Reviewed, UniProtKB/Swiss-Prot Q95XM2 (PHM_CAEEL)

Names and origin

Protein names

Recommended name:
    Probable peptidylglycine alpha-hydroxylating monooxygenase Y71G12B.4
      Short name=PHM
    EC=1.14.17.3

Gene names

ORF Names:

Y71G12B.4

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	324 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	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 such as neuropeptides is essential for full biological activity By similarity.
Catalytic activity	Peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O.
Cofactor	Binds 2 copper ions per subunit By similarity.
Subcellular location	Secreted Potential.
Sequence similarities	Belongs to the copper type II ascorbate-dependent monooxygenase family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Copper Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
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-SubCell membrane Inferred from electronic annotation. Source: InterPro
Molecular function	copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW peptidylglycine monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Chain	23 – 324	302	Probable peptidylglycine alpha-hydroxylating monooxygenase Y71G12B.4		PRO_0000248570
Sites
	Metal binding	66	1	Copper A By similarity
	Metal binding	67	1	Copper A By similarity
	Metal binding	142	1	Copper A By similarity
	Metal binding	207	1	Copper B By similarity
	Metal binding	209	1	Copper B By similarity
	Metal binding	284	1	Copper B By similarity
Amino acid modifications
	Glycosylation	182	1	N-linked (GlcNAc...) Ref.2 Ref.3
	Disulfide bond	41 ↔ 85		By similarity
	Disulfide bond	73 ↔ 101		By similarity
	Disulfide bond	264 ↔ 285		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q95XM2-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 46877A0A988B859E	FASTA	324	36,647
	10 20 30 40 50 60 MPRFYLLSSC ALLAFATSFC NAEKSQIRMP GVVPEADSYL CTSLELSDQE NYLTGFKALT 70 80 90 100 110 120 TKGTAHHILL FGCEEPGSDE LVWDCGEMNK PDDEMPRAPT CGSKPAILYA WALDAPPLEL 130 140 150 160 170 180 PQDVGFRVGG DSNIRHLVMQ VHYMHSKQEP DETGLEITHT EEPQPKLAAT MLLVTGGTLP 190 200 210 220 230 240 RNKTESFETA CMIEEDVVMH PFAYRTHTHR HGKEVSGWLV KEDQKHEDHW KLIGRRDPQL 250 260 270 280 290 300 AQMFVPVEDQ AMTIQQGDMV TARCILQNNE NRDISMGATE EDEMCNFYIM YWTDGEVMQD 310 320 NTCYSPGAPD YKWAREADLN HIPK

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-182, 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-182, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AC025726 Genomic DNA. Translation: AAK73930.1.
RefSeq	NP_490898.1.
UniGene	Cel.23148
3D structure databases
HSSP	HSSP built from PDB template 1PHM based on UniProtKB P14925.
ModBase	Search...
Genome annotation databases
Ensembl	Y71G12B.4; Y71G12B.4; Y71G12B.4; Caenorhabditis elegans. [Genome view]
GeneID	171746.
KEGG	cel:Y71G12B.4.
NMPDR	fig|6239.3.peg.283.
UCSC	Y71G12B.4. c. elegans.
Organism-specific databases
CTD	171746.
WormBase	WBGene00022144. Y71G12B.4.
WormPep	Y71G12B.4. CE26253. [WorfDB]
Phylogenomic databases
OMA	AYRTHTH.
Enzyme and pathway databases
BRENDA	1.14.17.3. 672.
Gene expression databases
ArrayExpress	Q95XM2.
Family and domain databases
InterPro	IPR014784. Cu2_ascorb_mOase-like_C. IPR014783. Cu2_ascorb_mOase_C. IPR000323. Cu2_ascorb_mOase_N. IPR000720. Pep_amidat_mOase. [Graphical view]
Gene3D	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. [Graphical view]
PRINTS	PR00790. PAMONOXGNASE.
PROSITE	PS00084. CU2_MONOOXYGENASE_1. False negative. PS00085. CU2_MONOOXYGENASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	872521.

Entry information

Entry name

PHM_CAEEL

Accession

Primary (citable) accession number: Q95XM2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	December 1, 2001
Last modified:	November 3, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project