Reviewed, UniProtKB/Swiss-Prot P83388 (AMDL_CAEEL)

Names and origin

Protein names

Recommended name:
    Probable peptidyl-glycine alpha-amidating monooxygenase T19B4.1
      Short name=PAM
Including the following 2 domains:
    1- Recommended name:
            Probable peptidylglycine alpha-hydroxylating monooxygenase
                Short name=PHM
              EC=1.14.17.3
    2- Recommended name:
            Probable peptidyl-alpha-hydroxyglycine alpha-amidating lyase
              EC=4.3.2.5
        Alternative name(s):
            Peptidylamidoglycolate lyase
              Short name=PAL

Gene names

ORF Names:

T19B4.1

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	663 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Probable bifunctional enzyme that catalyzes 2 sequencial 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.
Catalytic activity	Peptidylglycine + ascorbate + O(2) = peptidyl(2-hydroxyglycine) + dehydroascorbate + H(2)O. Peptidylamidoglycolate = peptidyl amide + glyoxylate.
Cofactor	Zinc; for the lyase reaction By similarity. Binds 2 copper ions per subunit; For the monoxygenase reaction By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	SecretedPotential.
Sequence similarities	In the C-terminal section; belongs to the peptidyl-alpha-hydroxyglycine alpha-amidating lyase family. In the N-terminal section; belongs to the copper type II ascorbate-dependent monooxygenase family. Contains 4 NHL repeats.

Ontologies

Keywords
Cellular component	Secreted
Domain	Repeat Signal
Ligand	Copper Metal-binding Zinc
Molecular function	Lyase Monooxygenase Oxidoreductase
PTM	Glycoprotein
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW peptide metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-KW membrane Inferred from electronic annotation. Source: InterPro
Molecular function	copper ion binding Inferred from electronic annotation. Source: InterPro peptidylamidoglycolate lyase activity Inferred from electronic annotation. Source: EC peptidylglycine monooxygenase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 663	642	Probable peptidyl-glycine alpha-amidating monooxygenase T19B4.1		PRO_0000248569
Regions
	Repeat	411 – 454	44	NHL 1
	Repeat	464 – 507	44	NHL 2
	Repeat	511 – 554	44	NHL 3
	Repeat	626 – 656	31	NHL 4
	Region	1 – 300	300	Peptidylglycine alpha-hydroxylating monooxygenase
	Region	301 – 663	363	Peptidyl-alpha-hydroxyglycine alpha-amidating lyase
Sites
	Metal binding	75	1	Copper A By similarity
	Metal binding	76	1	Copper A By similarity
	Metal binding	142	1	Copper A By similarity
	Metal binding	210	1	Copper B By similarity
	Metal binding	212	1	Copper B By similarity
	Metal binding	282	1	Copper B By similarity
Amino acid modifications
	Glycosylation	191	1	N-linked (GlcNAc...) Potential
	Glycosylation	269	1	N-linked (GlcNAc...) Potential
	Glycosylation	411	1	N-linked (GlcNAc...)
	Disulfide bond	82 ↔ 98		By similarity
	Disulfide bond	194 ↔ 305		By similarity
	Disulfide bond	261 ↔ 283		By similarity
	Disulfide bond	478 ↔ 497		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P83388-1 [UniParc]. Last modified December 6, 2005. Version 2. Checksum: 02D86AD68C1FFABE	FASTA	663	74,096
	10 20 30 40 50 60 MNDRISINLI YLVLTFCCVS AATVRTAKND DIQKFTIQMI GYSPQKTDDY VAVSIEATPG 70 80 90 100 110 120 YVVAFEPMAH ADRVHHMLLY GCTMPASEQG FWRGMETCGW GGGSYILYAW ARNAPNLVLP 130 140 150 160 170 180 KDVAFSVGHE QDGIKYFVLQ VHYAQPFAGE VHDFSGVTMH ISQKKPMNLA AVMLFVSGTP 190 200 210 220 230 240 IPPQLPAFQN NITCMFESST PIHPFAFRTH THAMGRLVSA FFKHDGHWTK IGKRNPQWPQ 250 260 270 280 290 300 LFEGIPSKLM IGSGDQMSAS CRFDSMDKNR TVNMGAMGVD EMCNFYMMFH YDAKLDNPYP 310 320 330 340 350 360 QGAICAKDYP SKMIDYPKDG FELLPSRPEL EHHAHQSKVP FGIVQEAIHE NLGGVKLGQV 370 380 390 400 410 420 AGLAFNNEQQ LLVFQRAGRV WDASTFDNYN ILLDKKPIAD PVILVISYSG NQTKLERKLG 430 440 450 460 470 480 GGQFYLPHGI YVDKDGFVYT TDVGSHTVAK WKIEGNELKN IWTSGELLMP GSDQHHYCKP 490 500 510 520 530 540 TGITRVEDQL YVTDGYCNSR VVVLDLNGKR IRQFGLPGED AGQFNLPHDI VSDSAGRLLV 550 560 570 580 590 600 TDRENGRVQH MTTQGHVIEE FKSTMFTNIY SAASHEDYVF MVPGRPIMGH ETEGIAVFVG 610 620 630 640 650 660 RSGTGLIEYA FGPTTKGKRE QMGPQFGQPH CLRVCPDGGH IFVGDIAEGK ARLWQFKIRH DQN

References

[1]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[2]	"Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins." Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J., Kasai K., Takahashi N., Isobe T. Nat. Biotechnol. 21:667-672(2003) [PubMed: 12754521] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-411, MASS SPECTROMETRY.
[3]	"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins." Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T. Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed: 17761667] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-411, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U80438 Genomic DNA. Translation: AAB37637.2.
PIR	T25895.
RefSeq	NP_491666.2.
UniGene	Cel.34918
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	T19B4.1. Caenorhabditis elegans. [Contig view]
GeneID	266833.
KEGG	cel:T19B4.1.
Organism-specific databases
WormBase	WBGene00020556. T19B4.1.
WormPep	T19B4.1. CE39282. [WorfDB]
Family and domain databases
InterPro	IPR011042. 6-blade_b-propeller_TolB-like. IPR014783. Cu2_ascorb_mOase_C. IPR014784. Cu2_ascorb_mOase_like_C. IPR000323. Cu2_ascorb_mOase_N. IPR001258. NHL_repeat. IPR013017. NHL_repeat_subgr. IPR000720. Pep_amidat_mOase. [Graphical view]
Gene3D	G3DSA:2.120.10.30. 6-blade_b-propeller_TolB-like. 1 hit. G3DSA:2.60.120.230. Cu2_ascorb_mOase_core. 1 hit. G3DSA:2.60.120.310. Cu2_ascorb_mOase_core. 1 hit.
Pfam	PF03712. Cu2_monoox_C. 1 hit. PF01082. Cu2_monooxygen. 1 hit. PF01436. NHL. 4 hits. [Graphical view]
PRINTS	PR00790. PAMONOXGNASE.
PROSITE	PS00084. CU2_MONOOXYGENASE_1. False negative. PS00085. CU2_MONOOXYGENASE_2. 1 hit. PS51125. NHL. 3 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	953204.

Entry information

Entry name

AMDL_CAEEL

Accession

Primary (citable) accession number: P83388
Secondary accession number(s): P91458

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	December 6, 2005
Last modified:	November 25, 2008
This is version 42 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project