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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).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 ABy similarity
Metal bindingi107 – 1071Copper ABy similarity
Metal bindingi171 – 1711Copper ABy similarity
Metal bindingi241 – 2411Copper BBy similarity
Metal bindingi243 – 2431Copper BBy similarity
Metal bindingi313 – 3131Copper BBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. central nervous system development Source: Ensembl
  2. heart development Source: Ensembl
  3. lactation Source: Ensembl
  4. limb development Source: Ensembl
  5. long-chain fatty acid metabolic process Source: Ensembl
  6. maternal process involved in female pregnancy Source: Ensembl
  7. odontogenesis Source: Ensembl
  8. ovulation cycle process Source: Ensembl
  9. peptide amidation Source: Ensembl
  10. peptide metabolic process Source: MGI
  11. protein amidation Source: Ensembl
  12. protein homooligomerization Source: Ensembl
  13. regulation of actin cytoskeleton organization Source: Ensembl
  14. regulation of protein secretion Source: Ensembl
  15. regulation of transcription from RNA polymerase II promoter Source: Ensembl
  16. response to copper ion Source: Ensembl
  17. response to drug Source: Ensembl
  18. response to estradiol Source: Ensembl
  19. response to glucocorticoid Source: Ensembl
  20. response to hypoxia Source: Ensembl
  21. response to pH Source: Ensembl
  22. toxin metabolic process Source: Ensembl
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

Cytoplasmic vesiclesecretory vesicle membrane By similarity; Single-pass membrane protein By similarity
Note: Secretory granules.

GO - Cellular componenti

  1. cell surface Source: Ensembl
  2. cytosol Source: MGI
  3. extracellular space Source: Ensembl
  4. extracellular vesicular exosome Source: Ensembl
  5. integral component of plasma membrane Source: MGI
  6. neuron projection Source: Ensembl
  7. perikaryon Source: Ensembl
  8. perinuclear region of cytoplasm Source: Ensembl
  9. secretory granule membrane Source: Ensembl
  10. trans-Golgi network Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 185By similarity
Disulfide bondi80 ↔ 125By similarity
Disulfide bondi113 ↔ 130By similarity
Disulfide bondi226 ↔ 333By similarity
Disulfide bondi292 ↔ 314By similarity
Disulfide bondi634 ↔ 655By similarity
Disulfide bondi702 ↔ 713By similarity
Glycosylationi765 – 7651N-linked (GlcNAc...)Sequence Analysis
Modified residuei935 – 9351PhosphoserineBy similarity
Modified residuei948 – 9481PhosphoserineBy similarity
Modified residuei949 – 9491PhosphothreonineBy 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

BgeeiP97467.
CleanExiMM_PAM.
ExpressionAtlasiP97467. baseline and differential.
GenevestigatoriP97467.

Interactioni

Subunit structurei

Monomer. Interacts with RASSF9 (By similarity).By similarity

Protein-protein interaction databases

IntActiP97467. 2 interactions.

Structurei

3D structure databases

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

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini35 – 869835IntragranularSequence AnalysisAdd
BLAST
Topological domaini894 – 97986CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei870 – 89324HelicalSequence AnalysisAdd
BLAST

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 monooxygenaseBy similarityAdd
BLAST
Regioni498 – 823326Peptidyl-alpha-hydroxyglycine alpha-amidating lyaseBy similarityAdd
BLAST
Regioni931 – 94818Interaction with RASSF9By similarityAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the peptidyl-alpha-hydroxyglycine alpha-amidating lyase family.Curated
In the N-terminal section; belongs to the copper type II ascorbate-dependent monooxygenase family.Curated
Contains 5 NHL repeats.PROSITE-ProRule annotation

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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGRARSRLL LLLGLLALQS SCLAFRSPLS VFKRFKETTR SFSNECLGTT
60 70 80 90 100
RPITPIDSSD FTLDIRMPGV TPKESDTYFC MSMRLPVDEE AFVIDFKPRA
110 120 130 140 150
SMDTVHHMLL FGCNMPSSTG SYWFCDEGTC TDKANILYAW ARNAPPTRLP
160 170 180 190 200
KGVGFRVGGE TGSKYFVLQV HYGDISAFRD NHKDCSGVSL HLTRVPQPLI
210 220 230 240 250
AGMYLMMSVN TVIPPGEKVV NSDISCHYKM YPMHVFAYRV HTHHLGKVVS
260 270 280 290 300
GYRVRNGQWT LIGRQSPQLP QAFYPVEHPV DVAFGDILAA RCVFTGEGRT
310 320 330 340 350
EATHIGGTSS DEMCNLYIMY YMEAKHAVSF MTCTQNVAPD MFRTIPEEAN
360 370 380 390 400
IPIPVKSDMV MIHGHHKETE NKEKSALIQQ PKQGEEEAFE QGDFYSLLSK
410 420 430 440 450
LLGEREDVVH VHKYNPTEKT ESGSDLVAEI ANVVQKKDLG RSDAREGAEH
460 470 480 490 500
EEGGNAILVR DRIHKFHRLE STLRPAESRA LSFQQPGEGP WEPELAGDFH
510 520 530 540 550
VEEALEWPGV YLLPGQVSGV ALDSKNNLVI FHRGDHVWDG NSFDSKFVYQ
560 570 580 590 600
QRGLGPIEED TILVIDPNKA EILQSSGKNL FYLPHGLSID TDGNYWVTDV
610 620 630 640 650
ALHQVFKLEP RSKEGPLLVL GRSMQPGSDQ NHFCQPTDVA VEPSTGAVFV
660 670 680 690 700
SDGYCNSRIV QFSPSGKFIT QWGEESSGSS PKPGQFSVPH SLALVPHLNQ
710 720 730 740 750
LCVADRENGR IQCFKTDTKE FVREIKHASF GRNVFAISYI PGFLFAVNGK
760 770 780 790 800
PYFGDQEPVQ GFVMNFSSGE IIDVFKPVRK HFDMPHDIVA SEDGTVYIGD
810 820 830 840 850
AHTNTVWKFT LTESRLEVEH RSVKKAGIEV PEIKEAEAVV EPKVKNKPTS
860 870 880 890 900
SELQKMQEKK KLIKDPGSGV PVVLITTLLV IPVVVLLAIA MFIRWKKSRA
910 920 930 940 950
FGDHDRKLES SSGRVLGRLR GKGSSGLNLG NFFASRKGYS RKGFDRVSTE
960 970
GSDQEKDEDD GSESEEEYSA PLPTPAPSS
Length:979
Mass (Da):108,963
Last modified:July 27, 2011 - v2
Checksum:i1F4C7276567A741A
GO

Experimental Info

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

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

Bgeei P97467.
CleanExi MM_PAM.
ExpressionAtlasi P97467. baseline and differential.
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: October 29, 2014
This is version 129 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