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Q9SLN5

- MAP1A_ARATH

UniProt

Q9SLN5 - MAP1A_ARATH

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Protein

Methionine aminopeptidase 1A

Gene
MAP1A, At2g45240, F4L23.25
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein 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) By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

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 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei214 – 2141Substrate By similarity
Metal bindingi231 – 2311Divalent metal cation 1 By similarity
Metal bindingi242 – 2421Divalent metal cation 1 By similarity
Metal bindingi242 – 2421Divalent metal cation 2; catalytic By similarity
Metal bindingi305 – 3051Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei312 – 3121Substrate By similarity
Metal bindingi338 – 3381Divalent metal cation 2; catalytic By similarity
Metal bindingi369 – 3691Divalent metal cation 1 By similarity
Metal bindingi369 – 3691Divalent metal cation 2; catalytic By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-HAMAP
  2. metalloaminopeptidase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. N-terminal protein amino acid modification Source: TAIR
  2. protein initiator methionine removal Source: UniProtKB-HAMAP
  3. protein processing Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciARA:AT2G45240-MONOMER.

Protein family/group databases

MEROPSiM24.017.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 1A (EC:3.4.11.18)
Short name:
MAP 1A
Short name:
MetAP 1A
Alternative name(s):
Peptidase M 1A
Gene namesi
Name:MAP1A
Ordered Locus Names:At2g45240
ORF Names:F4L23.25
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 2

Organism-specific databases

TAIRiAT2G45240.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: TAIR
  2. cytosol Source: TAIR
  3. cytosolic ribosome Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 398397Methionine aminopeptidase 1AUniRule annotationPRO_0000148969Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9SLN5.
PRIDEiQ9SLN5.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

GenevestigatoriQ9SLN5.

Interactioni

Subunit structurei

Associates with the 60S ribosomal subunit of the 80S translational complex By similarity.

Protein-protein interaction databases

MINTiMINT-8069122.
STRINGi3702.AT2G45240.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9SLN5.
SMRiQ9SLN5. Positions 95-389.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni15 – 5844Zinc finger-like; important for proper ribosome association By similarityAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030427.
InParanoidiQ9SLN5.
KOiK01265.
OMAiCFKRNWS.
PhylomeDBiQ9SLN5.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
IPR002893. Znf_MYND.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 1 hit.
TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
PROSITEiPS00680. MAP_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9SLN5-1 [UniParc]FASTAAdd to Basket

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MASESDASSI ATLSCARCEK PAHLQCPKCI DLKLPREQAS FCTQECFKAA    50
WSSHKSVHVK AQLSSIGDQN SDLISQGWLY CVKKGQARTP KLPHFDWTGP 100
LKQYPISTKR VVPAEIEKPD WAIDGTPKVE PNSDLQHVVE IKTPEQIQRM 150
RETCKIAREV LDAAARVIHP GVTTDEIDRV VHEATIAAGG YPSPLNYYFF 200
PKSCCTSVNE VICHGIPDAR KLEDGDIVNV DVTVCYKGCH GDLNETYFVG 250
NVDEASRQLV KCTYECLEKA IAIVKPGVRF REIGEIVNRH ATMSGLSVVR 300
SYCGHGIGDL FHCAPNIPHY ARNKAVGVMK AGQTFTIEPM INAGGWRDRT 350
WPDGWTAVTA DGKRSAQFEH TLLVTETGVE VLTARLPSSP DVYPWLTK 398
Length:398
Mass (Da):43,992
Last modified:May 1, 2000 - v1
Checksum:i4B9D23A90C5FA780
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311D → H in AAM65219. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiB84888.
RefSeqiNP_182049.1. NM_130087.3.
UniGeneiAt.12298.

Genome annotation databases

EnsemblPlantsiAT2G45240.1; AT2G45240.1; AT2G45240.
GeneIDi819132.
KEGGiath:AT2G45240.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi B84888.
RefSeqi NP_182049.1. NM_130087.3.
UniGenei At.12298.

3D structure databases

ProteinModelPortali Q9SLN5.
SMRi Q9SLN5. Positions 95-389.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-8069122.
STRINGi 3702.AT2G45240.1-P.

Protein family/group databases

MEROPSi M24.017.

Proteomic databases

PaxDbi Q9SLN5.
PRIDEi Q9SLN5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT2G45240.1 ; AT2G45240.1 ; AT2G45240 .
GeneIDi 819132.
KEGGi ath:AT2G45240.

Organism-specific databases

GeneFarmi 1939. 184.
TAIRi AT2G45240.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000030427.
InParanoidi Q9SLN5.
KOi K01265.
OMAi CFKRNWS.
PhylomeDBi Q9SLN5.

Enzyme and pathway databases

BioCyci ARA:AT2G45240-MONOMER.

Miscellaneous databases

PROi Q9SLN5.

Gene expression databases

Genevestigatori Q9SLN5.

Family and domain databases

Gene3Di 3.90.230.10. 1 hit.
HAMAPi MF_01974. MetAP_1.
InterProi IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
IPR002893. Znf_MYND.
[Graphical view ]
Pfami PF00557. Peptidase_M24. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view ]
PRINTSi PR00599. MAPEPTIDASE.
SUPFAMi SSF55920. SSF55920. 1 hit.
TIGRFAMsi TIGR00500. met_pdase_I. 1 hit.
PROSITEi PS00680. MAP_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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.
  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].
  6. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMAP1A_ARATH
AccessioniPrimary (citable) accession number: Q9SLN5
Secondary accession number(s): Q548T6, Q8LAQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 119 of the entry and version 1 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

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