ID MAP1_BOVIN Reviewed; 386 AA. AC A6QLA4; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 02-SEP-2026, entry version 113. 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 Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Heart ventricle; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (JUN-2007) 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=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03174}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03174}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03174}; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP- CC 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 zinc, CC cobalt, manganese or divalent iron ions. Has high activity with zinc; CC zinc cofactor is transferred into the active site region by the ZNG1 CC zinc chaperone. {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; BC147894; AAI47895.1; -; mRNA. DR RefSeq; NP_001095507.1; NM_001102037.1. DR AlphaFoldDB; A6QLA4; -. DR SMR; A6QLA4; -. DR FunCoup; A6QLA4; 3196. DR STRING; 9913.ENSBTAP00000072918; -. DR MEROPS; M24.017; -. DR PaxDb; 9913-ENSBTAP00000072918; -. DR GeneID; 516540; -. DR KEGG; bta:516540; -. DR CTD; 23173; -. DR VEuPathDB; HostDB:ENSBTAG00000016004; -. DR VGNC; VGNC:31395; METAP1. DR eggNOG; KOG2738; Eukaryota. DR HOGENOM; CLU_015857_2_1_1; -. DR InParanoid; A6QLA4; -. DR OMA; FYGDHAY; -. DR OrthoDB; 3209743at2759; -. DR Reactome; R-BTA-2514859; Inactivation, recovery and regulation of the phototransduction cascade. DR CD-CODE; D7FE2080; Nucleolus. DR Proteomes; UP000009136; Chromosome 6. DR Bgee; ENSBTAG00000016004; Expressed in conceptus and 108 other cell types or tissues. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004239; F:initiator methionyl aminopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR CDD; cd01086; MetAP1; 1. DR FunFam; 3.90.230.10:FF:000010; Methionine aminopeptidase; 1. DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 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 NCBIfam; TIGR00500; met_pdase_I; 1. DR PANTHER; PTHR43330; METHIONINE AMINOPEPTIDASE; 1. DR PANTHER; PTHR43330:SF7; METHIONINE AMINOPEPTIDASE 1; 1. DR Pfam; PF00557; Peptidase_M24; 1. DR Pfam; PF15801; zf-C6H2; 1. DR PRINTS; PR00599; MAPEPTIDASE. DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1. DR PROSITE; PS00680; MAP_1; 1. DR PROSITE; PS52013; ZF_C6H2; 1. PE 2: Evidence at transcript level; KW Acetylation; Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding; Protease; KW Reference proteome; Zinc; Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P53582" FT CHAIN 2..386 FT /note="Methionine aminopeptidase 1" FT /id="PRO_0000323734" FT ZN_FING 6..59 FT /note="C6H2-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01357" FT BINDING 9 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 14 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 22 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 25 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 36 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 40 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 48 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 52 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 203 FT /ligand="a protein" FT /ligand_id="ChEBI:CHEBI:16541" FT /ligand_part="N-terminal L-methionine residue" FT /ligand_part_id="ChEBI:CHEBI:64731" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 220 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 231 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 231 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 294 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 301 FT /ligand="a protein" FT /ligand_id="ChEBI:CHEBI:16541" FT /ligand_part="N-terminal L-methionine residue" FT /ligand_part_id="ChEBI:CHEBI:64731" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 327 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 358 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 358 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P53582" SQ SEQUENCE 386 AA; 43183 MW; A8B81D71B11C04C2 CRC64; MAAVETRVCE TDGCSSEAKL QCPTCIKLGI QGSYFCSQEC FKGSWATHKL LHKKAKDEKA KREVSSWTVE GDINTDPWAG YRYTGKLRPH YPLMPTRPVP SYIQRPDYAD HPLGMSESEQ ALKGTSQIKL LSSEDIEGMR LVCRLAREVL DIAAGLIKPG VTTEEIDHAV HLACIARNCY PSPLNYYNFP KSCCTSVNEV ICHGIPDRRP LQEGDIVNVD ITLYRNGYHG DLNETFFVGD VDEGARKLVQ TTYECLMQAI DAVKPGVRYR ELGNIIQKHA QANGFSVVRS YCGHGIHKLF HTAPNVPHYS KNKAVGVMKA GHVFTIEPMI CEGGWQDETW PDGWTAVTRD GKRSAQFEHT LLVTDTGCEI LTRRLDSAQP HFMSQF //