Q9SLN5 (AMP1A_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methionine aminopeptidase 1A
Short name=MAP 1A
Short name=MetAP 1A
EC=3.4.11.18

Alternative name(s):
Peptidase M 1A

Gene names

Name:	MAP1A
Ordered Locus Names:	At2g45240
ORF Names:	F4L23.25

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	398 AA.
Sequence status	Complete.
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.
Subcellular location	Cytoplasm Ref.1.
Tissue specificity	Ubiquitous. Ref.1
Sequence similarities	Belongs to the peptidase M24A family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Cobalt Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	N-terminal protein amino acid modification Traceable author statement. Source: TAIR protein processing Non-traceable author statement Ref.1. Source: TAIR proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: TAIR
Molecular function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 398	398	Methionine aminopeptidase 1A		PRO_0000148969
Sites
	Metal binding	231	1	Cobalt 1 By similarity
	Metal binding	242	1	Cobalt 1 By similarity
	Metal binding	242	1	Cobalt 2 By similarity
	Metal binding	305	1	Cobalt 2 By similarity
	Metal binding	338	1	Cobalt 2 By similarity
	Metal binding	369	1	Cobalt 1 By similarity
	Metal binding	369	1	Cobalt 2 By similarity
	Binding site	214	1	Substrate By similarity
	Binding site	312	1	Substrate By similarity
Experimental info
	Sequence conflict	31	1	D → H in AAM65219. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9SLN5 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 4B9D23A90C5FA780	FASTA	398	43,992
	10 20 30 40 50 60 MASESDASSI ATLSCARCEK PAHLQCPKCI DLKLPREQAS FCTQECFKAA WSSHKSVHVK 70 80 90 100 110 120 AQLSSIGDQN SDLISQGWLY CVKKGQARTP KLPHFDWTGP LKQYPISTKR VVPAEIEKPD 130 140 150 160 170 180 WAIDGTPKVE PNSDLQHVVE IKTPEQIQRM RETCKIAREV LDAAARVIHP GVTTDEIDRV 190 200 210 220 230 240 VHEATIAAGG YPSPLNYYFF PKSCCTSVNE VICHGIPDAR KLEDGDIVNV DVTVCYKGCH 250 260 270 280 290 300 GDLNETYFVG NVDEASRQLV KCTYECLEKA IAIVKPGVRF REIGEIVNRH ATMSGLSVVR 310 320 330 340 350 360 SYCGHGIGDL FHCAPNIPHY ARNKAVGVMK AGQTFTIEPM INAGGWRDRT WPDGWTAVTA 370 380 390 DGKRSAQFEH TLLVTETGVE VLTARLPSSP DVYPWLTK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms." Giglione C., Serero A., Pierre M., Boisson B., Meinnel T. EMBO J. 19:5916-5929(2000) [PubMed: 11060042] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[2]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF250960 mRNA. Translation: AAG33974.1. AC002387 Genomic DNA. Translation: AAB82638.1. CP002685 Genomic DNA. Translation: AEC10528.1. AY099542 mRNA. Translation: AAM20394.1. BT008490 mRNA. Translation: AAP37849.1. AY087682 mRNA. Translation: AAM65219.1.
IPI	IPI00520769.
PIR	B84888.
RefSeq	NP_182049.1. NM_130087.3.
UniGene	At.12298.
3D structure databases
ProteinModelPortal	Q9SLN5.
SMR	Q9SLN5. Positions 95-389.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9SLN5.
Proteomic databases
PRIDE	Q9SLN5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G45240.1; AT2G45240.1; AT2G45240.
GeneID	819132.
GenomeReviews	Gene locus AT2G45240 in contig CT485783_GR.
KEGG	ath:AT2G45240.
NMPDR	fig|3702.1.peg.11702.
Organism-specific databases
GeneFarm	1939. 184.
TAIR	At2g45240.
Phylogenomic databases
GeneTree	EPGT00070000030452.
HOGENOM	HBG299384.
InParanoid	Q9SLN5.
OMA	QEGMRKV.
PhylomeDB	Q9SLN5.
ProtClustDB	PLN03158.
Gene expression databases
ArrayExpress	Q9SLN5.
Genevestigator	Q9SLN5.
GermOnline	AT2G45240. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR001714. Pept_M24_MAP. IPR000994. Pept_M24_structural-domain. IPR002467. Pept_M24A_MAP1. IPR002893. Znf_MYND. [Graphical view]
Gene3D	G3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.
KO	K01265.
Pfam	PF00557. Peptidase_M24. 1 hit. PF01753. zf-MYND. 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...

Entry information

Entry name

AMP1A_ARATH

Accession

Primary (citable) accession number: Q9SLN5
Secondary accession number(s): Q548T6, Q8LAQ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	May 1, 2000
Last modified:	November 16, 2011
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program