Q8BP48 (AMPM1_MOUSE) 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:

Metap1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	386 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Ligand	Cobalt Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular process Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 386	385	Methionine aminopeptidase 1		PRO_0000148968
Sites
	Metal binding	220	1	Cobalt 1 By similarity
	Metal binding	231	1	Cobalt 1 By similarity
	Metal binding	231	1	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
	Binding site	203	1	Substrate By similarity
	Binding site	301	1	Substrate By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	253	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8BP48 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: C768875645674B97	FASTA	386	43,221
	10 20 30 40 50 60 MAAVETRVCE TDGCSSEAKL QCPTCIKLGI QGSYFCSQEC FKGSWATHKL LHKKAKDEKA 70 80 90 100 110 120 KREVCSWTVE GDVNTDPWAG YRYTGKLRPH YPLMPTRPVP SYIQRPDYAD HPLGMSESEQ 130 140 150 160 170 180 ALKGTSQIKL LSSEDIEGMR LVCRLAREVL DIAAGMIKAG VTTEEIDHAV HLACIARNCY 190 200 210 220 230 240 PSPLNYYNFP KSCCTSVNEV ICHGIPDRRP LQEGDIVNVD ITLYRNGYHG DLNETFFVGD 250 260 270 280 290 300 VDEGARKLVQ TTYECLMQAI DAVKPGVRYR ELGNIIQKHA QANGFSVVRS YCGHGIHKLF 310 320 330 340 350 360 HTAPNVPHYA KNKAVGVMKS GHVFTIEPMI CEGGWQDETW PDGWTAVTRD GKRSAQFEHT 370 380 LLVTDTGCEI LTRRLDSSRP HFMSQF

References

[1]

"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK077694 mRNA. Translation: BAC36961.1.
IPI	IPI00272622.
RefSeq	NP_780433.1. NM_175224.4.
UniGene	Mm.26833.
3D structure databases
ProteinModelPortal	Q8BP48.
SMR	Q8BP48. Positions 81-384.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8BP48. 1 interaction.
STRING	Q8BP48.
Protein family/group databases
MEROPS	M24.001.
PTM databases
PhosphoSite	Q8BP48.
Proteomic databases
PRIDE	Q8BP48.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000029804; ENSMUSP00000029804; ENSMUSG00000005813.
GeneID	75624.
KEGG	mmu:75624.
NMPDR	fig|10090.3.peg.9069.
Organism-specific databases
CTD	23173.
MGI	MGI:1922874. Metap1.
Phylogenomic databases
HOGENOM	HBG299384.
HOVERGEN	HBG067178.
InParanoid	Q8BP48.
OMA	IEPMISE.
OrthoDB	EOG40S0FP.
PhylomeDB	Q8BP48.
Gene expression databases
ArrayExpress	Q8BP48.
Bgee	Q8BP48.
CleanEx	MM_METAP1.
Genevestigator	Q8BP48.
GermOnline	ENSMUSG00000005813. Mus musculus.
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	343556.
SOURCE	Search...

Entry information

Entry name

AMPM1_MOUSE

Accession

Primary (citable) accession number: Q8BP48

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2003
Last sequence update:	March 1, 2003
Last modified:	November 16, 2011
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program