Q01662 (AMPM1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	MAP1
Ordered Locus Names:	YLR244C
ORF Names:	L9672.12

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	387 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Removes the amino-terminal methionine from nascent proteins.
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. true cofactor in vivo. Ref.4
Miscellaneous	Present with 19600 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the peptidase M24A family.

Ontologies

Keywords
Ligand	Cobalt Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of gene expression Inferred from mutant phenotype. Source: SGD protein initiator methionine removal involved in protein maturation Inferred from mutant phenotype. Source: SGD proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosolic ribosome Inferred from direct assay. Source: SGD
Molecular function	mRNA binding Inferred from direct assay. Source: SGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloaminopeptidase activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 10	10			PRO_0000018596
	Chain	11 – 387	377	Methionine aminopeptidase 1		PRO_0000018597
Sites
	Metal binding	219	1	Cobalt 1 By similarity
	Metal binding	230	1	Cobalt 1 By similarity
	Metal binding	230	1	Cobalt 2 By similarity
	Metal binding	230	1	Zinc or cobalt 1 By similarity
	Metal binding	230	1	Zinc or cobalt 2 By similarity
	Metal binding	294	1	Cobalt 2 By similarity
	Metal binding	327	1	Cobalt 2 By similarity
	Metal binding	358	1	Cobalt 1 By similarity
	Metal binding	358	1	Cobalt 2 By similarity
	Metal binding	358	1	Zinc or cobalt 1 By similarity
	Metal binding	358	1	Zinc or cobalt 2 By similarity
	Binding site	202	1	Substrate By similarity
	Binding site	301	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q01662 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 4F0A30E9908B8A55	FASTA	387	43,373
	10 20 30 40 50 60 MSTATTTVTT SDQASHPTKI YCSGLQCGRE TSSQMKCPVC LKQGIVSIFC DTSCYENNYK 70 80 90 100 110 120 AHKALHNAKD GLEGAYDPFP KFKYSGKVKA SYPLTPRRYV PEDIPKPDWA ANGLPVSEQR 130 140 150 160 170 180 NDRLNNIPIY KKDQIKKIRK ACMLGREVLD IAAAHVRPGI TTDELDEIVH NETIKRGAYP 190 200 210 220 230 240 SPLNYYNFPK SLCTSVNEVI CHGVPDKTVL KEGDIVNLDV SLYYQGYHAD LNETYYVGEN 250 260 270 280 290 300 ISKEALNTTE TSRECLKLAI KMCKPGTTFQ ELGDHIEKHA TENKCSVVRT YCGHGVGEFF 310 320 330 340 350 360 HCSPNIPHYA KNRTPGVMKP GMVFTIEPMI NEGTWKDMTW PDDWTSTTQD GKLSAQFEHT 370 380 LLVTEHGVEI LTARNKKSPG GPRQRIK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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(1992) [PubMed: 1569059] [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(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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(1998) [PubMed: 9865965] [Abstract] Cited for: COFACTOR.
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M77092 mRNA. Translation: AAA75193.1. U20865 Genomic DNA. Translation: AAB67398.1. BK006945 Genomic DNA. Translation: DAA09558.1.
PIR	S59390.
RefSeq	NP_013345.1. NM_001182131.1.
3D structure databases
ProteinModelPortal	Q01662.
SMR	Q01662. Positions 82-378.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q01662. 2 interactions.
MINT	MINT-2786997.
STRING	Q01662.
Protein family/group databases
MEROPS	M24.001.
Proteomic databases
PeptideAtlas	Q01662.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR244C; YLR244C; YLR244C.
GeneID	850945.
KEGG	sce:YLR244C.
NMPDR	fig|4932.3.peg.4358.
Organism-specific databases
CYGD	YLR244c.
SGD	S000004234. MAP1.
Phylogenomic databases
eggNOG	fuNOG04170.
GeneTree	EFGT00050000005419.
HOGENOM	HBG299384.
OMA	IEPMISE.
OrthoDB	EOG4TQQJJ.
Gene expression databases
ArrayExpress	Q01662.
Genevestigator	Q01662.
GermOnline	YLR244C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001714. Pept_M24_MAP. IPR000994. Pept_M24_structural-domain. IPR002467. Pept_M24A_MAP1. [Graphical view]
Gene3D	G3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.
KO	K01265.
Pfam	PF00557. Peptidase_M24. 1 hit. [Graphical view]
PRINTS	PR00599. MAPEPTIDASE.
SUPFAM	SSF55920. Peptidase_M24_cat_core. 1 hit.
TIGRFAMs	TIGR00500. Met_pdase_I. 1 hit.
PROSITE	PS00680. MAP_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	967402.

Entry information

Entry name

AMPM1_YEAST

Accession

Primary (citable) accession number: Q01662
Secondary accession number(s): D6VYP2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	February 1, 1996
Last modified:	December 14, 2011
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program