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Q5RBF3 (AMPM1_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 47. 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:
Methionine aminopeptidase 1

Short name=MAP 1
Short name=MetAP 1
EC=3.4.11.18
Alternative name(s):
Peptidase M 1
Gene names
Name:METAP1
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Removes the amino-terminal methionine from nascent proteins By similarity.

Catalytic activity

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.

Cofactor

Binds 2 cobalt ions per subunit. The true nature of the physiological cofactor is under debate. The enzyme is also active with zinc, manganese or divalent iron ions By similarity.

Binds 1 sodium ion per subunit. The sodium ion has a structural role By similarity.

Sequence similarities

Belongs to the peptidase M24A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 386385Methionine aminopeptidase 1
PRO_0000323735

Sites

Metal binding2201Cobalt 1 By similarity
Metal binding2311Cobalt 1 By similarity
Metal binding2311Cobalt 2 By similarity
Metal binding2941Cobalt 2 By similarity
Metal binding3271Cobalt 2 By similarity
Metal binding3581Cobalt 1 By similarity
Metal binding3581Cobalt 2 By similarity
Binding site2031Substrate By similarity
Binding site3011Substrate By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue2531Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RBF3 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: F1F31286745F3978

FASTA38643,229
        10         20         30         40         50         60 
MAAVETRVCE TDGCSSEAKL QCPTCIKLGI QGSYFCSQEC FKGSWATHKL LHKKAKDEKA 

        70         80         90        100        110        120 
KREVSSWTVE GDINTDPWAG YRYTGKLRPH YPLMPTRPVP SYIQRPDYAD HPLGMSESEQ 

       130        140        150        160        170        180 
ALKGTSQIKL LSSEDIEGMR LVCRLAREVL DIAAGMIKPG VTTEEIDHAV HLACIARNCY 

       190        200        210        220        230        240 
PSPLNYYNFP KSCCTSVNEV ICHGIPDRRP LQEGDIVNVD ITLYRNGYHG DLNETFFVGE 

       250        260        270        280        290        300 
VDDGARKLVQ TTYECLMQAI DAVKPGVRYR ELGNIIQKHA QANGFSVVRS YCGHGIHKLF 

       310        320        330        340        350        360 
HTAPNVPHYA KNKAVGVMKS GHVFTIEPMI CEGGWQDETW PDGWTAVTRD GKRSAQFEHT 

       370        380 
LLVTDTGCEI LTRRLDSARP HFMSQF 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR858696 mRNA. Translation: CAH90907.1.
RefSeqNP_001125517.1. NM_001132045.1.
UniGenePab.13560.

3D structure databases

HSSPHSSP built from PDB template 2B3H based on UniProtKB P53582.
ProteinModelPortalQ5RBF3.
SMRQ5RBF3. Positions 81-384.
ModBaseSearch...

Protein family/group databases

MEROPSM24.001.

Proteomic databases

PRIDEQ5RBF3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSPPYT00000017366; ENSPPYP00000016687; ENSPPYG00000014945.
GeneID100172428.
KEGGpon:100172428.

Organism-specific databases

CTD23173.

Phylogenomic databases

HOVERGENHBG067178.
InParanoidQ5RBF3.
OMAIEPMISE.
OrthoDBEOG40S0FP.

Family and domain databases

InterProIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]
Gene3DG3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.
KOK01265.
PfamPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSPR00599. MAPEPTIDASE.
SUPFAMSSF55920. Peptidase_M24_cat_core. 1 hit.
TIGRFAMsTIGR00500. Met_pdase_I. 1 hit.
PROSITEPS00680. MAP_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPM1_PONAB
AccessionPrimary (citable) accession number: Q5RBF3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: December 21, 2004
Last modified: November 16, 2011
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families