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Protein

Methionine aminopeptidase 1B, chloroplastic

Gene

MAP1B

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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 sitei199 – 1991SubstrateUniRule annotation
Metal bindingi216 – 2161Divalent metal cation 1UniRule annotation
Metal bindingi227 – 2271Divalent metal cation 1UniRule annotation
Metal bindingi227 – 2271Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi290 – 2901Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei297 – 2971SubstrateUniRule annotation
Metal bindingi322 – 3221Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi353 – 3531Divalent metal cation 1UniRule annotation
Metal bindingi353 – 3531Divalent 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:AT1G13270-MONOMER.
ARA:GQT-2392-MONOMER.

Protein family/group databases

MEROPSiM24.A05.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 1B, chloroplasticUniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 1BUniRule annotation
Short name:
MetAP 1BUniRule annotation
Alternative name(s):
Peptidase M 1BUniRule annotation
Gene namesi
Name:MAP1B
Ordered Locus Names:At1g13270
ORF Names:T6J4.3
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G13270.

Subcellular locationi

  • Plastidchloroplast UniRule annotation1 Publication

GO - Cellular componenti

  • chloroplast Source: TAIR
  • mitochondrion Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5555ChloroplastUniRule annotationAdd
BLAST
Chaini56 – 369314Methionine aminopeptidase 1B, chloroplasticPRO_0000045805Add
BLAST

Proteomic databases

PaxDbiQ9FV52.
PRIDEiQ9FV52.

Expressioni

Tissue specificityi

Ubiquitous. Preferentially expressed in green tissues.1 Publication

Gene expression databases

ExpressionAtlasiQ9FV52. baseline and differential.
GenevestigatoriQ9FV52.

Interactioni

Protein-protein interaction databases

BioGridi23127. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9FV52.
SMRiQ9FV52. Positions 91-367.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030427.
InParanoidiQ9FV52.
KOiK01265.
OMAiGTHEWEM.
PhylomeDBiQ9FV52.

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.
[Graphical view]
PfamiPF00557. Peptidase_M24. 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.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9FV52-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASSVFLSSF SSSSSLQLCS SFHGEYLAPS RCFLGAPVTS SSLSLSGKKN
60 70 80 90 100
SYSPRQFHVS AKKVSGLEEA IRIRKMRELE TKSKVRRNPP LRRGRVSPRL
110 120 130 140 150
LVPDHIPRPP YVESGVLPDI SSEFQIPGPE GIAKMRAACE LAARVLNYAG
160 170 180 190 200
TLVKPSVTTN EIDKAVHDMI IEAGAYPSPL GYGGFPKSVC TSVNECMCHG
210 220 230 240 250
IPDSRQLQSG DIINIDVTVY LDGYHGDTSR TFFCGEVDEG FKRLVKVTEE
260 270 280 290 300
CLERGIAVCK DGASFKKIGK RISEHAEKFG YNVVERFVGH GVGPVFHSEP
310 320 330 340 350
LIYHYRNDEP GLMVEGQTFT IEPILTIGTT ECVTWPDNWT TLTADGGVAA
360
QFEHTILITR TGSEILTKC
Length:369
Mass (Da):40,424
Last modified:January 24, 2006 - v2
Checksum:i0D28974852F33747
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341L → I in AAG33975 (PubMed:11060042).Curated
Sequence conflicti243 – 2431R → Q in AAG33975 (PubMed:11060042).Curated
Sequence conflicti254 – 2541R → K in AAG33975 (PubMed:11060042).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF250961 mRNA. Translation: AAG33975.1.
AC011810 Genomic DNA. Translation: AAG09564.1.
CP002684 Genomic DNA. Translation: AEE28993.1.
BT000449 mRNA. Translation: AAN17426.1.
BT001213 mRNA. Translation: AAN65100.1.
PIRiC86267.
RefSeqiNP_172785.1. NM_101198.3. [Q9FV52-1]
UniGeneiAt.21097.

Genome annotation databases

EnsemblPlantsiAT1G13270.1; AT1G13270.1; AT1G13270. [Q9FV52-1]
GeneIDi837887.
KEGGiath:AT1G13270.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF250961 mRNA. Translation: AAG33975.1.
AC011810 Genomic DNA. Translation: AAG09564.1.
CP002684 Genomic DNA. Translation: AEE28993.1.
BT000449 mRNA. Translation: AAN17426.1.
BT001213 mRNA. Translation: AAN65100.1.
PIRiC86267.
RefSeqiNP_172785.1. NM_101198.3. [Q9FV52-1]
UniGeneiAt.21097.

3D structure databases

ProteinModelPortaliQ9FV52.
SMRiQ9FV52. Positions 91-367.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi23127. 1 interaction.

Protein family/group databases

MEROPSiM24.A05.

Proteomic databases

PaxDbiQ9FV52.
PRIDEiQ9FV52.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G13270.1; AT1G13270.1; AT1G13270. [Q9FV52-1]
GeneIDi837887.
KEGGiath:AT1G13270.

Organism-specific databases

GeneFarmi2345. 184.
TAIRiAT1G13270.

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030427.
InParanoidiQ9FV52.
KOiK01265.
OMAiGTHEWEM.
PhylomeDBiQ9FV52.

Enzyme and pathway databases

BioCyciARA:AT1G13270-MONOMER.
ARA:GQT-2392-MONOMER.

Miscellaneous databases

PROiQ9FV52.

Gene expression databases

ExpressionAtlasiQ9FV52. baseline and differential.
GenevestigatoriQ9FV52.

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.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 1 hit.
TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
PROSITEiPS00680. MAP_1. 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. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.

Entry informationi

Entry nameiMAP1B_ARATH
AccessioniPrimary (citable) accession number: Q9FV52
Secondary accession number(s): Q9FX70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: January 24, 2006
Last modified: April 29, 2015
This is version 100 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.