Methionine aminopeptidase 1D, mitochondrial precursor

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q6UB28 (AMP1D_HUMAN)

Last modified October 13, 2009. Version 47. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

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

Hide | Top

Names and origin

Protein names

Recommended name:
Methionine aminopeptidase 1D, mitochondrial
EC=3.4.11.18

Gene names

Name:

MAP1D

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length	335 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Function	Removes the amino-terminal methionine from nascent proteins By similarity. May play a role in colon tumorigenesis.
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.
Subcellular location	Mitochondrion. Ref.1
Tissue specificity	Overexpressed in colon cancer cell lines and colon tumors as compared to normal tissues (at protein level). Ref.2
Sequence similarities	Belongs to the peptidase M24A family.
Caution	It is uncertain whether Met-1 or a Met upstream of this sequence is the initiator.
Biophysicochemical properties	Kinetic parameters: K_M=573 µM for Met-pro-p-nitroanilide (at pH 8) pH dependence: Optimum pH is 7.5-8.0.

Hide | Top

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	Cobalt Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	N-terminal protein amino acid modification Ref.1 Traceable author statement. Source: HGNC peptidyl-methionine modification Ref.1 Traceable author statement. Source: HGNC proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Ref.1 Inferred from direct assay. Source: HGNC
Molecular function	aminopeptidase activity Ref.1 Traceable author statement. Source: UniProtKB cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activity Ref.1 Traceable author statement. Source: UniProtKB
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 19

Mitochondrion Potential

Chain

20 – 335

316

Methionine aminopeptidase 1D, mitochondrial

PRO_0000314126

Sites

Metal binding

178

Cobalt 1 By similarity

Metal binding

189

Cobalt 1 By similarity

Metal binding

189

Cobalt 2 By similarity

Metal binding

252

Cobalt 2 By similarity

Metal binding

284

Cobalt 2 By similarity

Metal binding

315

Cobalt 1 By similarity

Metal binding

315

Cobalt 2 By similarity

Binding site

161

Substrate By similarity

Binding site

259

Substrate By similarity

Natural variations

Natural variant

G → V: dbSNP rs10497377. Ref.2

VAR_050273

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q6UB28-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 2EB90946DC983D7B
Show »

FASTA

335

37,088

        10         20         30         40         50         60 
MAAPSGVHLL VRRGSHRIFS SPLNHIYLHK QSSSQQRRNF FFRRQRDISH SIVLPAAVSS 

        70         80         90        100        110        120 
AHPVPKHIKK PDYVTTGIVP DWGDSIEVKN EDQIQGLHQA CQLARHVLLL AGKSLKVDMT 

       130        140        150        160        170        180 
TEEIDALVHR EIISHNAYPS PLGYGGFPKS VCTSVNNVLC HGIPDSRPLQ DGDIINIDVT 

       190        200        210        220        230        240 
VYYNGYHGDT SETFLVGNVD ECGKKLVEVA RRCRDEAIAA CRAGAPFSVI GNTISHITHQ 

       250        260        270        280        290        300 
NGFQVCPHFV GHGIGSYFHG HPEIWHHAND SDLPMEEGMA FTIEPIITEG SPEFKVLEDA 

       310        320        330 
WTVVSLDNQR SAQFEHTVLI TSRGAQILTK LPHEA

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"An unusual peptide deformylase features in the human mitochondrial N-terminal methionine excision pathway." Serero A., Giglione C., Sardini A., Martinez-Sanz J., Meinnel T. J. Biol. Chem. 278:52953-52963(2003) [PubMed: 14532271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
[2]	"MAP1D, a novel methionine aminopeptidase family member is overexpressed in colon cancer." Leszczyniecka M., Bhatia U., Cueto M., Nirmala N.R., Towbin H., Vattay A., Wang B., Zabludoff S., Phillips P.E. Oncogene 25:3471-3478(2006) [PubMed: 16568094] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANT VAL-14.
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	"Kinetic and mutational studies of the number of interacting divalent cations required by bacterial and human methionine aminopeptidases." Hu X.V., Chen X., Han K.C., Mildvan A.S., Liu J.O. Biochemistry 46:12833-12843(2007) [PubMed: 17929833] [Abstract] Cited for: COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.

Hide | Top

Cross-references

Sequence databases
	AY374142 mRNA. Translation: AAR27795.1. DQ005576 mRNA. Translation: AAY55948.1. Different initiation. CH471058 Genomic DNA. Translation: EAX11190.1. BC113644 mRNA. Translation: AAI13645.1.
IPI	IPI00874126.
RefSeq	NP_954697.1.
UniGene	Hs.298250
3D structure databases
HSSP	HSSP built from PDB template 1O0X based on UniProtKB Q9X1I7.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6UB28.
Protein family/group databases
MEROPS	M24.028.
Proteomic databases
PRIDE	Q6UB28.
Genome annotation databases
Ensembl	ENST00000315796; ENSP00000315152; ENSG00000172878; Homo sapiens. [Genome view] ENST00000392582; ENSP00000376361; ENSG00000172878; Homo sapiens. [Genome view]
GeneID	254042.
KEGG	hsa:254042.
NMPDR	fig\|9606.3.peg.18908.
UCSC	uc002uhk.1. human.
Organism-specific databases
CTD	254042.
GeneCards	GC02P172573.
MIM	610267. gene.
Phylogenomic databases
HOVERGEN	Q6UB28.
Enzyme and pathway databases
BRENDA	3.4.11.18. 247.
Gene expression databases
ArrayExpress	Q6UB28.
Bgee	Q6UB28.
Genevestigator	Q6UB28.
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.
PANTHER	PTHR10804:SF13. Pept_M24A_MAP1. 1 hit. PTHR10804. Peptidase_M24_cat_core. 1 hit.
Pfam	PF00557. Peptidase_M24. 1 hit. [Graphical view]
PRINTS	PR00599. MAPEPTIDASE.
TIGRFAMs	TIGR00500. met_pdase_I. 1 hit.
PROSITE	PS00680. MAP_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	92234.
SOURCE	Search...

Hide | Top

Entry information

Entry name

AMP1D_HUMAN

Accession

Primary (citable) accession number: Q6UB28
Secondary accession number(s): Q1WNX3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	July 5, 2004
Last modified:	October 13, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Hide | Top