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Q9FV51

- MAP1C_ARATH

UniProt

Q9FV51 - MAP1C_ARATH

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Protein

Methionine aminopeptidase 1C, chloroplastic/mitochondrial

Gene

MAP1C

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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 Fe(2+)-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 sitei172 – 1721SubstrateUniRule annotation
Metal bindingi189 – 1891Divalent metal cation 1UniRule annotation
Metal bindingi200 – 2001Divalent metal cation 1UniRule annotation
Metal bindingi200 – 2001Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi262 – 2621Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei269 – 2691SubstrateUniRule annotation
Metal bindingi296 – 2961Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi327 – 3271Divalent metal cation 1UniRule annotation
Metal bindingi327 – 3271Divalent metal cation 2; catalyticUniRule annotation

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
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciARA:AT3G25740-MONOMER.

Protein family/group databases

MEROPSiM24.A07.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 1C, chloroplastic/mitochondrialUniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 1CUniRule annotation
Short name:
MetAP 1CUniRule annotation
Alternative name(s):
Peptidase M 1CUniRule annotation
Gene namesi
Name:MAP1C
Ordered Locus Names:At3g25740
ORF Names:K13N2.8
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G25740.

Subcellular locationi

Plastidchloroplast 1 PublicationUniRule annotation. Mitochondrion 1 PublicationUniRule annotation

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Mitochondrion, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 344Methionine aminopeptidase 1C, chloroplastic/mitochondrialPRO_0000045806
Transit peptidei1 – ?Chloroplast and mitochondrionUniRule annotation

Proteomic databases

PaxDbiQ9FV51.
PRIDEiQ9FV51.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

ExpressionAtlasiQ9FV51. baseline and differential.
GenevestigatoriQ9FV51.

Structurei

3D structure databases

ProteinModelPortaliQ9FV51.
SMRiQ9FV51. Positions 67-341.
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.
InParanoidiQ9FV51.
OMAiMERFIGH.
PhylomeDBiQ9FV51.

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.

Sequencei

Sequence statusi: Complete.

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

Q9FV51-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLQKISQSIS LCNGDQFKPL IYLAGAPTNF ISSPLSGKKK SSSLRIKRIQ
60 70 80 90 100
QLQSTLEDRI NPPLVCGTVS PRLSVPDHIL KPLYVESSKV PEISSELQIP
110 120 130 140 150
DSIGIVKMKK ACELAARVLD YAGTLVRPFV TTDEIDKAVH QMVIEFGAYP
160 170 180 190 200
SPLGYGGFPK SVCTSVNECM FHGIPDSRPL QNGDIINIDV AVYLDGYHGD
210 220 230 240 250
TSKTFLCGDV NGSLKQLVKV TEECLEKGIS VCKDGASFKQ IGKIISEHAA
260 270 280 290 300
KYGYNMERFI GHGVGTVLHS EPLIYLHSNY DYELEYMIEG QTFTLEPILT
310 320 330 340
IGTTEFVTWP DKWTIVTADG GPAAQFEHTI LITTTGAEIL TISS
Length:344
Mass (Da):37,679
Last modified:January 24, 2006 - v2
Checksum:iABD84A7FF64D70BA
GO

Sequence cautioni

The sequence BAA95761.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti264 – 2641V → L in AAG33976. (PubMed:11060042)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF250962 mRNA. Translation: AAG33976.1.
AB028607 Genomic DNA. Translation: BAA95761.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE77063.1.
RefSeqiNP_189202.1. NM_113473.2.
UniGeneiAt.16911.

Genome annotation databases

EnsemblPlantsiAT3G25740.1; AT3G25740.1; AT3G25740.
GeneIDi822165.
KEGGiath:AT3G25740.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF250962 mRNA. Translation: AAG33976.1 .
AB028607 Genomic DNA. Translation: BAA95761.1 . Sequence problems.
CP002686 Genomic DNA. Translation: AEE77063.1 .
RefSeqi NP_189202.1. NM_113473.2.
UniGenei At.16911.

3D structure databases

ProteinModelPortali Q9FV51.
SMRi Q9FV51. Positions 67-341.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M24.A07.

Proteomic databases

PaxDbi Q9FV51.
PRIDEi Q9FV51.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT3G25740.1 ; AT3G25740.1 ; AT3G25740 .
GeneIDi 822165.
KEGGi ath:AT3G25740.

Organism-specific databases

GeneFarmi 2287. 184.
TAIRi AT3G25740.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000030427.
InParanoidi Q9FV51.
OMAi MERFIGH.
PhylomeDBi Q9FV51.

Enzyme and pathway databases

BioCyci ARA:AT3G25740-MONOMER.

Gene expression databases

ExpressionAtlasi Q9FV51. baseline and differential.
Genevestigatori Q9FV51.

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.
[Graphical view ]
Pfami PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
PRINTSi PR00599. MAPEPTIDASE.
SUPFAMi SSF55920. SSF55920. 1 hit.
TIGRFAMsi TIGR00500. met_pdase_I. 1 hit.
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. "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
    Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
    DNA Res. 7:131-135(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.

Entry informationi

Entry nameiMAP1C_ARATH
AccessioniPrimary (citable) accession number: Q9FV51
Secondary accession number(s): Q9LS05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: January 24, 2006
Last modified: November 26, 2014
This is version 97 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