Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P08478 (AMD1_XENLA)

Last modified June 16, 2009. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Peptidyl-glycine alpha-amidating monooxygenase A
      Short name=PAM-A
Alternative name(s):
    Peptidyl-glycine alpha-amidating monooxygenase I
    Peptide C-terminal alpha-amidating enzyme I
      Short name=AE-I
Including the following 2 domains:
    1- Recommended name:
            Peptidylglycine alpha-hydroxylating monooxygenase A
                Short name=PHM-A
              EC=1.14.17.3
    2- Recommended name:
            Peptidyl-alpha-hydroxyglycine alpha-amidating lyase A
              EC=4.3.2.5
        Alternative name(s):
            Peptidylamidoglycolate lyase-A
              Short name=PAL-A
Gene names
Name: pam-A
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Hide | Top

Protein attributes

Sequence length935 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 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. Ref.2

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 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 4 NHL repeats.

Hide | Top

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P08478-1)

Also known as: AE-III;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P08478-2)

Also known as: AE-I;

The sequence of this isoform differs from the canonical sequence as follows:
     391-400: DVHLEEDTDW → GLITLGDSAV
     401-935: Missing.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3636 Potential
Chain37 – 935899Peptidyl-glycine alpha-amidating monooxygenase A
PRO_0000006367

Regions

Topological domain22 – 825804Intragranular Potential
Transmembrane826 – 84621 Potential
Topological domain847 – 93589Cytoplasmic Potential
Repeat463 – 50442NHL 1
Repeat512 – 55746NHL 2
Repeat565 – 60945NHL 3
Repeat662 – 70544NHL 4
Region1 – 390390Peptidylglycine alpha-hydroxylating monooxygenase By similarity
Region391 – 712322Peptidyl-alpha-hydroxyglycine alpha-amidating lyase By similarity

Sites

Metal binding1031Copper A By similarity
Metal binding1041Copper A By similarity
Metal binding1681Copper A By similarity
Metal binding2381Copper B By similarity
Metal binding2401Copper B By similarity
Metal binding3101Copper B By similarity

Amino acid modifications

Glycosylation6581N-linked (GlcNAc...) Potential
Glycosylation7391N-linked (GlcNAc...) Potential
Disulfide bond43 ↔ 182 By similarity
Disulfide bond77 ↔ 122 By similarity
Disulfide bond110 ↔ 127 By similarity
Disulfide bond223 ↔ 330 By similarity
Disulfide bond289 ↔ 311 By similarity
Disulfide bond526 ↔ 547 By similarity
Disulfide bond594 ↔ 605 By similarity

Natural variations

Alternative sequence391 – 40010DVHLEEDTDW → GLITLGDSAV in isoform 2.
VSP_020312
Alternative sequence401 – 935535Missing in isoform 2.
VSP_020313

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (AE-III) [UniParc].

Last modified September 5, 2006. Version 2.
Checksum: 0463D2E57338D5AD

FASTA935103,379
        10         20         30         40         50         60 
MASLSSSFLV LFLLFQNSCY CFRSPLSVFK RYEESTRSLS NDCLGTTRPV MSPGSSDYTL 

        70         80         90        100        110        120 
DIRMPGVTPT ESDTYLCKSY RLPVDDEAYV VDFRPHANMD TAHHMLLFGC NIPSSTDDYW 

       130        140        150        160        170        180 
DCSAGTCMDK SSIMYAWAKN APPTKLPEGV GFRVGGKSGS RYFVLQVHYG NVKAFQDKHK 

       190        200        210        220        230        240 
DCTGVTVRVT PEKQPQIAGI YLSMSVDTVI PPGEEAVNSD IACLYNRPTI HPFAYRVHTH 

       250        260        270        280        290        300 
QLGQVVSGFR VRHGKWSLIG RQSPQLPQAF YPVEHPVEIS PGDIIATRCL FTGKGRTSAT 

       310        320        330        340        350        360 
YIGGTSNDEM CNLYIMYYMD AAHATSYMTC VQTGEPKLFQ NIPEIANVPI PVSPDMMMMM 

       370        380        390        400        410        420 
GHGHHHTEAE PEKNTGLQQP KREEEEVLDQ DVHLEEDTDW PGVNLKVGQV SGLALDPKNN 

       430        440        450        460        470        480 
LAIFHRGDHV WDENSFDRNF VYQQRGIGPI QESTILVVDP SSSKVLKSTG KNLFFLPHGL 

       490        500        510        520        530        540 
TIDRDGNYWV TDVALHQVFK LGAGKETPLL VLGRAFQPGS DRKHFCQPTD VAVDPITGNF 

       550        560        570        580        590        600 
FVADGYCNSR IMQFSPNGMF IMQWGEETSS NVPRPGQFRI PHSLTMVPDQ GQLCVADREN 

       610        620        630        640        650        660 
GRIQCFHAET GNFVKQIKHQ EFGREVFAVS YAPGGVLYAV NGKPYYGYSA PVQGFMLNFS 

       670        680        690        700        710        720 
NGDILDTFIP ARKNFDMPHD IAAADDGTVY VGDAHANAVW KFSPSKAEHR SVKKAGIEVE 

       730        740        750        760        770        780 
EITETEIFET HIRSRPKTNE SVEKQTQEKQ QKQKNSAGVS TQEKQNVVQE INAGVPTQEK 

       790        800        810        820        830        840 
QNVVQESSAG VSTQEKQSVV QESSAGVSTQ EKQSVVQESS AGVSFVLIIT LLIIPIAVLI 

       850        860        870        880        890        900 
AIAIFIRWRK VRMYGGDIDH KSESSSVGIL GKLRGKGSGG LNLGTFFATH KGYSRKGFDR 

       910        920        930 
LSTEGSDQEK DDDDGSDSEE EYSAPPIPPA PVSSS

« Hide

Isoform 2 (AE-I).

Checksum: FE4E8FA261D1EA33
Show »

FASTA40044,457

Hide | Top

References

« Hide 'large scale' references
[1]"Cloning and sequence of cDNA encoding a peptide C-terminal alpha-amidating enzyme from Xenopus laevis."
Mizuno K., Ohsuye K., Wada Y., Fuchimura K., Tanaka S., Matsuo H.
Biochem. Biophys. Res. Commun. 148:546-552(1987) [PubMed: 3689360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE.
[2]"Purification and cDNA cloning of Xenopus laevis skin peptidylhydroxyglycine N-C lyase, catalyzing the second reaction of C-terminal alpha-amidation."
Iwasaki Y., Kawahara T., Shimoi H., Suzuki K., Ghisalba O., Kangawa K., Matsuo H., Nishikawa Y.
Eur. J. Biochem. 201:551-559(1991) [PubMed: 1935950] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, FUNCTION.
Tissue: Skin.
[3]NIH - Xenopus Gene Collection (XGC) project
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Embryo.

Hide | Top

Cross-references

Sequence databases

M18134 mRNA. Translation: AAA49640.1.
X62771 mRNA. Translation: CAA44615.1.
BC043987 mRNA. Translation: AAH43987.1.
PIRURXLA1. A29726.
S17855.
RefSeqNP_001079520.2.
UniGeneXl.417

3D structure databases

HSSPHSSP built from PDB template 1PHM based on UniProtKB P14925.
ModBaseSearch...

Genome annotation databases

GeneID379207.
KEGGxla:379207.

Organism-specific databases

XenbaseXB-FEAT-950934. pam.

Phylogenomic databases

HOVERGENP08478.

Enzyme and pathway databases

BRENDA1.14.17.3. 648.
4.3.2.5. 648.

Family and domain databases

InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR014784. Cu2_ascorb_mOase-like_C.
IPR014783. Cu2_ascorb_mOase_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. 4 hits.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameAMD1_XENLA
AccessionPrimary (citable) accession number: P08478
Secondary accession number(s): Q5D0B6, Q91697
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: September 5, 2006
Last modified: June 16, 2009
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectXenopus annotation project

Hide | Top

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents