AMDL_CAEEL
ID AMDL_CAEEL Reviewed; 663 AA.
AC P83388; P91458;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Probable peptidyl-glycine alpha-amidating monooxygenase pamn-1 {ECO:0000305};
DE Short=PAM;
DE Includes:
DE RecName: Full=Probable peptidylglycine alpha-hydroxylating monooxygenase;
DE Short=PHM;
DE EC=1.14.17.3;
DE Includes:
DE RecName: Full=Probable peptidyl-alpha-hydroxyglycine alpha-amidating lyase;
DE EC=4.3.2.5;
DE AltName: Full=Peptidylamidoglycolate lyase;
DE Short=PAL;
DE Flags: Precursor;
GN Name=pamn-1 {ECO:0000312|WormBase:T19B4.1};
GN ORFNames=T19B4.1 {ECO:0000312|WormBase:T19B4.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-411, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-411, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Probable bifunctional enzyme that catalyzes 2 sequential
CC steps in C-terminal alpha-amidation of peptides. The monooxygenase part
CC produces an unstable peptidyl(2-hydroxyglycine) intermediate that is
CC dismutated to glyoxylate and the corresponding desglycine peptide amide
CC by the lyase part. C-terminal amidation of peptides such as
CC neuropeptides is essential for full biological activity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a [peptide]-C-terminal glycine + 2 L-ascorbate + O2 = a
CC [peptide]-C-terminal (2S)-2-hydroxyglycine + H2O + 2 monodehydro-L-
CC ascorbate radical; Xref=Rhea:RHEA:21452, Rhea:RHEA-COMP:13486,
CC Rhea:RHEA-COMP:15321, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:59513, ChEBI:CHEBI:137000,
CC ChEBI:CHEBI:142768; EC=1.14.17.3;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a [peptide]-C-terminal (2S)-2-hydroxyglycine = a [peptide]-C-
CC terminal amide + glyoxylate; Xref=Rhea:RHEA:20924, Rhea:RHEA-
CC COMP:13485, Rhea:RHEA-COMP:15321, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:137001, ChEBI:CHEBI:142768; EC=4.3.2.5;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Zn(2+) is required for the lyase reaction. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250};
CC Note=Binds 2 copper ions per subunit for the monooxygenase reaction.
CC {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidyl-alpha-
CC hydroxyglycine alpha-amidating lyase family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the copper type II
CC ascorbate-dependent monooxygenase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FO080338; CCD62973.1; -; Genomic_DNA.
DR PIR; T25895; T25895.
DR RefSeq; NP_491666.2; NM_059265.5.
DR AlphaFoldDB; P83388; -.
DR SMR; P83388; -.
DR STRING; 6239.T19B4.1; -.
DR iPTMnet; P83388; -.
DR EPD; P83388; -.
DR PaxDb; P83388; -.
DR PeptideAtlas; P83388; -.
DR EnsemblMetazoa; T19B4.1.1; T19B4.1.1; WBGene00020556.
DR UCSC; T19B4.1; c. elegans.
DR WormBase; T19B4.1; CE39282; WBGene00020556; pamn-1.
DR eggNOG; KOG3567; Eukaryota.
DR HOGENOM; CLU_012293_1_0_1; -.
DR InParanoid; P83388; -.
DR OMA; KRNPQWP; -.
DR OrthoDB; 476471at2759; -.
DR PhylomeDB; P83388; -.
DR PRO; PR:P83388; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00020556; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004598; F:peptidylamidoglycolate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0004504; F:peptidylglycine monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006518; P:peptide metabolic process; IEA:InterPro.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 2.60.120.230; -; 1.
DR Gene3D; 2.60.120.310; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR014784; Cu2_ascorb_mOase-like_C.
DR InterPro; IPR014783; Cu2_ascorb_mOase_CS-2.
DR InterPro; IPR000323; Cu2_ascorb_mOase_N.
DR InterPro; IPR036939; Cu2_ascorb_mOase_N_sf.
DR InterPro; IPR024548; Cu2_monoox_C.
DR InterPro; IPR001258; NHL_repeat.
DR InterPro; IPR000720; PHM/PAL.
DR InterPro; IPR008977; PHM/PNGase_F_dom_sf.
DR Pfam; PF03712; Cu2_monoox_C; 1.
DR Pfam; PF01082; Cu2_monooxygen; 1.
DR Pfam; PF01436; NHL; 3.
DR PRINTS; PR00790; PAMONOXGNASE.
DR SUPFAM; SSF49742; SSF49742; 2.
DR PROSITE; PS00085; CU2_MONOOXYGENASE_2; 1.
DR PROSITE; PS51125; NHL; 3.
PE 1: Evidence at protein level;
KW Copper; Disulfide bond; Glycoprotein; Lyase; Metal-binding; Monooxygenase;
KW Multifunctional enzyme; Oxidoreductase; Reference proteome; Repeat;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..663
FT /note="Probable peptidyl-glycine alpha-amidating
FT monooxygenase pamn-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000248569"
FT REPEAT 411..454
FT /note="NHL 1"
FT REPEAT 464..507
FT /note="NHL 2"
FT REPEAT 511..554
FT /note="NHL 3"
FT REPEAT 626..656
FT /note="NHL 4"
FT REGION 1..300
FT /note="Peptidylglycine alpha-hydroxylating monooxygenase"
FT REGION 301..663
FT /note="Peptidyl-alpha-hydroxyglycine alpha-amidating lyase"
FT BINDING 75
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT DISULFID 82..98
FT /evidence="ECO:0000250"
FT DISULFID 194..305
FT /evidence="ECO:0000250"
FT DISULFID 261..283
FT /evidence="ECO:0000250"
FT DISULFID 478..497
FT /evidence="ECO:0000250"
SQ SEQUENCE 663 AA; 74096 MW; 02D86AD68C1FFABE CRC64;
MNDRISINLI YLVLTFCCVS AATVRTAKND DIQKFTIQMI GYSPQKTDDY VAVSIEATPG
YVVAFEPMAH ADRVHHMLLY GCTMPASEQG FWRGMETCGW GGGSYILYAW ARNAPNLVLP
KDVAFSVGHE QDGIKYFVLQ VHYAQPFAGE VHDFSGVTMH ISQKKPMNLA AVMLFVSGTP
IPPQLPAFQN NITCMFESST PIHPFAFRTH THAMGRLVSA FFKHDGHWTK IGKRNPQWPQ
LFEGIPSKLM IGSGDQMSAS CRFDSMDKNR TVNMGAMGVD EMCNFYMMFH YDAKLDNPYP
QGAICAKDYP SKMIDYPKDG FELLPSRPEL EHHAHQSKVP FGIVQEAIHE NLGGVKLGQV
AGLAFNNEQQ LLVFQRAGRV WDASTFDNYN ILLDKKPIAD PVILVISYSG NQTKLERKLG
GGQFYLPHGI YVDKDGFVYT TDVGSHTVAK WKIEGNELKN IWTSGELLMP GSDQHHYCKP
TGITRVEDQL YVTDGYCNSR VVVLDLNGKR IRQFGLPGED AGQFNLPHDI VSDSAGRLLV
TDRENGRVQH MTTQGHVIEE FKSTMFTNIY SAASHEDYVF MVPGRPIMGH ETEGIAVFVG
RSGTGLIEYA FGPTTKGKRE QMGPQFGQPH CLRVCPDGGH IFVGDIAEGK ARLWQFKIRH
DQN
