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P97467 (AMD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-glycine alpha-amidating monooxygenase

Short name=PAM

Including the following 2 domains:

  1. Peptidylglycine alpha-hydroxylating monooxygenase
    Short name=PHM
    EC=1.14.17.3
  2. 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) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 By similarity
Propeptide25 – 3410 By similarity
PRO_0000006363
Chain35 – 979945Peptidyl-glycine alpha-amidating monooxygenase
PRO_0000006364

Regions

Topological domain35 – 869835Intragranular Potential
Transmembrane870 – 89324Helical; 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 residue9351Phosphoserine By similarity
Modified residue9481Phosphoserine By similarity
Modified residue9491Phosphothreonine By similarity
Modified residue9521Phosphoserine; by UHMK1
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

Experimental info

Sequence conflict9701A → R in AAB38364. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P97467 [UniParc].

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

FASTA979108,963
        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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U79523 mRNA. Translation: AAB38364.1.
AC102191 Genomic DNA. No translation available.
AC157923 Genomic DNA. No translation available.
RefSeqNP_038654.2. NM_013626.3.
XP_006529307.1. XM_006529244.1.
UniGeneMm.441453.
Mm.5121.

3D structure databases

ProteinModelPortalP97467.
SMRP97467. Positions 44-355, 498-823.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP97467. 2 interactions.

PTM databases

PhosphoSiteP97467.

Proteomic databases

PaxDbP97467.
PRIDEP97467.

Protocols and materials databases

DNASU18484.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000058762; ENSMUSP00000057112; ENSMUSG00000026335.
GeneID18484.
KEGGmmu:18484.
UCSCuc007cfp.1. mouse.

Organism-specific databases

CTD5066.
MGIMGI:97475. Pam.

Phylogenomic databases

eggNOGCOG3391.
GeneTreeENSGT00730000111058.
HOGENOMHOG000293368.
HOVERGENHBG004218.
InParanoidP97467.
KOK00504.
OMATVHHMLL.
OrthoDBEOG70ZZNT.
TreeFamTF320698.

Gene expression databases

ArrayExpressP97467.
BgeeP97467.
CleanExMM_PAM.
GenevestigatorP97467.

Family and domain databases

Gene3D2.120.10.30. 2 hits.
2.60.120.230. 1 hit.
2.60.120.310. 1 hit.
InterProIPR011042. 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]
PfamPF01082. Cu2_monooxygen. 1 hit.
PF01436. NHL. 4 hits.
[Graphical view]
PRINTSPR00790. PAMONOXGNASE.
SUPFAMSSF49742. SSF49742. 2 hits.
PROSITEPS00084. CU2_MONOOXYGENASE_1. 1 hit.
PS00085. CU2_MONOOXYGENASE_2. 1 hit.
PS51125. NHL. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPAM. mouse.
NextBio294198.
PROP97467.
SOURCESearch...

Entry information

Entry nameAMD_MOUSE
AccessionPrimary (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: March 19, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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