Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Methionine aminopeptidase 1

Gene

metap1

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Binding sitei203SubstrateUniRule annotation1
Metal bindingi220Divalent metal cation 1UniRule annotation1
Metal bindingi231Divalent metal cation 1UniRule annotation1
Metal bindingi231Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi294Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation1
Binding sitei301SubstrateUniRule annotation1
Metal bindingi327Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi358Divalent metal cation 1UniRule annotation1
Metal bindingi358Divalent metal cation 2; catalyticUniRule annotation1

GO - Molecular functioni

Keywordsi

Molecular functionAminopeptidase, Hydrolase, Protease
LigandMetal-binding

Protein family/group databases

MEROPSiM24.001

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 1UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 1UniRule annotation
Short name:
MetAP 1UniRule annotation
Alternative name(s):
Peptidase M 1UniRule annotation
Gene namesi
Name:metap1
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6254194 metap1

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003237381 – 385Methionine aminopeptidase 1Add BLAST385

Proteomic databases

PRIDEiQ7ZWV9

Interactioni

Subunit structurei

Associates with the 60S ribosomal subunit of the 80S translational complex.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ7ZWV9
SMRiQ7ZWV9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni9 – 52Zinc finger-like; important for proper ribosome associationUniRule annotationAdd BLAST44

Sequence similaritiesi

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

Phylogenomic databases

HOVERGENiHBG067178
KOiK01265

Family and domain databases

CDDicd01086 MetAP1, 1 hit
HAMAPiMF_01974 MetAP_1, 1 hit
InterProiView protein in InterPro
IPR036005 Creatinase/aminopeptidase-like
IPR000994 Pept_M24
IPR001714 Pept_M24_MAP
IPR002467 Pept_M24A_MAP1
IPR031615 Zfn-C6H2
PfamiView protein in Pfam
PF00557 Peptidase_M24, 1 hit
PF15801 zf-C6H2, 1 hit
PRINTSiPR00599 MAPEPTIDASE
SUPFAMiSSF55920 SSF55920, 1 hit
TIGRFAMsiTIGR00500 met_pdase_I, 1 hit
PROSITEiView protein in PROSITE
PS00680 MAP_1, 1 hit

Sequencei

Sequence statusi: Complete.

Q7ZWV9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVESRVCE TEGCSSEAKL QCPTCIKLGI QGSYFCSQEC FKGSWATHKL
60 70 80 90 100
LHKKAKDDKI KPEVSPWTMD GEVNTDPWPG YRYTGKLRPH YPLTPMRPVP
110 120 130 140 150
SYIQRPDYAD HPLGMSESEQ TLKGTSQIKT LSPEDIEGMR VVCRLAREVL
160 170 180 190 200
GVAAMMVKSG ITTEEIDHAV HLACISRNCY PSPLNYYNFP KSCCTSVNEV
210 220 230 240 250
ICHGIPDRRP LQDGDIVNVD ITVYRDGYHG DLNETFYVGD VDEGAKRLVE
260 270 280 290 300
TTYECLMQAI DEVKPGVRYR ELGNIIQKHA QANGFSIVRS YCGHGIHKLF
310 320 330 340 350
HTAPNVPHYG KNKAVGVMKP GHVFTIEPMI CEGGWQDETW PDGWTAITRD
360 370 380
GKRSAQFEHT LLVTETGCEI LTCRLEENGR PYFIS
Length:385
Mass (Da):43,196
Last modified:March 18, 2008 - v2
Checksum:iE3CCA9B269376EEF
GO

Sequence cautioni

The sequence AAH46685 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC046685 mRNA Translation: AAH46685.1 Different initiation.
BC070567 mRNA Translation: AAH70567.1
RefSeqiXP_018107543.1, XM_018252054.1
UniGeneiXl.76058

Genome annotation databases

GeneIDi399247
KEGGixla:399247

Similar proteinsi

Entry informationi

Entry nameiMAP1_XENLA
AccessioniPrimary (citable) accession number: Q7ZWV9
Secondary accession number(s): Q6NRY8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: May 23, 2018
This is version 89 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health