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Protein

Methionine aminopeptidase 2A

Gene

MAP2A

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).UniRule annotation

Catalytic activityi

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation

Cofactori

Co2+UniRule annotation, Zn2+UniRule annotation, Mn2+UniRule annotation, Fe2+UniRule annotationNote: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei194 – 1941SubstrateUniRule annotation
Metal bindingi214 – 2141Divalent metal cation 1UniRule annotation
Metal bindingi225 – 2251Divalent metal cation 1UniRule annotation
Metal bindingi225 – 2251Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi294 – 2941Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei302 – 3021SubstrateUniRule annotation
Metal bindingi327 – 3271Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi422 – 4221Divalent metal cation 1UniRule annotation
Metal bindingi422 – 4221Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

GO - Biological processi

  • N-terminal protein amino acid modification Source: TAIR
  • protein initiator methionine removal Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciARA:AT2G44180-MONOMER.
ReactomeiREACT_307091. Inactivation, recovery and regulation of the phototransduction cascade.

Protein family/group databases

MEROPSiM24.A02.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 2AUniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 2AUniRule annotation
Short name:
MetAP 2AUniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
Name:MAP2AUniRule annotation
Ordered Locus Names:At2g44180
ORF Names:F6E13.31
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G44180.

Subcellular locationi

  • Cytoplasm UniRule annotation1 Publication

GO - Cellular componenti

  • cytoplasm Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 441441Methionine aminopeptidase 2APRO_0000148970Add
BLAST

Proteomic databases

PaxDbiQ9FV49.
PRIDEiQ9FV49.

Expressioni

Tissue specificityi

Ubiquitous. Preferentially expressed in roots.1 Publication

Gene expression databases

ExpressionAtlasiQ9FV49. baseline and differential.
GenevestigatoriQ9FV49.

Structurei

3D structure databases

ProteinModelPortaliQ9FV49.
SMRiQ9FV49. Positions 80-441.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi63 – 7513Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
InParanoidiQ9FV49.
KOiK01265.
OMAiNGHTIEP.
PhylomeDBiQ9FV49.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPiMF_03175. MetAP_2_euk.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10804:SF9. PTHR10804:SF9. 1 hit.
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 2 hits.
TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
PROSITEiPS01202. MAP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9FV49-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIGNPEVAT MGKENTEAES SNGNESQLSS DLTKSLDLAE VKEDEKDNNQ
60 70 80 90 100
EEEDGLKAEA STKKKKKKSK SKKKKSSLQQ TDPPSIPVLE LFPSGDFPQG
110 120 130 140 150
EIQQYNDDNL WRTTSEEKRE MERLQKPIYN SLRQAAEVHR QVRKYMRSIL
160 170 180 190 200
KPGMLMIDLC ETLENTVRKL ISENGLQAGI AFPTGCSLNN VAAHWTPNSG
210 220 230 240 250
DKTVLQYDDV MKLDFGTHID GHIVDSAFTV AFNPMFDPLL AASRDATYTG
260 270 280 290 300
IKEAGVDVRL CDVGAAVQEV MESYEVEING KVYQVKSIRN LNGHSIGRYQ
310 320 330 340 350
IHAEKSVPNV RGGEQTKMEE GELYAIETFG STGKGYVRED LECSHYMKNY
360 370 380 390 400
DVGHVPLRLP RAKQLLATIN KNFSTLAFCR RYLDRLGETK YLMALKNLCD
410 420 430 440
SGIIEPCPPV CDVKGSYISQ FEHTILLRPT CKEIISKGDD Y
Length:441
Mass (Da):49,395
Last modified:January 24, 2006 - v2
Checksum:iFEC98F6679F0D573
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121G → E in AAG33978 (PubMed:11060042).Curated
Sequence conflicti51 – 511Missing in AAG33978 (PubMed:11060042).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF250964 mRNA. Translation: AAG33978.1.
AC004005 Genomic DNA. Translation: AAC23422.2.
CP002685 Genomic DNA. Translation: AEC10386.1.
BT006476 mRNA. Translation: AAP21284.1.
PIRiT00698.
RefSeqiNP_566013.1. NM_129981.4.
UniGeneiAt.19509.

Genome annotation databases

EnsemblPlantsiAT2G44180.1; AT2G44180.1; AT2G44180.
GeneIDi819025.
KEGGiath:AT2G44180.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF250964 mRNA. Translation: AAG33978.1.
AC004005 Genomic DNA. Translation: AAC23422.2.
CP002685 Genomic DNA. Translation: AEC10386.1.
BT006476 mRNA. Translation: AAP21284.1.
PIRiT00698.
RefSeqiNP_566013.1. NM_129981.4.
UniGeneiAt.19509.

3D structure databases

ProteinModelPortaliQ9FV49.
SMRiQ9FV49. Positions 80-441.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM24.A02.

Proteomic databases

PaxDbiQ9FV49.
PRIDEiQ9FV49.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G44180.1; AT2G44180.1; AT2G44180.
GeneIDi819025.
KEGGiath:AT2G44180.

Organism-specific databases

GeneFarmi1935. 191.
TAIRiAT2G44180.

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
InParanoidiQ9FV49.
KOiK01265.
OMAiNGHTIEP.
PhylomeDBiQ9FV49.

Enzyme and pathway databases

BioCyciARA:AT2G44180-MONOMER.
ReactomeiREACT_307091. Inactivation, recovery and regulation of the phototransduction cascade.

Miscellaneous databases

PROiQ9FV49.

Gene expression databases

ExpressionAtlasiQ9FV49. baseline and differential.
GenevestigatoriQ9FV49.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPiMF_03175. MetAP_2_euk.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10804:SF9. PTHR10804:SF9. 1 hit.
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 2 hits.
TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
PROSITEiPS01202. MAP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  2. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.

Entry informationi

Entry nameiMAP21_ARATH
AccessioniPrimary (citable) accession number: Q9FV49
Secondary accession number(s): O80587
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: January 24, 2006
Last modified: May 27, 2015
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.