenase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables peptidylglycine monooxygenase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables peptidylglycine monooxygenase activity IEA
Inferred from Electronic Annotation
more info
  
enables peptidylglycine monooxygenase activity ISO
Inferred from Sequence Orthology
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein kinase binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables zinc ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables zinc ion binding IEA
Inferred from Electronic Annotation
more info
  
enables zinc ion binding ISO
Inferred from Sequence Orthology
more info
  
Process Evidence Code Pubs
involved_in fatty acid primary amide biosynthetic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in heart development IEP
Inferred from Expression Pattern
more info
 PubMed 
involved_in lactation IEP
Inferred from Expression Pattern
more info
 PubMed 
involved_in limb development IEP
Inferred from Expression Pattern
more info
 PubMed 
involved_in long-chain fatty acid metabolic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in maternal process involved in female pregnancy IEP
Inferred from Expression Pattern
more info
 PubMed 
acts_upstream_of_or_within mitotic chromosome condensation ISO
Inferred from Sequence Orthology
more info
  
involved_in ovulation cycle process IEP
Inferred from Expression Pattern
more info
 PubMed 
involved_in peptide amidation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in peptide amidation IEA
Inferred from Electronic Annotation
more info
  
involved_in peptide amidation ISO
Inferred from Sequence Orthology
more info
  
involved_in peptide metabolic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in peptide metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in regulation of actin cytoskeleton organization IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in regulation of transcription by RNA polymerase II IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in response to copper ion IEP
Inferred from Expression Pattern
more info
 PubMed 
involved_in response to estradiol IEP
Inferred from Expression Pattern
more info
 PubMed 
involved_in response to glucocorticoid IEP
Inferred from Expression Pattern
more info
 PubMed 
involved_in response to hypoxia IEP
Inferred from Expression Pattern
more info
 PubMed 
involved_in response to pH IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in response to xenobiotic stimulus IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in response to zinc ion IEA
Inferred from Electronic Annotation
more info
  
involved_in response to zinc ion ISO
Inferred from Sequence Orthology
more info
  
involved_in toxin metabolic process IDA
Inferred from Direct Assay
more info
 PubMed 
Component Evidence Code Pubs
located_in cell surface IDA
Inferred from Direct Assay
more info
 PubMed 
part_of chromatin ISO
Inferred from Sequence Orthology
more info
  
located_in condensed chromosome ISO
Inferred from Sequence Orthology
more info
  
is_active_in extracellular region IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in extracellular space IDA
Inferred from Direct Assay
more info
 PubMed 
located_in neuronal cell body IDA
Inferred from Direct Assay
more info
 PubMed 
located_in perikaryon IDA
Inferred from Direct Assay
more info
 PubMed 
located_in perinuclear region of cytoplasm IDA
Inferred from Direct Assay
more info
 PubMed 
located_in secretory granule IDA
Inferred from Direct Assay
more info
 PubMed 
located_in trans-Golgi network IDA
Inferred from Direct Assay
more info
 PubMed 
located_in transport vesicle membrane IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
peptidylglycine alpha-amidating monooxygenase
Names
basic salivary proline-rich protein 4-like
peptidyl-glycine alpha-amidating monooxygenase
NP_037132.2
XP_006245656.1
XP_006245659.1
XP_008765582.1
XP_017451775.1
XP_017451776.1
XP_038938966.1
XP_038938967.1
XP_038938968.1
XP_038938969.1
XP_038938970.1
XP_038938971.1
XP_038938972.1
XP_038938973.1
XP_038938974.1
XP_038938975.1
XP_038938976.1
XP_038938977.1
XP_063122753.1
XP_063122754.1
XP_063122755.1
XP_063122756.1
XP_063122757.1
XP_063122758.1
XP_063122759.1
XP_063122760.1
XP_063122761.1
XP_063122762.1
XP_063122763.1
XP_063122764.1
XP_063122765.1

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_013000.3 → NP_037132.2  peptidylglycine alpha-amidating monooxygenase precursor

    See identical proteins and their annotated locations for NP_037132.2

    Status: PROVISIONAL

    Source sequence(s)
    JAXUCZ010000009
    UniProtKB/Swiss-Prot
    P14925, P70710, Q64616, Q64668
    UniProtKB/TrEMBL
    A0A8L2QMN5, A6JR60
    Related
    ENSRNOP00000046774.5, ENSRNOT00000043451.6
    Conserved Domains (3) summary
    cd14958
    Location:503 → 810
    NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)
    pfam01082
    Location:64 → 173
    Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain
    pfam03712
    Location:201 → 347
    Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain

RefSeqs of Annotated Genomes: GCF_036323735.1-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCr8

Genomic

  1. NC_086027.1 Reference GRCr8

    Range
    105445812..105719287
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_039083040.2 → XP_038938968.1  peptidylglycine alpha-amidating monooxygenase isoform X2

    UniProtKB/Swiss-Prot
    P14925, P70710, Q64616, Q64668
    UniProtKB/TrEMBL
    A0A8L2QMN5, A6JR60
    Conserved Domains (3) summary
    cd14958
    Location:503 → 810
    NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)
    pfam01082
    Location:64 → 173
    Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain
    pfam03712
    Location:201 → 347
    Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain

  2. XM_063266691.1 → XP_063122761.1  peptidylglycine alpha-amidating monooxygenase isoform X13

    UniProtKB/TrEMBL
    A6JR72

  3. XM_039083046.2 → XP_038938974.1  peptidylglycine alpha-amidating monooxygenase isoform X12

    UniProtKB/TrEMBL
    A0A8I5ZMR1
    Conserved Domains (3) summary
    cd14958
    Location:398 → 705
    NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)
    pfam01082
    Location:64 → 173
    Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain
    pfam03712
    Location:201 → 347
    Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain

  4. XM_039083038.2 → XP_038938966.1  peptidylglycine alpha-amidating monooxygenase isoform X1

    UniProtKB/TrEMBL
    A0A8L2QMN5
    Conserved Domains (3) summary
    cd14958
    Location:503 → 810
    NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)
    pfam01082
    Location:64 → 173
    Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain
    pfam03712
    Location:201 → 347
    Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain

  5. XM_063266686.1 → XP_063122756.1  peptidylglycine alpha-amidating monooxygenase isoform X2

    UniProtKB/Swiss-Prot
    P14925, P70710, Q64616, Q64668
    UniProtKB/TrEMBL
    A6JR60

  6. XM_063266687.1 → XP_063122757.1  peptidylglycine alpha-amidating monooxygenase isoform X9

  7. XM_063266690.1 → XP_063122760.1  peptidylglycine alpha-amidating monooxygenase isoform X11

  8. XM_063266694.1 → XP_063122764.1  peptidylglycine alpha-amidating monooxygenase isoform X15

  9. XM_063266695.1 → XP_063122765.1  peptidylglycine alpha-amidating monooxygenase isoform X16

  10. XM_063266688.1 → XP_063122758.1  peptidylglycine alpha-amidating monooxygenase isoform X10

    UniProtKB/TrEMBL
    A6JR70

  11. XM_039083044.2 → XP_038938972.1  peptidylglycine alpha-amidating monooxygenase isoform X10

    UniProtKB/TrEMBL
    A0A8I5ZMR1, A6JR70
    Related
    ENSRNOP00000079092.1
    Conserved Domains (3) summary
    cd14958
    Location:398 → 705
    NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)
    pfam01082
    Location:64 → 173
    Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain
    pfam03712
    Location:201 → 347
    Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain

  12. XM_039083049.2 → XP_038938977.1  peptidylglycine alpha-amidating monooxygenase isoform X16

    UniProtKB/TrEMBL
    A0A8I5ZMR1
    Related
    ENSRNOP00000087123.1
    Conserved Domains (3) summary
    cd14958
    Location:398 → 705
    NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)
    pfam01082
    Location:64 → 173
    Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain
    pfam03712
    Location:201 → 347
    Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain

  13. XM_063266693.1 → XP_063122763.1  peptidylglycine alpha-amidating monooxygenase isoform X14

  14. XM_039083047.2 → XP_038938975.1  peptidylglycine alpha-amidating monooxygenase isoform X13

    UniProtKB/TrEMBL
    A0A8I5ZMR1, A6JR72
    Related
    ENSRNOP00000053295.2
    Conserved Domains (3) summary
    cd14958
    Location:398 → 705
    NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)
    pfam01082
    Location:64 → 173
    Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain
    pfam03712
    Location:201 → 347
    Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain

  15. XM_017596286.3 → XP_017451775.1  peptidylglycine alpha-amidating monooxygenase isoform X1

    UniProtKB/TrEMBL
    A0A8L2QMN5
    Conserved Domains (3) summary
    cd14958
    Location:503 → 810
    NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)
    pfam01082
    Location:64 → 173
    Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain
    pfam03712
    Location:201 → 347
    Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain

  16. XM_039083041.2 → XP_038938969.1  peptidylglycine alpha-amidating monooxygenase isoform X5

    UniProtKB/TrEMBL
    A0A8L2QMN5, A6JR64
    Conserved Domains (3) summary
    cd14958
    Location:503 → 810
    NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)
    pfam01082
    Location:64 → 173
    Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain
    pfam03712
    Location:201 → 347
    Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain

  17. XM_017596287.3 → XP_017451776.1  peptidylglycine alpha-amidating monooxygenase isoform X3

    UniProtKB/TrEMBL
    A0A8L2QMN5

  18. XM_006245594.5 → XP_006245656.1  peptidylglycine alpha-amidating monooxygenase isoform X4

    UniProtKB/TrEMBL
    A0A8L2QMN5
    Conserved Domains (3) summary
    cd14958
    Location:503 → 810
    NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)
    pfam01082
    Location:64 → 173
    Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain
    pfam03712
    Location:201 → 347
    Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain

  19. XM_008767360.4 → XP_008765582.1  peptidylglycine alpha-amidating monooxygenase isoform X6

    UniProtKB/TrEMBL
    A0A8L2QMN5
    Conserved Domains (3) summary
    cd14958
    Location:503 → 810
    NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)
    pfam01082
    Location:64 → 173
    Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain
    pfam03712
    Location:201 → 347
    Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain

  20. XM_039083042.2 → XP_038938970.1  peptidylglycine alpha-amidating monooxygenase isoform X7

    UniProtKB/TrEMBL
    A0A8L2QMN5, A6JR66
    Conserved Domains (3) summary
    cd14958
    Location:503 → 810
    NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)
    pfam01082
    Location:64 → 173
    Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain
    pfam03712
    Location:201 → 347
    Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain

  21. XM_006245597.5 → XP_006245659.1  peptidylglycine alpha-amidating monooxygenase isoform X8

    UniProtKB/TrEMBL
    A0A8L2QMN5
    Conserved Domains (3) summary
    cd14958
    Location:503 → 810
    NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)
    pfam01082
    Location:64 → 173
    Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain
    pfam03712
    Location:201 → 347
    Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain

  22. XM_039083043.2 → XP_038938971.1  peptidylglycine alpha-amidating monooxygenase isoform X9

    UniProtKB/TrEMBL
    A0A8I5ZMR1
    Conserved Domains (3) summary
    cd14958
    Location:398 → 705
    NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)
    pfam01082
    Location:64 → 173
    Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain
    pfam03712
    Location:201 → 347
    Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain

  23. XM_039083045.2 → XP_038938973.1  peptidylglycine alpha-amidating monooxygenase isoform X11

    UniProtKB/TrEMBL
    A0A8I5ZMR1
    Conserved Domains (3) summary
    cd14958
    Location:398 → 705
    NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)
    pfam01082
    Location:64 → 173
    Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain
    pfam03712
    Location:201 → 347
    Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain

  24. XM_039083048.2 → XP_038938976.1  peptidylglycine alpha-amidating monooxygenase isoform X15

    UniProtKB/TrEMBL
    A0A8I5ZMR1
    Related
    ENSRNOP00000089015.1
    Conserved Domains (3) summary
    cd14958
    Location:398 → 705
    NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)
    pfam01082
    Location:64 → 173
    Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain
    pfam03712
    Location:201 → 347
    Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain

  25. XM_063266684.1 → XP_063122754.1  peptidylglycine alpha-amidating monooxygenase isoform X1

  26. XM_063266689.1 → XP_063122759.1  peptidylglycine alpha-amidating monooxygenase isoform X10

    UniProtKB/TrEMBL
    A6JR70

  27. XM_063266685.1 → XP_063122755.1  peptidylglycine alpha-amidating monooxygenase isoform X1

  28. XM_039083039.2 → XP_038938967.1  peptidylglycine alpha-amidating monooxygenase isoform X1

    UniProtKB/TrEMBL
    A0A8L2QMN5
    Conserved Domains (3) summary
    cd14958
    Location:503 → 810
    NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)
    pfam01082
    Location:64 → 173
    Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain
    pfam03712
    Location:201 → 347
    Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain

  29. XM_063266692.1 → XP_063122762.1  peptidylglycine alpha-amidating monooxygenase isoform X13

    UniProtKB/TrEMBL
    A6JR72

  30. XM_063266683.1 → XP_063122753.1  peptidylglycine alpha-amidating monooxygenase isoform X1

Nucleotide Protein Strain
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P14925.1 GenPept UniProtKB/Swiss-Prot:P14925

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