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Protein

Methionine aminopeptidase 1

Gene

MAP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Plays the major role in N-terminal methionine removal. Less efficient when the second residue is Val.UniRule annotation4 Publications

Catalytic activityi

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

Cofactori

Co2+UniRule annotation, Zn2+UniRule annotation, Mn2+UniRule annotation, Fe2+UniRule annotationNote: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.UniRule annotation

Enzyme regulationi

In contract to the MetAP 2 isoform, is not inhibited by the fungal metabolite fumagillin, an antiangiogenic drug.1 Publication

Kineticsi

Kcat is 1173, 1416 and 507 (Min-1) with a Met-Ala-Ser, a Met-Gly-Met-Met and a Met-Ala-Ser-Trp peptide substrate, respectively.

  1. KM=2.68 mM for a Met-Ala-Ser peptide2 Publications
  2. KM=6.56 mM for a Met-Gly-Met-Met peptide2 Publications
  3. KM=139 µM for a Met-Ala-Ser-Trp peptide2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei202 – 2021SubstrateUniRule annotation
Metal bindingi219 – 2191Divalent metal cation 1UniRule annotation
Metal bindingi230 – 2301Divalent metal cation 1UniRule annotation
Metal bindingi230 – 2301Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi294 – 2941Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei301 – 3011SubstrateUniRule annotation
Metal bindingi327 – 3271Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi358 – 3581Divalent metal cation 1UniRule annotation
Metal bindingi358 – 3581Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-HAMAP
  2. metalloaminopeptidase activity Source: SGD
  3. mRNA binding Source: SGD

GO - Biological processi

  1. negative regulation of gene expression Source: SGD
  2. protein initiator methionine removal involved in protein maturation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:YLR244C-MONOMER.
ReactomeiREACT_288501. Inactivation, recovery and regulation of the phototransduction cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 1UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 1UniRule annotation
Short name:
MetAP 1UniRule annotation
Alternative name(s):
Peptidase M 1UniRule annotation
Gene namesi
Name:MAP1
Ordered Locus Names:YLR244C
ORF Names:L9672.12
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XII

Organism-specific databases

CYGDiYLR244c.
SGDiS000004234. MAP1.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic ribosome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221C → S: Changes the ribosome profile distribution of the protein and also increases its occurrence in the cytosolic fraction. 1 Publication
Mutagenesisi62 – 621H → R: Changes the ribosome profile distribution of the protein. 1 Publication
Mutagenesisi219 – 2191D → N: Reduces activity 1000-fold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Propeptidei2 – 1091 PublicationPRO_0000018596
Chaini11 – 387377Methionine aminopeptidase 1PRO_0000018597Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ01662.
PaxDbiQ01662.
PeptideAtlasiQ01662.

Expressioni

Gene expression databases

GenevestigatoriQ01662.

Interactioni

Subunit structurei

Associates with the 60S ribosomal subunit of the 80S translational complex.UniRule annotation1 Publication

Protein-protein interaction databases

BioGridi31511. 22 interactions.
IntActiQ01662. 2 interactions.
MINTiMINT-2786997.
STRINGi4932.YLR244C.

Structurei

3D structure databases

ProteinModelPortaliQ01662.
SMRiQ01662. Positions 62-379.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 6645Zinc finger-like; important for proper ribosome associationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0024.
GeneTreeiENSGT00390000002284.
HOGENOMiHOG000030427.
InParanoidiQ01662.
KOiK01265.
OMAiHAKKNGY.
OrthoDBiEOG78WM23.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 1 hit.
TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
PROSITEiPS00680. MAP_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q01662-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTATTTVTT SDQASHPTKI YCSGLQCGRE TSSQMKCPVC LKQGIVSIFC
60 70 80 90 100
DTSCYENNYK AHKALHNAKD GLEGAYDPFP KFKYSGKVKA SYPLTPRRYV
110 120 130 140 150
PEDIPKPDWA ANGLPVSEQR NDRLNNIPIY KKDQIKKIRK ACMLGREVLD
160 170 180 190 200
IAAAHVRPGI TTDELDEIVH NETIKRGAYP SPLNYYNFPK SLCTSVNEVI
210 220 230 240 250
CHGVPDKTVL KEGDIVNLDV SLYYQGYHAD LNETYYVGEN ISKEALNTTE
260 270 280 290 300
TSRECLKLAI KMCKPGTTFQ ELGDHIEKHA TENKCSVVRT YCGHGVGEFF
310 320 330 340 350
HCSPNIPHYA KNRTPGVMKP GMVFTIEPMI NEGTWKDMTW PDDWTSTTQD
360 370 380
GKLSAQFEHT LLVTEHGVEI LTARNKKSPG GPRQRIK
Length:387
Mass (Da):43,373
Last modified:February 1, 1996 - v2
Checksum:i4F0A30E9908B8A55
GO

Mass spectrometryi

Molecular mass is 43779 Da from positions 2 - 387. Determined by MALDI. The measured mass is that of a near-native protein after Factor Xa-catalyzed cleavage of a GST fusion, having a remnant Gly-Ile-Pro-Glu-Phe peptide before the native Ser-2.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77092 mRNA. Translation: AAA75193.1.
U20865 Genomic DNA. Translation: AAB67398.1.
BK006945 Genomic DNA. Translation: DAA09558.1.
PIRiS59390.
RefSeqiNP_013345.1. NM_001182131.1.

Genome annotation databases

EnsemblFungiiYLR244C; YLR244C; YLR244C.
GeneIDi850945.
KEGGisce:YLR244C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77092 mRNA. Translation: AAA75193.1.
U20865 Genomic DNA. Translation: AAB67398.1.
BK006945 Genomic DNA. Translation: DAA09558.1.
PIRiS59390.
RefSeqiNP_013345.1. NM_001182131.1.

3D structure databases

ProteinModelPortaliQ01662.
SMRiQ01662. Positions 62-379.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31511. 22 interactions.
IntActiQ01662. 2 interactions.
MINTiMINT-2786997.
STRINGi4932.YLR244C.

Chemistry

BindingDBiQ01662.
ChEMBLiCHEMBL2526.

Proteomic databases

MaxQBiQ01662.
PaxDbiQ01662.
PeptideAtlasiQ01662.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR244C; YLR244C; YLR244C.
GeneIDi850945.
KEGGisce:YLR244C.

Organism-specific databases

CYGDiYLR244c.
SGDiS000004234. MAP1.

Phylogenomic databases

eggNOGiCOG0024.
GeneTreeiENSGT00390000002284.
HOGENOMiHOG000030427.
InParanoidiQ01662.
KOiK01265.
OMAiHAKKNGY.
OrthoDBiEOG78WM23.

Enzyme and pathway databases

BioCyciYEAST:YLR244C-MONOMER.
ReactomeiREACT_288501. Inactivation, recovery and regulation of the phototransduction cascade.

Miscellaneous databases

NextBioi967402.
PROiQ01662.

Gene expression databases

GenevestigatoriQ01662.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 1 hit.
TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
PROSITEiPS00680. MAP_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, sequencing, deletion, and overexpression of a methionine aminopeptidase gene from Saccharomyces cerevisiae."
    Chang Y.-H., Teichert U., Smith J.A.
    J. Biol. Chem. 267:8007-8011(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 11-24.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Evidence that two zinc fingers in the methionine aminopeptidase from Saccharomyces cerevisiae are important for normal growth."
    Zuo S., Guo Q., Ling C., Chang Y.H.
    Mol. Gen. Genet. 246:247-253(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ZINC-BINDING, BIOPHYSICOCHEMICAL PROPERTIES.
  5. "A dominant negative mutation in Saccharomyces cerevisiae methionine aminopeptidase-1 affects catalysis and interferes with the function of methionine aminopeptidase-2."
    Klinkenberg M., Ling C., Chang Y.H.
    Arch. Biochem. Biophys. 347:193-200(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-219.
  6. "The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2."
    Sin N., Meng L., Wang M.Q., Wen J.J., Bornmann W.G., Crews C.M.
    Proc. Natl. Acad. Sci. U.S.A. 94:6099-6103(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  7. "Yeast methionine aminopeptidase I can utilize either Zn2+ or Co2+ as a cofactor: a case of mistaken identity?"
    Walker K.W., Bradshaw R.A.
    Protein Sci. 7:2684-2687(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR.
  8. "Yeast (Saccharomyces cerevisiae) methionine aminopeptidase I: rapid purification and improved activity assay."
    Walker K.W., Yi E., Bradshaw R.A.
    Biotechnol. Appl. Biochem. 29:157-163(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY.
  9. "The specificity in vivo of two distinct methionine aminopeptidases in Saccharomyces cerevisiae."
    Chen S., Vetro J.A., Chang Y.H.
    Arch. Biochem. Biophys. 398:87-93(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBSTRATE SPECIFICITY.
  10. "Yeast methionine aminopeptidase type 1 is ribosome-associated and requires its N-terminal zinc finger domain for normal function in vivo."
    Vetro J.A., Chang Y.H.
    J. Cell. Biochem. 85:678-688(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, MUTAGENESIS OF CYS-22 AND HIS-62.
  11. "N-terminal methionine removal and methionine metabolism in Saccharomyces cerevisiae."
    Dummitt B., Micka W.S., Chang Y.H.
    J. Cell. Biochem. 89:964-974(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMAP1_YEAST
AccessioniPrimary (citable) accession number: Q01662
Secondary accession number(s): D6VYP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1996
Last modified: April 1, 2015
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 19600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.