Peptidyl-glycine alpha-amidating monooxygenase precursor

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Reviewed, UniProtKB/Swiss-Prot P97467 (AMD_MOUSE)

Last modified November 25, 2008. Version 74. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

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

Gene names

Name:

Pam

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length	979 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	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 By similarity.
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. Interacts with RASSF9 By similarity.
Subcellular location	Cytoplasmic vesicle › secretory vesicle membrane; Single-pass membrane proteinBy similarity. Note= Secretory granules.
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 5 NHL repeats.

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Ontologies

Keywords
Cellular component	Cytoplasmic vesicle Membrane
Domain	Repeat Signal Transmembrane
Ligand	Copper Metal-binding Vitamin C Zinc
Molecular function	Lyase Monooxygenase Oxidoreductase
PTM	Cleavage on pair of basic residues Glycoprotein Phosphoprotein
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW peptide metabolic process Traceable author statement. Source: MGI
Cellular component	cytoplasmic vesicle Inferred from electronic annotation. Source: UniProtKB-KW cytosol Traceable author statement. Source: MGI integral to plasma membrane Traceable author statement. Source: MGI
Molecular function	L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW copper ion binding Inferred from electronic annotation. Source: InterPro peptidylamidoglycolate lyase activity Inferred from electronic annotation. Source: EC peptidylglycine monooxygenase activity Traceable author statement. Source: MGI protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
Kalrn	P97924	1	EBI-1397216,EBI-1397166	From a different organism.
Uhmk1	Q63285	1	EBI-1397216,EBI-1397144	From a different organism.

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

By similarity

Propeptide

25 – 34

By similarity

PRO_0000006363

Chain

35 – 979

945

Peptidyl-glycine alpha-amidating monooxygenase

PRO_0000006364

Regions

Topological domain

35 – 869

835

Intragranular Potential

Transmembrane

870 – 893

Potential

Topological domain

894 – 979

Cytoplasmic Potential

Repeat

501 – 544

NHL 1

Repeat

570 – 611

NHL 2

Repeat

620 – 665

NHL 3

Repeat

673 – 717

NHL 4

Repeat

769 – 812

NHL 5

Region

1 – 497

497

Peptidylglycine alpha-hydroxylating monooxygenase By similarity

Region

498 – 823

326

Peptidyl-alpha-hydroxyglycine alpha-amidating lyase By similarity

Region

931 – 948

Interaction with RASSF9 By similarity

Sites

Metal binding

106

Copper A By similarity

Metal binding

107

Copper A By similarity

Metal binding

171

Copper A By similarity

Metal binding

241

Copper B By similarity

Metal binding

243

Copper B By similarity

Metal binding

313

Copper B By similarity

Amino acid modifications

Modified residue

924

Phosphoserine

Modified residue

925

Phosphoserine

Modified residue

962

Phosphoserine By similarity

Modified residue

964

Phosphoserine By similarity

Glycosylation

765

N-linked (GlcNAc...) Potential

Disulfide bond

46 ↔ 185

By similarity

Disulfide bond

80 ↔ 125

By similarity

Disulfide bond

113 ↔ 130

By similarity

Disulfide bond

226 ↔ 333

By similarity

Disulfide bond

292 ↔ 314

By similarity

Disulfide bond

634 ↔ 655

By similarity

Disulfide bond

702 ↔ 713

By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

P97467-1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 1F5BED76567A741A
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FASTA

979

109,048

        10         20         30         40         50         60 
MAGRARSRLL LLLGLLALQS SCLAFRSPLS VFKRFKETTR SFSNECLGTT RPITPIDSSD 

        70         80         90        100        110        120 
FTLDIRMPGV TPKESDTYFC MSMRLPVDEE AFVIDFKPRA SMDTVHHMLL FGCNMPSSTG 

       130        140        150        160        170        180 
SYWFCDEGTC TDKANILYAW ARNAPPTRLP KGVGFRVGGE TGSKYFVLQV HYGDISAFRD 

       190        200        210        220        230        240 
NHKDCSGVSL HLTRVPQPLI AGMYLMMSVN TVIPPGEKVV NSDISCHYKM YPMHVFAYRV 

       250        260        270        280        290        300 
HTHHLGKVVS GYRVRNGQWT LIGRQSPQLP QAFYPVEHPV DVAFGDILAA RCVFTGEGRT 

       310        320        330        340        350        360 
EATHIGGTSS DEMCNLYIMY YMEAKHAVSF MTCTQNVAPD MFRTIPEEAN IPIPVKSDMV 

       370        380        390        400        410        420 
MIHGHHKETE NKEKSALIQQ PKQGEEEAFE QGDFYSLLSK LLGEREDVVH VHKYNPTEKT 

       430        440        450        460        470        480 
ESGSDLVAEI ANVVQKKDLG RSDAREGAEH EEGGNAILVR DRIHKFHRLE STLRPAESRA 

       490        500        510        520        530        540 
LSFQQPGEGP WEPELAGDFH VEEALEWPGV YLLPGQVSGV ALDSKNNLVI FHRGDHVWDG 

       550        560        570        580        590        600 
NSFDSKFVYQ QRGLGPIEED TILVIDPNKA EILQSSGKNL FYLPHGLSID TDGNYWVTDV 

       610        620        630        640        650        660 
ALHQVFKLEP RSKEGPLLVL GRSMQPGSDQ NHFCQPTDVA VEPSTGAVFV SDGYCNSRIV 

       670        680        690        700        710        720 
QFSPSGKFIT QWGEESSGSS PKPGQFSVPH SLALVPHLNQ LCVADRENGR IQCFKTDTKE 

       730        740        750        760        770        780 
FVREIKHASF GRNVFAISYI PGFLFAVNGK PYFGDQEPVQ GFVMNFSSGE IIDVFKPVRK 

       790        800        810        820        830        840 
HFDMPHDIVA SEDGTVYIGD AHTNTVWKFT LTESRLEVEH RSVKKAGIEV PEIKEAEAVV 

       850        860        870        880        890        900 
EPKVKNKPTS SELQKMQEKK KLIKDPGSGV PVVLITTLLV IPVVVLLAIA MFIRWKKSRA 

       910        920        930        940        950        960 
FGDHDRKLES SSGRVLGRLR GKGSSGLNLG NFFASRKGYS RKGFDRVSTE GSDQEKDEDD 

       970 
GSESEEEYSR PLPTPAPSS

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-924 AND SER-925, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	U79523 mRNA. Translation: AAB38364.1.
RefSeq	NP_038654.2.
UniGene	Mm.441453 Mm.5121
3D structure databases
HSSP	HSSP built from PDB template 3PHM based on UniProtKB P14925.
SMR	P97467. Positions 44-355.
ModBase	Search...
Protein-protein interaction databases
IntAct	P97467.
PTM databases
PhosphoSite	P97467.
Genome annotation databases
Ensembl	ENSMUSG00000026335. Mus musculus. [Contig view]
GeneID	18484.
KEGG	mmu:18484.
Organism-specific databases
MGI	MGI:97475. Pam.
Phylogenomic databases
HOGENOM	P97467.
HOVERGEN	P97467.
Gene expression databases
ArrayExpress	P97467.
CleanEx	MM_PAM.
GermOnline	ENSMUSG00000026335. Mus musculus.
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. 1 hit. PS00085. CU2_MONOOXYGENASE_2. 1 hit. PS51125. NHL. 5 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	294198.
SOURCE	Search...

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Entry information

Entry name

AMD_MOUSE

Accession

Primary (citable) accession number: P97467

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 1, 1997
Last modified:	November 25, 2008
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents