Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot P97467 (AMD_MOUSE)

Last modified July 22, 2008. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Hide | Top

Protein attributes

Sequence length979 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

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.

Hide | Top

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KalrnP979241EBI-1397216,EBI-1397166From a different organism.
Uhmk1Q632851EBI-1397216,EBI-1397144From a different organism.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Signal peptide1 – 2424 By similarity
Propeptide25 – 3410 By similarity
Chain35 – 979945Peptidyl-glycine alpha-amidating monooxygenase

Regions

Topological domain35 – 869835Intragranular Potential
Transmembrane870 – 89324 Potential
Topological domain894 – 97986Cytoplasmic Potential
Repeat501 – 54444NHL 1
Repeat570 – 61142NHL 2
Repeat620 – 66546NHL 3
Repeat673 – 71745NHL 4
Repeat769 – 81244NHL 5
Region1 – 497497Peptidylglycine alpha-hydroxylating monooxygenase By similarity
Region498 – 823326Peptidyl-alpha-hydroxyglycine alpha-amidating lyase By similarity
Region931 – 94818Interaction with RASSF9 By similarity

Sites

Metal binding1061Copper A By similarity
Metal binding1071Copper A By similarity
Metal binding1711Copper A By similarity
Metal binding2411Copper B By similarity
Metal binding2431Copper B By similarity
Metal binding3131Copper B By similarity

Amino acid modifications

Modified residue9241Phosphoserine
Modified residue9251Phosphoserine
Modified residue9621Phosphoserine By similarity
Modified residue9641Phosphoserine By similarity
Glycosylation7651N-linked (GlcNAc...) Potential
Disulfide bond46 ↔ 185 By similarity
Disulfide bond80 ↔ 125 By similarity
Disulfide bond113 ↔ 130 By similarity
Disulfide bond226 ↔ 333 By similarity
Disulfide bond292 ↔ 314 By similarity
Disulfide bond634 ↔ 655 By similarity
Disulfide bond702 ↔ 713 By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P97467-1 [UniParc].

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

FASTA979109,048
        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

« Hide

Hide | Top

References

« Hide '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.

Hide | Top

Cross-references

Sequence databases

U79523 mRNA. Translation: AAB38364.1.
RefSeqNP_038654.2.
UniGeneMm.441453
Mm.5121

3D structure databases

HSSPHSSP built from PDB template 3PHM based on UniProtKB P14925.
SMRP97467. Positions 44-355.
ModBaseSearch...

Protein-protein interaction databases

IntActP97467.

PTM databases

PhosphoSiteP97467.

Genome annotation databases

EnsemblENSMUSG00000026335. Mus musculus. [Contig view]
GeneID18484.
KEGGmmu:18484.

Organism-specific databases

MGIMGI:97475. Pam.

Phylogenomic databases

HOGENOMP97467.
HOVERGENP97467.

Gene expression databases

ArrayExpressP97467.
CleanExMM_PAM.
GermOnlineENSMUSG00000026335. Mus musculus.

Family and domain databases

InterProIPR011042. 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]
Gene3DG3DSA: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.
PfamPF03712. Cu2_monoox_C. 1 hit.
PF01082. Cu2_monooxygen. 1 hit.
PF01436. NHL. 4 hits.
[Graphical view]
PRINTSPR00790. PAMONOXGNASE.
PROSITEPS00084. CU2_MONOOXYGENASE_1. 1 hit.
PS00085. CU2_MONOOXYGENASE_2. 1 hit.
PS51125. NHL. 5 hits.
[Graphical view]
ProDomP97467.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

SOURCESearch...
ProtoNetSearch...

Hide | Top

Entry information

Entry nameAMD_MOUSE
AccessionPrimary (citable) accession number: P97467
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: July 22, 2008
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

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 · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents