MAP11_DANRE
ID MAP11_DANRE Reviewed; 386 AA.
AC Q4QRK0; Q6DHD3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Methionine aminopeptidase 1 {ECO:0000255|HAMAP-Rule:MF_03174};
DE Short=MAP 1 {ECO:0000255|HAMAP-Rule:MF_03174};
DE Short=MetAP 1 {ECO:0000255|HAMAP-Rule:MF_03174};
DE EC=3.4.11.18 {ECO:0000255|HAMAP-Rule:MF_03174};
DE AltName: Full=Peptidase M 1 {ECO:0000255|HAMAP-Rule:MF_03174};
GN Name=metap1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cotranslationally removes the N-terminal methionine from
CC nascent proteins. The N-terminal methionine is often cleaved when the
CC second residue in the primary sequence is small and uncharged (Met-
CC Ala-, Cys, Gly, Pro, Ser, Thr, or Val). {ECO:0000255|HAMAP-
CC Rule:MF_03174}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal amino acids, preferentially methionine,
CC from peptides and arylamides.; EC=3.4.11.18;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03174};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03174};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03174};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03174};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03174};
CC Note=Binds 2 divalent metal cations per subunit. Has a high-affinity
CC and a low affinity metal-binding site. The true nature of the
CC physiological cofactor is under debate. The enzyme is active with
CC cobalt, zinc, manganese or divalent iron ions. Most likely, methionine
CC aminopeptidases function as mononuclear Fe(2+)-metalloproteases under
CC physiological conditions, and the catalytically relevant metal-binding
CC site has been assigned to the histidine-containing high-affinity site.
CC {ECO:0000255|HAMAP-Rule:MF_03174};
CC -!- SUBUNIT: Associates with the 60S ribosomal subunit of the 80S
CC translational complex. {ECO:0000255|HAMAP-Rule:MF_03174}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03174}.
CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC aminopeptidase type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_03174}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC076042; AAH76042.1; -; mRNA.
DR EMBL; BC096796; AAH96796.1; -; mRNA.
DR AlphaFoldDB; Q4QRK0; -.
DR SMR; Q4QRK0; -.
DR STRING; 7955.ENSDARP00000113818; -.
DR MEROPS; M24.017; -.
DR PaxDb; Q4QRK0; -.
DR ZFIN; ZDB-GENE-050626-124; metap1.
DR eggNOG; KOG2738; Eukaryota.
DR InParanoid; Q4QRK0; -.
DR PhylomeDB; Q4QRK0; -.
DR Reactome; R-DRE-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR PRO; PR:Q4QRK0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0035551; P:protein initiator methionine removal involved in protein maturation; IBA:GO_Central.
DR CDD; cd01086; MetAP1; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR HAMAP; MF_01974; MetAP_1; 1.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001714; Pept_M24_MAP.
DR InterPro; IPR002467; Pept_M24A_MAP1.
DR InterPro; IPR031615; Zfn-C6H2.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF15801; zf-C6H2; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF55920; SSF55920; 1.
DR TIGRFAMs; TIGR00500; met_pdase_I; 1.
DR PROSITE; PS00680; MAP_1; 1.
PE 2: Evidence at transcript level;
KW Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding; Protease;
KW Reference proteome.
FT CHAIN 1..386
FT /note="Methionine aminopeptidase 1"
FT /id="PRO_0000323737"
FT REGION 9..52
FT /note="Zinc finger-like; important for proper ribosome
FT association"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 219
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 230
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 230
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 293
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 326
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 357
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 357
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT CONFLICT 275
FT /note="I -> T (in Ref. 1; AAH96796)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 386 AA; 43567 MW; 74A2F0661A5BFDAB CRC64;
MAAVETRECE TEGCHSEAKL QCPTCIKLGI QGSYFCSQEC FKGSWATHKL LHKKAKEDKT
NDEEKNCVEK EVNTDPWPGY RYTGKLRPYY PLTPMRLVPS NIQRPDYADH PLGMSESEQT
MKGTSQIKIL NAEEIEGMRV VCKLAREVLD IAAMMVKPGV TTEEIDHAVH LACTARNCYP
SPLNYYNFPK SCCTSVNEVI CHGIPDRRHL QEGDILNIDI TVYHNGYHGD LNETFFVGEV
DEGAKRLVQT TYECLMQAID SVKPGIRYRE LGNIIQKHAQ ANGFSVVRSY CGHGIHKLFH
TAPNVPHYAK NKAVGVMKPG HVFTIEPMIC EGGWQDETWP DGWTAVTRDG KRSAQFEHTL
LVTETGCEIL TRRLEDNGRA HFLSQM
