Q9FV49 (AMP2A_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methionine aminopeptidase 2A
Short name=MAP 2A
Short name=MetAP 2A
EC=3.4.11.18

Alternative name(s):
Peptidase M 2A

Gene names

Name:	MAP2A
Ordered Locus Names:	At2g44180
ORF Names:	F6E13.31

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	441 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. Preferentially expressed in roots. 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 proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay Ref.1. Source: TAIR
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
	Chain	1 – 441	441	Methionine aminopeptidase 2A		PRO_0000148970
Regions
	Compositional bias	63 – 75	13	Lys-rich
Sites
	Metal binding	214	1	Cobalt 1 By similarity
	Metal binding	225	1	Cobalt 1 By similarity
	Metal binding	225	1	Cobalt 2 By similarity
	Metal binding	294	1	Cobalt 2 By similarity
	Metal binding	327	1	Cobalt 2 By similarity
	Metal binding	422	1	Cobalt 1 By similarity
	Metal binding	422	1	Cobalt 2 By similarity
	Binding site	194	1	Substrate By similarity
	Binding site	302	1	Substrate By similarity
Experimental info
	Sequence conflict	12	1	G → E in AAG33978. Ref.1
	Sequence conflict	51	1	Missing in AAG33978. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9FV49 [UniParc]. Last modified January 24, 2006. Version 2. Checksum: FEC98F6679F0D573	FASTA	441	49,395
	10 20 30 40 50 60 MAIGNPEVAT MGKENTEAES SNGNESQLSS DLTKSLDLAE VKEDEKDNNQ EEEDGLKAEA 70 80 90 100 110 120 STKKKKKKSK SKKKKSSLQQ TDPPSIPVLE LFPSGDFPQG EIQQYNDDNL WRTTSEEKRE 130 140 150 160 170 180 MERLQKPIYN SLRQAAEVHR QVRKYMRSIL KPGMLMIDLC ETLENTVRKL ISENGLQAGI 190 200 210 220 230 240 AFPTGCSLNN VAAHWTPNSG DKTVLQYDDV MKLDFGTHID GHIVDSAFTV AFNPMFDPLL 250 260 270 280 290 300 AASRDATYTG IKEAGVDVRL CDVGAAVQEV MESYEVEING KVYQVKSIRN LNGHSIGRYQ 310 320 330 340 350 360 IHAEKSVPNV RGGEQTKMEE GELYAIETFG STGKGYVRED LECSHYMKNY DVGHVPLRLP 370 380 390 400 410 420 RAKQLLATIN KNFSTLAFCR RYLDRLGETK YLMALKNLCD SGIIEPCPPV CDVKGSYISQ 430 440 FEHTILLRPT CKEIISKGDD Y

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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF250964 mRNA. Translation: AAG33978.1. AC004005 Genomic DNA. Translation: AAC23422.2. CP002685 Genomic DNA. Translation: AEC10386.1. BT006476 mRNA. Translation: AAP21284.1.
IPI	IPI00538764.
PIR	T00698.
RefSeq	NP_566013.1. NM_129981.4.
UniGene	At.19509.
3D structure databases
ProteinModelPortal	Q9FV49.
SMR	Q9FV49. Positions 80-441.
ModBase	Search...
Protein family/group databases
MEROPS	M24.A02.
Proteomic databases
PRIDE	Q9FV49.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G44180.1; AT2G44180.1; AT2G44180.
GeneID	819025.
GenomeReviews	Gene locus AT2G44180 in contig CT485783_GR.
KEGG	ath:AT2G44180.
NMPDR	fig|3702.1.peg.11591.
Organism-specific databases
GeneFarm	1935. 191.
TAIR	At2g44180.
Phylogenomic databases
eggNOG	KOG2775.
GeneTree	EPGT00070000029106.
HOGENOM	HBG318153.
InParanoid	Q9FV49.
OMA	FSERDMA.
PhylomeDB	Q9FV49.
ProtClustDB	CLSN2688923.
Gene expression databases
Genevestigator	Q9FV49.
GermOnline	AT2G44180. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR001714. Pept_M24_MAP. IPR000994. Pept_M24_structural-domain. IPR002468. Pept_M24A_MAP2. IPR018349. Pept_M24A_MAP2_BS. IPR011991. WHTH_trsnscrt_rep_DNA-bd. [Graphical view]
Gene3D	G3DSA:3.90.230.10. Peptidase_M24_cat_core. 2 hits. G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
KO	K01265.
PANTHER	PTHR10804:SF9. Pept_M24A_MAP2. 1 hit.
Pfam	PF00557. Peptidase_M24. 1 hit. [Graphical view]
PRINTS	PR00599. MAPEPTIDASE.
SUPFAM	SSF55920. Peptidase_M24_cat_core. 1 hit.
TIGRFAMs	TIGR00501. Met_pdase_II. 1 hit.
PROSITE	PS01202. MAP_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMP2A_ARATH

Accession

Primary (citable) accession number: Q9FV49
Secondary accession number(s): O80587

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	January 24, 2006
Last modified:	November 16, 2011
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program