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

    Gene ID: 25508, updated on 27-Nov-2024

    Summary

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    Symbol
    Pamprovided by RGD
    Full Name
    peptidylglycine alpha-amidating monooxygenaseprovided by RGD
    Primary source
    RGD:3252
    See related
    EnsemblRapid: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 fatty acid primary amide biosynthetic process; lactation; and peptide amidation. Located in several cellular components, including perikaryon; perinuclear region of cytoplasm; and trans-Golgi network. Biomarker of hypothyroidism. Orthologous to human PAM (peptidylglycine alpha-amidating monooxygenase). [provided by Alliance of Genome Resources, Nov 2024]
    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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    See Pam in Genome Data Viewer
    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. Regulation of peptide amidation in cultured pituitary cells. May V, et al. J Biol Chem, 1985 Dec 25. PMID 2999151
    2. Dioxygen binds end-on to mononuclear copper in a precatalytic enzyme complex. Prigge ST, et al. Science, 2004 May 7. PMID 15131304
    3. Isolation and functional expression of pituitary peptidylglycine alpha-amidating enzyme mRNA. A variant lacking the transmembrane domain. Kato I, et al. FEBS Lett, 1990 Sep 3. PMID 2401356
    4. Cloning, co-expression with an amidating enzyme, and activity of the scorpion toxin BmK ITa1 cDNA in insect cells. Liu Z, et al. Mol Biotechnol, 2003 May. PMID 12721493
    5. Supplying copper to the cuproenzyme peptidylglycine alpha-amidating monooxygenase. El Meskini R, et al. J Biol Chem, 2003 Apr 4. PMID 12529325

    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 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 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 
    located_in 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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    NEW Try the new Transcript table

    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
      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
      Related
      ENSRNOP00000046774.7, ENSRNOT00000043451.8
      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
      ENSRNOP00000079092.3, ENSRNOT00000102263.3
      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
      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
      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
      Related
      ENSRNOP00000098552.2, ENSRNOT00000120994.2
      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
      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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