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P97467

- AMD_MOUSE

UniProt

P97467 - AMD_MOUSE

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Protein

Peptidyl-glycine alpha-amidating monooxygenase

Gene
Pam
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

Peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O.
Peptidylamidoglycolate = peptidyl amide + glyoxylate.

Cofactori

Zinc; for the lyase reaction By similarity.
Binds 2 copper ions per subunit; For the monoxygenase reaction By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi106 – 1061Copper A By similarity
Metal bindingi107 – 1071Copper A By similarity
Metal bindingi171 – 1711Copper A By similarity
Metal bindingi241 – 2411Copper B By similarity
Metal bindingi243 – 2431Copper B By similarity
Metal bindingi313 – 3131Copper B By similarity

GO - Molecular functioni

  1. copper ion binding Source: InterPro
  2. L-ascorbic acid binding Source: UniProtKB-KW
  3. peptidylamidoglycolate lyase activity Source: UniProtKB-EC
  4. peptidylglycine monooxygenase activity Source: MGI

GO - Biological processi

  1. peptide metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Vitamin C, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-glycine alpha-amidating monooxygenase
Short name:
PAM
Including the following 2 domains:
Peptidylglycine alpha-hydroxylating monooxygenase (EC:1.14.17.3)
Short name:
PHM
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (EC:4.3.2.5)
Alternative name(s):
Peptidylamidoglycolate lyase
Short name:
PAL
Gene namesi
Name:Pam
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:97475. Pam.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini35 – 869835Intragranular Reviewed predictionAdd
BLAST
Transmembranei870 – 89324Helical; Reviewed predictionAdd
BLAST
Topological domaini894 – 97986Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. cytosol Source: MGI
  2. integral component of plasma membrane Source: MGI
  3. transport vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424 By similarityAdd
BLAST
Propeptidei25 – 3410 By similarityPRO_0000006363
Chaini35 – 979945Peptidyl-glycine alpha-amidating monooxygenasePRO_0000006364Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 185 By similarity
Disulfide bondi80 ↔ 125 By similarity
Disulfide bondi113 ↔ 130 By similarity
Disulfide bondi226 ↔ 333 By similarity
Disulfide bondi292 ↔ 314 By similarity
Disulfide bondi634 ↔ 655 By similarity
Disulfide bondi702 ↔ 713 By similarity
Glycosylationi765 – 7651N-linked (GlcNAc...) Reviewed prediction
Modified residuei935 – 9351Phosphoserine By similarity
Modified residuei948 – 9481Phosphoserine By similarity
Modified residuei949 – 9491Phosphothreonine By similarity
Modified residuei952 – 9521Phosphoserine; by UHMK1

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP97467.
PaxDbiP97467.
PRIDEiP97467.

PTM databases

PhosphoSiteiP97467.

Expressioni

Gene expression databases

ArrayExpressiP97467.
BgeeiP97467.
CleanExiMM_PAM.
GenevestigatoriP97467.

Interactioni

Subunit structurei

Monomer. Interacts with RASSF9 By similarity.

Protein-protein interaction databases

IntActiP97467. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliP97467.
SMRiP97467. Positions 44-355, 498-823.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati501 – 54444NHL 1Add
BLAST
Repeati570 – 61142NHL 2Add
BLAST
Repeati620 – 66546NHL 3Add
BLAST
Repeati673 – 71745NHL 4Add
BLAST
Repeati769 – 81244NHL 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 497497Peptidylglycine alpha-hydroxylating monooxygenase By similarityAdd
BLAST
Regioni498 – 823326Peptidyl-alpha-hydroxyglycine alpha-amidating lyase By similarityAdd
BLAST
Regioni931 – 94818Interaction with RASSF9 By similarityAdd
BLAST

Sequence similaritiesi

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.

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3391.
GeneTreeiENSGT00730000111058.
HOGENOMiHOG000293368.
HOVERGENiHBG004218.
InParanoidiP97467.
KOiK00504.
K18200.
OMAiTVHHMLL.
OrthoDBiEOG70ZZNT.
TreeFamiTF320698.

Family and domain databases

Gene3Di2.120.10.30. 2 hits.
2.60.120.230. 1 hit.
2.60.120.310. 1 hit.
InterProiIPR011042. 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]
PfamiPF01082. Cu2_monooxygen. 1 hit.
PF01436. NHL. 4 hits.
[Graphical view]
PRINTSiPR00790. PAMONOXGNASE.
SUPFAMiSSF49742. SSF49742. 2 hits.
PROSITEiPS00084. CU2_MONOOXYGENASE_1. 1 hit.
PS00085. CU2_MONOOXYGENASE_2. 1 hit.
PS51125. NHL. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P97467-1 [UniParc]FASTAAdd to Basket

« Hide

MAGRARSRLL LLLGLLALQS SCLAFRSPLS VFKRFKETTR SFSNECLGTT    50
RPITPIDSSD FTLDIRMPGV TPKESDTYFC MSMRLPVDEE AFVIDFKPRA 100
SMDTVHHMLL FGCNMPSSTG SYWFCDEGTC TDKANILYAW ARNAPPTRLP 150
KGVGFRVGGE TGSKYFVLQV HYGDISAFRD NHKDCSGVSL HLTRVPQPLI 200
AGMYLMMSVN TVIPPGEKVV NSDISCHYKM YPMHVFAYRV HTHHLGKVVS 250
GYRVRNGQWT LIGRQSPQLP QAFYPVEHPV DVAFGDILAA RCVFTGEGRT 300
EATHIGGTSS DEMCNLYIMY YMEAKHAVSF MTCTQNVAPD MFRTIPEEAN 350
IPIPVKSDMV MIHGHHKETE NKEKSALIQQ PKQGEEEAFE QGDFYSLLSK 400
LLGEREDVVH VHKYNPTEKT ESGSDLVAEI ANVVQKKDLG RSDAREGAEH 450
EEGGNAILVR DRIHKFHRLE STLRPAESRA LSFQQPGEGP WEPELAGDFH 500
VEEALEWPGV YLLPGQVSGV ALDSKNNLVI FHRGDHVWDG NSFDSKFVYQ 550
QRGLGPIEED TILVIDPNKA EILQSSGKNL FYLPHGLSID TDGNYWVTDV 600
ALHQVFKLEP RSKEGPLLVL GRSMQPGSDQ NHFCQPTDVA VEPSTGAVFV 650
SDGYCNSRIV QFSPSGKFIT QWGEESSGSS PKPGQFSVPH SLALVPHLNQ 700
LCVADRENGR IQCFKTDTKE FVREIKHASF GRNVFAISYI PGFLFAVNGK 750
PYFGDQEPVQ GFVMNFSSGE IIDVFKPVRK HFDMPHDIVA SEDGTVYIGD 800
AHTNTVWKFT LTESRLEVEH RSVKKAGIEV PEIKEAEAVV EPKVKNKPTS 850
SELQKMQEKK KLIKDPGSGV PVVLITTLLV IPVVVLLAIA MFIRWKKSRA 900
FGDHDRKLES SSGRVLGRLR GKGSSGLNLG NFFASRKGYS RKGFDRVSTE 950
GSDQEKDEDD GSESEEEYSA PLPTPAPSS 979
Length:979
Mass (Da):108,963
Last modified:July 27, 2011 - v2
Checksum:i1F4C7276567A741A
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti970 – 9701A → R in AAB38364. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U79523 mRNA. Translation: AAB38364.1.
AC102191 Genomic DNA. No translation available.
AC157923 Genomic DNA. No translation available.
RefSeqiNP_038654.2. NM_013626.3.
XP_006529307.1. XM_006529244.1.
UniGeneiMm.441453.
Mm.5121.

Genome annotation databases

EnsembliENSMUST00000058762; ENSMUSP00000057112; ENSMUSG00000026335.
GeneIDi18484.
KEGGimmu:18484.
UCSCiuc007cfp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U79523 mRNA. Translation: AAB38364.1 .
AC102191 Genomic DNA. No translation available.
AC157923 Genomic DNA. No translation available.
RefSeqi NP_038654.2. NM_013626.3.
XP_006529307.1. XM_006529244.1.
UniGenei Mm.441453.
Mm.5121.

3D structure databases

ProteinModelPortali P97467.
SMRi P97467. Positions 44-355, 498-823.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P97467. 2 interactions.

PTM databases

PhosphoSitei P97467.

Proteomic databases

MaxQBi P97467.
PaxDbi P97467.
PRIDEi P97467.

Protocols and materials databases

DNASUi 18484.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000058762 ; ENSMUSP00000057112 ; ENSMUSG00000026335 .
GeneIDi 18484.
KEGGi mmu:18484.
UCSCi uc007cfp.1. mouse.

Organism-specific databases

CTDi 5066.
MGIi MGI:97475. Pam.

Phylogenomic databases

eggNOGi COG3391.
GeneTreei ENSGT00730000111058.
HOGENOMi HOG000293368.
HOVERGENi HBG004218.
InParanoidi P97467.
KOi K00504.
K18200.
OMAi TVHHMLL.
OrthoDBi EOG70ZZNT.
TreeFami TF320698.

Miscellaneous databases

ChiTaRSi PAM. mouse.
NextBioi 294198.
PROi P97467.
SOURCEi Search...

Gene expression databases

ArrayExpressi P97467.
Bgeei P97467.
CleanExi MM_PAM.
Genevestigatori P97467.

Family and domain databases

Gene3Di 2.120.10.30. 2 hits.
2.60.120.230. 1 hit.
2.60.120.310. 1 hit.
InterProi 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 ]
Pfami PF01082. Cu2_monooxygen. 1 hit.
PF01436. NHL. 4 hits.
[Graphical view ]
PRINTSi PR00790. PAMONOXGNASE.
SUPFAMi SSF49742. SSF49742. 2 hits.
PROSITEi PS00084. CU2_MONOOXYGENASE_1. 1 hit.
PS00085. CU2_MONOOXYGENASE_2. 1 hit.
PS51125. NHL. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.

Entry informationi

Entry nameiAMD_MOUSE
AccessioniPrimary (citable) accession number: P97467
Secondary accession number(s): E9QL07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: June 11, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi