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P97467

- AMD_MOUSE

UniProt

P97467 - AMD_MOUSE

Protein

Peptidyl-glycine alpha-amidating monooxygenase

Gene

Pam

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity By similarity.By similarity

    Catalytic activityi

    Peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O.
    Peptidylamidoglycolate = peptidyl amide + glyoxylate.

    Cofactori

    Zinc; for the lyase reaction.By similarity
    Binds 2 copper ions per subunit; For the monoxygenase reaction.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi106 – 1061Copper ABy similarity
    Metal bindingi107 – 1071Copper ABy similarity
    Metal bindingi171 – 1711Copper ABy similarity
    Metal bindingi241 – 2411Copper BBy similarity
    Metal bindingi243 – 2431Copper BBy similarity
    Metal bindingi313 – 3131Copper BBy similarity

    GO - Molecular functioni

    1. copper ion binding Source: InterPro
    2. L-ascorbic acid binding Source: UniProtKB-KW
    3. peptidylamidoglycolate lyase activity Source: UniProtKB-EC
    4. peptidylglycine monooxygenase activity Source: MGI

    GO - Biological processi

    1. peptide metabolic process Source: MGI

    Keywords - Molecular functioni

    Lyase, Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    Copper, Metal-binding, Vitamin C, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-glycine alpha-amidating monooxygenase
    Short name:
    PAM
    Including the following 2 domains:
    Peptidylglycine alpha-hydroxylating monooxygenase (EC:1.14.17.3)
    Short name:
    PHM
    Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (EC:4.3.2.5)
    Alternative name(s):
    Peptidylamidoglycolate lyase
    Short name:
    PAL
    Gene namesi
    Name:Pam
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:97475. Pam.

    Subcellular locationi

    Cytoplasmic vesiclesecretory vesicle membrane By similarity; Single-pass membrane protein By similarity
    Note: Secretory granules.

    GO - Cellular componenti

    1. cytosol Source: MGI
    2. integral component of plasma membrane Source: MGI
    3. transport vesicle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424By similarityAdd
    BLAST
    Propeptidei25 – 3410By similarityPRO_0000006363
    Chaini35 – 979945Peptidyl-glycine alpha-amidating monooxygenasePRO_0000006364Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi46 ↔ 185By similarity
    Disulfide bondi80 ↔ 125By similarity
    Disulfide bondi113 ↔ 130By similarity
    Disulfide bondi226 ↔ 333By similarity
    Disulfide bondi292 ↔ 314By similarity
    Disulfide bondi634 ↔ 655By similarity
    Disulfide bondi702 ↔ 713By similarity
    Glycosylationi765 – 7651N-linked (GlcNAc...)Sequence Analysis
    Modified residuei935 – 9351PhosphoserineBy similarity
    Modified residuei948 – 9481PhosphoserineBy similarity
    Modified residuei949 – 9491PhosphothreonineBy similarity
    Modified residuei952 – 9521Phosphoserine; by UHMK1

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP97467.
    PaxDbiP97467.
    PRIDEiP97467.

    PTM databases

    PhosphoSiteiP97467.

    Expressioni

    Gene expression databases

    ArrayExpressiP97467.
    BgeeiP97467.
    CleanExiMM_PAM.
    GenevestigatoriP97467.

    Interactioni

    Subunit structurei

    Monomer. Interacts with RASSF9 By similarity.By similarity

    Protein-protein interaction databases

    IntActiP97467. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP97467.
    SMRiP97467. Positions 44-355, 498-823.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini35 – 869835IntragranularSequence AnalysisAdd
    BLAST
    Topological domaini894 – 97986CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei870 – 89324HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati501 – 54444NHL 1Add
    BLAST
    Repeati570 – 61142NHL 2Add
    BLAST
    Repeati620 – 66546NHL 3Add
    BLAST
    Repeati673 – 71745NHL 4Add
    BLAST
    Repeati769 – 81244NHL 5Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 497497Peptidylglycine alpha-hydroxylating monooxygenaseBy similarityAdd
    BLAST
    Regioni498 – 823326Peptidyl-alpha-hydroxyglycine alpha-amidating lyaseBy similarityAdd
    BLAST
    Regioni931 – 94818Interaction with RASSF9By similarityAdd
    BLAST

    Sequence similaritiesi

    In the C-terminal section; belongs to the peptidyl-alpha-hydroxyglycine alpha-amidating lyase family.Curated
    In the N-terminal section; belongs to the copper type II ascorbate-dependent monooxygenase family.Curated
    Contains 5 NHL repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG3391.
    GeneTreeiENSGT00730000111058.
    HOGENOMiHOG000293368.
    HOVERGENiHBG004218.
    InParanoidiP97467.
    KOiK00504.
    K18200.
    OMAiTVHHMLL.
    OrthoDBiEOG70ZZNT.
    TreeFamiTF320698.

    Family and domain databases

    Gene3Di2.120.10.30. 2 hits.
    2.60.120.230. 1 hit.
    2.60.120.310. 1 hit.
    InterProiIPR011042. 6-blade_b-propeller_TolB-like.
    IPR014784. Cu2_ascorb_mOase-like_C.
    IPR020611. Cu2_ascorb_mOase_CS-1.
    IPR014783. Cu2_ascorb_mOase_CS-2.
    IPR000323. Cu2_ascorb_mOase_N.
    IPR001258. NHL_repeat.
    IPR013017. NHL_repeat_subgr.
    IPR000720. Pep_amidat_mOase.
    IPR008977. PHM/PNGase_F_dom.
    [Graphical view]
    PfamiPF01082. Cu2_monooxygen. 1 hit.
    PF01436. NHL. 4 hits.
    [Graphical view]
    PRINTSiPR00790. PAMONOXGNASE.
    SUPFAMiSSF49742. SSF49742. 2 hits.
    PROSITEiPS00084. CU2_MONOOXYGENASE_1. 1 hit.
    PS00085. CU2_MONOOXYGENASE_2. 1 hit.
    PS51125. NHL. 5 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P97467-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGRARSRLL LLLGLLALQS SCLAFRSPLS VFKRFKETTR SFSNECLGTT    50
    RPITPIDSSD FTLDIRMPGV TPKESDTYFC MSMRLPVDEE AFVIDFKPRA 100
    SMDTVHHMLL FGCNMPSSTG SYWFCDEGTC TDKANILYAW ARNAPPTRLP 150
    KGVGFRVGGE TGSKYFVLQV HYGDISAFRD NHKDCSGVSL HLTRVPQPLI 200
    AGMYLMMSVN TVIPPGEKVV NSDISCHYKM YPMHVFAYRV HTHHLGKVVS 250
    GYRVRNGQWT LIGRQSPQLP QAFYPVEHPV DVAFGDILAA RCVFTGEGRT 300
    EATHIGGTSS DEMCNLYIMY YMEAKHAVSF MTCTQNVAPD MFRTIPEEAN 350
    IPIPVKSDMV MIHGHHKETE NKEKSALIQQ PKQGEEEAFE QGDFYSLLSK 400
    LLGEREDVVH VHKYNPTEKT ESGSDLVAEI ANVVQKKDLG RSDAREGAEH 450
    EEGGNAILVR DRIHKFHRLE STLRPAESRA LSFQQPGEGP WEPELAGDFH 500
    VEEALEWPGV YLLPGQVSGV ALDSKNNLVI FHRGDHVWDG NSFDSKFVYQ 550
    QRGLGPIEED TILVIDPNKA EILQSSGKNL FYLPHGLSID TDGNYWVTDV 600
    ALHQVFKLEP RSKEGPLLVL GRSMQPGSDQ NHFCQPTDVA VEPSTGAVFV 650
    SDGYCNSRIV QFSPSGKFIT QWGEESSGSS PKPGQFSVPH SLALVPHLNQ 700
    LCVADRENGR IQCFKTDTKE FVREIKHASF GRNVFAISYI PGFLFAVNGK 750
    PYFGDQEPVQ GFVMNFSSGE IIDVFKPVRK HFDMPHDIVA SEDGTVYIGD 800
    AHTNTVWKFT LTESRLEVEH RSVKKAGIEV PEIKEAEAVV EPKVKNKPTS 850
    SELQKMQEKK KLIKDPGSGV PVVLITTLLV IPVVVLLAIA MFIRWKKSRA 900
    FGDHDRKLES SSGRVLGRLR GKGSSGLNLG NFFASRKGYS RKGFDRVSTE 950
    GSDQEKDEDD GSESEEEYSA PLPTPAPSS 979
    Length:979
    Mass (Da):108,963
    Last modified:July 27, 2011 - v2
    Checksum:i1F4C7276567A741A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti970 – 9701A → R in AAB38364. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U79523 mRNA. Translation: AAB38364.1.
    AC102191 Genomic DNA. No translation available.
    AC157923 Genomic DNA. No translation available.
    RefSeqiNP_038654.2. NM_013626.3.
    XP_006529307.1. XM_006529244.1.
    UniGeneiMm.441453.
    Mm.5121.

    Genome annotation databases

    EnsembliENSMUST00000058762; ENSMUSP00000057112; ENSMUSG00000026335.
    GeneIDi18484.
    KEGGimmu:18484.
    UCSCiuc007cfp.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U79523 mRNA. Translation: AAB38364.1 .
    AC102191 Genomic DNA. No translation available.
    AC157923 Genomic DNA. No translation available.
    RefSeqi NP_038654.2. NM_013626.3.
    XP_006529307.1. XM_006529244.1.
    UniGenei Mm.441453.
    Mm.5121.

    3D structure databases

    ProteinModelPortali P97467.
    SMRi P97467. Positions 44-355, 498-823.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P97467. 2 interactions.

    PTM databases

    PhosphoSitei P97467.

    Proteomic databases

    MaxQBi P97467.
    PaxDbi P97467.
    PRIDEi P97467.

    Protocols and materials databases

    DNASUi 18484.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000058762 ; ENSMUSP00000057112 ; ENSMUSG00000026335 .
    GeneIDi 18484.
    KEGGi mmu:18484.
    UCSCi uc007cfp.1. mouse.

    Organism-specific databases

    CTDi 5066.
    MGIi MGI:97475. Pam.

    Phylogenomic databases

    eggNOGi COG3391.
    GeneTreei ENSGT00730000111058.
    HOGENOMi HOG000293368.
    HOVERGENi HBG004218.
    InParanoidi P97467.
    KOi K00504.
    K18200.
    OMAi TVHHMLL.
    OrthoDBi EOG70ZZNT.
    TreeFami TF320698.

    Miscellaneous databases

    ChiTaRSi PAM. mouse.
    NextBioi 294198.
    PROi P97467.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P97467.
    Bgeei P97467.
    CleanExi MM_PAM.
    Genevestigatori P97467.

    Family and domain databases

    Gene3Di 2.120.10.30. 2 hits.
    2.60.120.230. 1 hit.
    2.60.120.310. 1 hit.
    InterProi IPR011042. 6-blade_b-propeller_TolB-like.
    IPR014784. Cu2_ascorb_mOase-like_C.
    IPR020611. Cu2_ascorb_mOase_CS-1.
    IPR014783. Cu2_ascorb_mOase_CS-2.
    IPR000323. Cu2_ascorb_mOase_N.
    IPR001258. NHL_repeat.
    IPR013017. NHL_repeat_subgr.
    IPR000720. Pep_amidat_mOase.
    IPR008977. PHM/PNGase_F_dom.
    [Graphical view ]
    Pfami PF01082. Cu2_monooxygen. 1 hit.
    PF01436. NHL. 4 hits.
    [Graphical view ]
    PRINTSi PR00790. PAMONOXGNASE.
    SUPFAMi SSF49742. SSF49742. 2 hits.
    PROSITEi PS00084. CU2_MONOOXYGENASE_1. 1 hit.
    PS00085. CU2_MONOOXYGENASE_2. 1 hit.
    PS51125. NHL. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Jeong J.H., Baek S.J., Park D.H.
      Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.

    Entry informationi

    Entry nameiAMD_MOUSE
    AccessioniPrimary (citable) accession number: P97467
    Secondary accession number(s): E9QL07
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 128 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3