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Protein

Peptidylglycine alpha-hydroxylating monooxygenase

Gene

Phm

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Monooxygenase that catalyzes an essential reaction in C-terminal alpha-amidation of peptides. Produces an unstable peptidyl(2-hydroxyglycine) intermediate. C-terminal amidation of peptides is required for normal developmental transitions and for biosynthesis of secretory peptides throughout the life.2 Publications

Catalytic activityi

Peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O.1 Publication

Cofactori

Cu2+1 PublicationNote: Binds 2 copper ions per subunit.1 Publication

Kineticsi

  1. KM=2.2 µM for alpha-N-acetyl-Tyr-Val-Gly1 Publication

    pH dependencei

    Optimum pH is 5.0.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi95 – 951Copper ABy similarity
    Metal bindingi96 – 961Copper ABy similarity
    Metal bindingi172 – 1721Copper ABy similarity
    Metal bindingi241 – 2411Copper BBy similarity
    Metal bindingi243 – 2431Copper BBy similarity
    Metal bindingi317 – 3171Copper BBy similarity

    GO - Molecular functioni

    GO - Biological processi

    • memory Source: FlyBase
    • multicellular organism reproduction Source: FlyBase
    • peptide amidation Source: FlyBase
    • regulation of imaginal disc-derived wing size Source: FlyBase
    • response to fungus Source: FlyBase
    Complete GO annotation...

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    Copper, Metal-binding

    Enzyme and pathway databases

    SignaLinkiO01404.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidylglycine alpha-hydroxylating monooxygenase (EC:1.14.17.3)
    Short name:
    dPHM
    Gene namesi
    Name:Phm
    ORF Names:CG3832
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    Proteomesi
    • UP000000803 Componenti: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0283509. Phm.

    Subcellular locationi

    GO - Cellular componenti

    • extracellular space Source: FlyBase
    • membrane Source: InterPro
    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Disruption phenotypei

    Death as late embryos with morphological defects that resemble those of animals with mutations in genes of the ecdysone-inducible regulatory circuit. Amidated peptides are largely absent but peptide precursors, a nonamidated neuropeptide, nonpeptide transmitters, and other peptide biosynthetic enzymes are detected.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence analysisAdd
    BLAST
    Chaini25 – 365341Peptidylglycine alpha-hydroxylating monooxygenasePRO_0000248571Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi69 ↔ 114By similarity
    Glycosylationi88 – 881N-linked (GlcNAc...)Sequence analysis
    Disulfide bondi102 ↔ 129By similarity
    Glycosylationi280 – 2801N-linked (GlcNAc...)Sequence analysis
    Disulfide bondi297 ↔ 318By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiO01404.

    Expressioni

    Tissue specificityi

    Expressed in the central nervous system (CNS) in a small number of CNS neurons (approximately a few hundred). Expression is present both in cell bodies and within neuropil regions. It is strongly expressed in neuroendocrine neurons (at protein level).1 Publication

    Inductioni

    Transcriptionally regulated by DIMM.1 Publication

    Gene expression databases

    BgeeiFBgn0019948.
    ExpressionAtlasiO01404. differential.
    GenevisibleiO01404. DM.

    Interactioni

    Protein-protein interaction databases

    BioGridi63409. 5 interactions.
    IntActiO01404. 2 interactions.
    MINTiMINT-312887.
    STRINGi7227.FBpp0072112.

    Structurei

    3D structure databases

    ProteinModelPortaliO01404.
    SMRiO01404. Positions 56-358.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiKOG3567. Eukaryota.
    ENOG410XS0X. LUCA.
    GeneTreeiENSGT00730000111058.
    InParanoidiO01404.
    KOiK00504.
    OMAiDTGLHNI.
    OrthoDBiEOG091G0DV8.
    PhylomeDBiO01404.

    Family and domain databases

    Gene3Di2.60.120.230. 1 hit.
    2.60.120.310. 1 hit.
    InterProiIPR014784. Cu2_ascorb_mOase-like_C.
    IPR014783. Cu2_ascorb_mOase_CS-2.
    IPR000323. Cu2_ascorb_mOase_N.
    IPR024548. Cu2_monoox_C.
    IPR000720. PHM/PAL.
    IPR008977. PHM/PNGase_F_dom.
    [Graphical view]
    PfamiPF03712. Cu2_monoox_C. 1 hit.
    PF01082. Cu2_monooxygen. 1 hit.
    [Graphical view]
    PRINTSiPR00790. PAMONOXGNASE.
    SUPFAMiSSF49742. SSF49742. 2 hits.
    PROSITEiPS00085. CU2_MONOOXYGENASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O01404-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPRISEIAAS VGLLLLIGVI SVDGLVKEGD YQNSLYQQNL ESNSATGATA
    60 70 80 90 100
    SFPFLMPNVS PQTPDLYLCT PIKVDPTTTY YIVGFNPNAT MNTAHHMLLY
    110 120 130 140 150
    GCGEPGTSKT TWNCGEMNRA SQEESASPCG PHSNSQIVYA WARDAQKLNL
    160 170 180 190 200
    PEGVGFKVGK NSPIKYLVLQ VHYAHIDKFK DGSTDDSGVF LDYTEEPRKK
    210 220 230 240 250
    LAGTLLLGTD GQIPAMKTEH LETACEVNEQ KVLHPFAYRV HTHGLGKVVS
    260 270 280 290 300
    GYRVRTNSDG EQEWLQLGKR DPLTPQMFYN TSNTDPIIEG DKIAVRCTMQ
    310 320 330 340 350
    STRHRTTKIG PTNEDEMCNF YLMYYVDHGE TLNMKFCFSQ GAPYYFWSNP
    360
    DSGLHNIPHI EASTL
    Length:365
    Mass (Da):40,564
    Last modified:November 1, 1998 - v2
    Checksum:i9368D9D92018C178
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF006663 mRNA. Translation: AAB61676.1.
    U77426 Genomic DNA. Translation: AAB52566.1.
    U77427 Genomic DNA. Translation: AAB52567.1.
    U77428 Genomic DNA. Translation: AAB52568.2.
    U77429 Genomic DNA. Translation: AAB52569.1.
    U77430 Genomic DNA. Translation: AAB52570.1.
    U77431 Genomic DNA. Translation: AAB52571.1.
    U77432 Genomic DNA. Translation: AAB52572.1.
    AE013599 Genomic DNA. Translation: AAF47127.1.
    AY069103 mRNA. Translation: AAL39248.1.
    RefSeqiNP_477225.1. NM_057877.4.
    NP_726394.1. NM_166644.2.
    UniGeneiDm.2282.

    Genome annotation databases

    EnsemblMetazoaiFBtr0072202; FBpp0072111; FBgn0019948.
    FBtr0072203; FBpp0072112; FBgn0019948.
    GeneIDi37823.
    KEGGidme:Dmel_CG3832.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF006663 mRNA. Translation: AAB61676.1.
    U77426 Genomic DNA. Translation: AAB52566.1.
    U77427 Genomic DNA. Translation: AAB52567.1.
    U77428 Genomic DNA. Translation: AAB52568.2.
    U77429 Genomic DNA. Translation: AAB52569.1.
    U77430 Genomic DNA. Translation: AAB52570.1.
    U77431 Genomic DNA. Translation: AAB52571.1.
    U77432 Genomic DNA. Translation: AAB52572.1.
    AE013599 Genomic DNA. Translation: AAF47127.1.
    AY069103 mRNA. Translation: AAL39248.1.
    RefSeqiNP_477225.1. NM_057877.4.
    NP_726394.1. NM_166644.2.
    UniGeneiDm.2282.

    3D structure databases

    ProteinModelPortaliO01404.
    SMRiO01404. Positions 56-358.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi63409. 5 interactions.
    IntActiO01404. 2 interactions.
    MINTiMINT-312887.
    STRINGi7227.FBpp0072112.

    Proteomic databases

    PaxDbiO01404.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblMetazoaiFBtr0072202; FBpp0072111; FBgn0019948.
    FBtr0072203; FBpp0072112; FBgn0019948.
    GeneIDi37823.
    KEGGidme:Dmel_CG3832.

    Organism-specific databases

    FlyBaseiFBgn0283509. Phm.

    Phylogenomic databases

    eggNOGiKOG3567. Eukaryota.
    ENOG410XS0X. LUCA.
    GeneTreeiENSGT00730000111058.
    InParanoidiO01404.
    KOiK00504.
    OMAiDTGLHNI.
    OrthoDBiEOG091G0DV8.
    PhylomeDBiO01404.

    Enzyme and pathway databases

    SignaLinkiO01404.

    Miscellaneous databases

    GenomeRNAii37823.
    PROiO01404.

    Gene expression databases

    BgeeiFBgn0019948.
    ExpressionAtlasiO01404. differential.
    GenevisibleiO01404. DM.

    Family and domain databases

    Gene3Di2.60.120.230. 1 hit.
    2.60.120.310. 1 hit.
    InterProiIPR014784. Cu2_ascorb_mOase-like_C.
    IPR014783. Cu2_ascorb_mOase_CS-2.
    IPR000323. Cu2_ascorb_mOase_N.
    IPR024548. Cu2_monoox_C.
    IPR000720. PHM/PAL.
    IPR008977. PHM/PNGase_F_dom.
    [Graphical view]
    PfamiPF03712. Cu2_monoox_C. 1 hit.
    PF01082. Cu2_monooxygen. 1 hit.
    [Graphical view]
    PRINTSiPR00790. PAMONOXGNASE.
    SUPFAMiSSF49742. SSF49742. 2 hits.
    PROSITEiPS00085. CU2_MONOOXYGENASE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPHM_DROME
    AccessioniPrimary (citable) accession number: O01404
    Secondary accession number(s): O01402
    , O01403, O01405, O01406, O01407, O01408, Q7JNH8, Q7JNH9, Q7JNI0, Q7JNI1, Q7JNI2, Q7JNI3, Q7JNI4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2006
    Last sequence update: November 1, 1998
    Last modified: September 7, 2016
    This is version 126 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.