Peptidyl-glycine alpha-amidating monooxygenase precursor

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P97467 (AMD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 117. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Peptidyl-glycine alpha-amidating monooxygenase
Short name=PAM

Including the following 2 domains:

Peptidylglycine alpha-hydroxylating monooxygenase
Short name=PHM
EC=1.14.17.3
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) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

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

General annotation (Comments)

Function	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.
Catalytic activity	Peptidylglycine + ascorbate + O₂ = peptidyl(2-hydroxyglycine) + dehydroascorbate + H₂O. 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 protein By 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.

Ontologies

Keywords
Cellular component	Cytoplasmic vesicle Membrane
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Copper Metal-binding Vitamin C Zinc
Molecular function	Lyase Monooxygenase Oxidoreductase
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	peptide metabolic process Traceable author statement PubMed 10219055. Source: MGI
Cellular_component	cytosol Traceable author statement PubMed 10219055. Source: MGI integral to plasma membrane Traceable author statement PubMed 10219055. Source: MGI transport vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
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 PubMed 10219055. Source: MGI
Complete GO annotation...

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

Helical; 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 Ref.3

Modified residue

925

Phosphoserine Ref.3

Modified residue

935

Phosphoserine By similarity

Modified residue

948

Phosphoserine Ref.4

Modified residue

949

Phosphothreonine By similarity

Modified residue

952

Phosphoserine; by UHMK1 Ref.4

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

Experimental info

Sequence conflict

970

A → R in AAB38364. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P97467 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 1F4C7276567A741A
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FASTA

979

108,963

        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 
GSESEEEYSA PLPTPAPSS

« Hide

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]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-924 AND SER-925, MASS SPECTROMETRY. Tissue: Liver.
[4]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-948 AND SER-952, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U79523 mRNA. Translation: AAB38364.1. AC102191 Genomic DNA. No translation available. AC157923 Genomic DNA. No translation available.
IPI	IPI00323974.
RefSeq	NP_038654.2. NM_013626.3.
UniGene	Mm.441453. Mm.5121.
3D structure databases
ProteinModelPortal	P97467.
SMR	P97467. Positions 44-355, 498-823.
ModBase	Search...
Protein-protein interaction databases
IntAct	P97467. 2 interactions.
PTM databases
PhosphoSite	P97467.
Proteomic databases
PaxDb	P97467.
PRIDE	P97467.
Protocols and materials databases
DNASU	18484.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000058762; ENSMUSP00000057112; ENSMUSG00000026335.
GeneID	18484.
KEGG	mmu:18484.
UCSC	uc007cfo.1. mouse.
Organism-specific databases
CTD	5066.
MGI	MGI:97475. Pam.
Phylogenomic databases
eggNOG	COG3391.
GeneTree	ENSGT00530000063085.
HOGENOM	HOG000293368.
HOVERGEN	HBG004218.
InParanoid	P97467.
KO	K00504.
OMA	DTVHHML.
Gene expression databases
ArrayExpress	P97467.
Bgee	P97467.
CleanEx	MM_PAM.
Genevestigator	P97467.
GermOnline	ENSMUSG00000026335. Mus musculus.
Family and domain databases
Gene3D	2.120.10.30. 2 hits. 2.60.120.230. 1 hit. 2.60.120.310. 1 hit.
InterPro	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]
Pfam	PF01082. Cu2_monooxygen. 1 hit. PF01436. NHL. 4 hits. [Graphical view]
PRINTS	PR00790. PAMONOXGNASE.
SUPFAM	SSF49742. PHM_PNGase_F. 2 hits.
PROSITE	PS00084. CU2_MONOOXYGENASE_1. 1 hit. PS00085. CU2_MONOOXYGENASE_2. 1 hit. PS51125. NHL. 5 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PAM. mouse.
NextBio	294198.
SOURCE	Search...

Entry information

Entry name

AMD_MOUSE

Accession

Primary (citable) accession number: P97467
Secondary accession number(s): E9QL07

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents