MAP11_HUMAN
ID MAP11_HUMAN Reviewed; 386 AA.
AC P53582; B4E2E6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 210.
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; Synonyms=KIAA0094;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III. The
RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 110-386.
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT
RP IONS, FUNCTION, AND COFACTOR.
RX PubMed=16274222; DOI=10.1021/bi051691k;
RA Addlagatta A., Hu X., Liu J.O., Matthews B.W.;
RT "Structural basis for the functional differences between type I and type II
RT human methionine aminopeptidases.";
RL Biochemistry 44:14741-14749(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT IONS
RP AND INHIBITORS.
RX PubMed=16724298; DOI=10.1002/anie.200600757;
RA Hu X., Addlagatta A., Matthews B.W., Liu J.O.;
RT "Identification of pyridinylpyrimidines as inhibitors of human methionine
RT aminopeptidases.";
RL Angew. Chem. Int. Ed. 45:3772-3775(2006).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT IONS
RP AND INHIBITORS, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=17114291; DOI=10.1073/pnas.0608389103;
RA Hu X., Addlagatta A., Lu J., Matthews B.W., Liu J.O.;
RT "Elucidation of the function of type 1 human methionine aminopeptidase
RT during cell cycle progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:18148-18153(2006).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT IONS
RP AND THE INHIBITOR OVALICIN.
RX PubMed=16823043; DOI=10.1110/ps.062278006;
RA Addlagatta A., Matthews B.W.;
RT "Structure of the angiogenesis inhibitor ovalicin bound to its noncognate
RT target, human Type 1 methionine aminopeptidase.";
RL Protein Sci. 15:1842-1848(2006).
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). Required for normal progression
CC through the cell cycle. {ECO:0000255|HAMAP-Rule:MF_03174,
CC ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:17114291}.
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 ECO:0000269|PubMed:17114291};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03174,
CC ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298,
CC ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291};
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 -!- INTERACTION:
CC P53582; O76003: GLRX3; NbExp=3; IntAct=EBI-1051435, EBI-374781;
CC P53582; Q0VD86: INCA1; NbExp=3; IntAct=EBI-1051435, EBI-6509505;
CC P53582; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1051435, EBI-16439278;
CC P53582; Q14596-2: NBR1; NbExp=3; IntAct=EBI-1051435, EBI-11081753;
CC P53582; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-1051435, EBI-949255;
CC P53582; Q9UGI0: ZRANB1; NbExp=4; IntAct=EBI-1051435, EBI-527853;
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 -!- SEQUENCE CAUTION:
CC Sequence=AAH30054.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA07679.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D42084; BAA07679.1; ALT_INIT; mRNA.
DR EMBL; AK304239; BAG65108.1; -; mRNA.
DR EMBL; CH471057; EAX06083.1; -; Genomic_DNA.
DR EMBL; BC030054; AAH30054.1; ALT_INIT; mRNA.
DR CCDS; CCDS47110.1; -.
DR RefSeq; NP_055958.2; NM_015143.2.
DR PDB; 2B3H; X-ray; 1.10 A; A=81-384.
DR PDB; 2B3K; X-ray; 1.55 A; A=81-384.
DR PDB; 2B3L; X-ray; 1.50 A; A=81-384.
DR PDB; 2G6P; X-ray; 1.90 A; A=81-384.
DR PDB; 2GZ5; X-ray; 1.10 A; A=81-384.
DR PDB; 2NQ6; X-ray; 1.50 A; A=81-384.
DR PDB; 2NQ7; X-ray; 1.60 A; A=81-384.
DR PDB; 4FLI; X-ray; 1.55 A; A=81-386.
DR PDB; 4FLJ; X-ray; 1.74 A; A=81-386.
DR PDB; 4FLK; X-ray; 1.47 A; A=81-386.
DR PDB; 4FLL; X-ray; 1.50 A; A=81-386.
DR PDB; 4HXX; X-ray; 2.09 A; A=81-384.
DR PDB; 4IKR; X-ray; 1.78 A; A=81-384.
DR PDB; 4IKS; X-ray; 1.70 A; A=81-384.
DR PDB; 4IKT; X-ray; 1.60 A; A=81-384.
DR PDB; 4IKU; X-ray; 1.30 A; A=81-384.
DR PDB; 4IU6; X-ray; 1.90 A; A=1-384.
DR PDB; 4U1B; X-ray; 1.89 A; A=81-386.
DR PDB; 4U69; X-ray; 1.60 A; A=81-386.
DR PDB; 4U6C; X-ray; 1.91 A; A=81-386.
DR PDB; 4U6E; X-ray; 1.90 A; A=81-386.
DR PDB; 4U6J; X-ray; 1.56 A; A=81-386.
DR PDB; 4U6W; X-ray; 1.83 A; A=81-386.
DR PDB; 4U6Z; X-ray; 1.80 A; A=81-386.
DR PDB; 4U70; X-ray; 1.60 A; A=81-386.
DR PDB; 4U71; X-ray; 1.80 A; A=81-386.
DR PDB; 4U73; X-ray; 1.80 A; A=81-386.
DR PDB; 4U75; X-ray; 1.94 A; A=81-386.
DR PDB; 4U76; X-ray; 1.87 A; A=81-386.
DR PDB; 5YKP; X-ray; 1.68 A; A=81-384.
DR PDB; 5YR4; X-ray; 1.82 A; A=81-384.
DR PDB; 5YR5; X-ray; 1.60 A; A=81-384.
DR PDB; 5YR6; X-ray; 1.75 A; A=81-384.
DR PDB; 5YR7; X-ray; 2.06 A; A=81-386.
DR PDB; 6LZB; X-ray; 1.29 A; A=81-384.
DR PDB; 6LZC; X-ray; 1.35 A; A=81-384.
DR PDBsum; 2B3H; -.
DR PDBsum; 2B3K; -.
DR PDBsum; 2B3L; -.
DR PDBsum; 2G6P; -.
DR PDBsum; 2GZ5; -.
DR PDBsum; 2NQ6; -.
DR PDBsum; 2NQ7; -.
DR PDBsum; 4FLI; -.
DR PDBsum; 4FLJ; -.
DR PDBsum; 4FLK; -.
DR PDBsum; 4FLL; -.
DR PDBsum; 4HXX; -.
DR PDBsum; 4IKR; -.
DR PDBsum; 4IKS; -.
DR PDBsum; 4IKT; -.
DR PDBsum; 4IKU; -.
DR PDBsum; 4IU6; -.
DR PDBsum; 4U1B; -.
DR PDBsum; 4U69; -.
DR PDBsum; 4U6C; -.
DR PDBsum; 4U6E; -.
DR PDBsum; 4U6J; -.
DR PDBsum; 4U6W; -.
DR PDBsum; 4U6Z; -.
DR PDBsum; 4U70; -.
DR PDBsum; 4U71; -.
DR PDBsum; 4U73; -.
DR PDBsum; 4U75; -.
DR PDBsum; 4U76; -.
DR PDBsum; 5YKP; -.
DR PDBsum; 5YR4; -.
DR PDBsum; 5YR5; -.
DR PDBsum; 5YR6; -.
DR PDBsum; 5YR7; -.
DR PDBsum; 6LZB; -.
DR PDBsum; 6LZC; -.
DR AlphaFoldDB; P53582; -.
DR SMR; P53582; -.
DR BioGRID; 116785; 39.
DR IntAct; P53582; 23.
DR MINT; P53582; -.
DR STRING; 9606.ENSP00000296411; -.
DR BindingDB; P53582; -.
DR ChEMBL; CHEMBL2474; -.
DR DrugBank; DB07903; 3-[(2,2-DIMETHYLPROPANOYL)AMINO]-N-1,3-THIAZOL-2-YLPYRIDINE-2-CARBOXAMIDE.
DR DrugBank; DB07901; 5-CHLORO-6-METHYL-N-(2-PHENYLETHYL)-2-PYRIDIN-2-YLPYRIMIDIN-4-AMINE.
DR DrugBank; DB04324; Ovalicin.
DR DrugBank; DB07902; TERT-BUTYL {2-[(1,3-THIAZOL-2-YLAMINO)CARBONYL]PYRIDIN-3-YL}CARBAMATE.
DR DrugCentral; P53582; -.
DR GuidetoPHARMACOLOGY; 1572; -.
DR MEROPS; M24.017; -.
DR GlyGen; P53582; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P53582; -.
DR PhosphoSitePlus; P53582; -.
DR SwissPalm; P53582; -.
DR BioMuta; METAP1; -.
DR DMDM; 33302602; -.
DR EPD; P53582; -.
DR jPOST; P53582; -.
DR MassIVE; P53582; -.
DR MaxQB; P53582; -.
DR PaxDb; P53582; -.
DR PeptideAtlas; P53582; -.
DR PRIDE; P53582; -.
DR ProteomicsDB; 56586; -.
DR Antibodypedia; 25840; 204 antibodies from 25 providers.
DR DNASU; 23173; -.
DR Ensembl; ENST00000296411.11; ENSP00000296411.6; ENSG00000164024.12.
DR GeneID; 23173; -.
DR KEGG; hsa:23173; -.
DR MANE-Select; ENST00000296411.11; ENSP00000296411.6; NM_015143.3; NP_055958.2.
DR UCSC; uc003huf.5; human.
DR CTD; 23173; -.
DR DisGeNET; 23173; -.
DR GeneCards; METAP1; -.
DR HGNC; HGNC:15789; METAP1.
DR HPA; ENSG00000164024; Low tissue specificity.
DR MIM; 610151; gene.
DR neXtProt; NX_P53582; -.
DR OpenTargets; ENSG00000164024; -.
DR PharmGKB; PA30764; -.
DR VEuPathDB; HostDB:ENSG00000164024; -.
DR eggNOG; KOG2738; Eukaryota.
DR GeneTree; ENSGT00940000158205; -.
DR HOGENOM; CLU_015857_2_1_1; -.
DR InParanoid; P53582; -.
DR OMA; GDHAYTF; -.
DR OrthoDB; 1002357at2759; -.
DR PhylomeDB; P53582; -.
DR TreeFam; TF105753; -.
DR BioCyc; MetaCyc:HS08982-MON; -.
DR BRENDA; 3.4.11.18; 2681.
DR PathwayCommons; P53582; -.
DR Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR SABIO-RK; P53582; -.
DR SignaLink; P53582; -.
DR BioGRID-ORCS; 23173; 452 hits in 1092 CRISPR screens.
DR ChiTaRS; METAP1; human.
DR EvolutionaryTrace; P53582; -.
DR GeneWiki; METAP1; -.
DR GenomeRNAi; 23173; -.
DR Pharos; P53582; Tchem.
DR PRO; PR:P53582; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P53582; protein.
DR Bgee; ENSG00000164024; Expressed in esophagus squamous epithelium and 207 other tissues.
DR ExpressionAtlas; P53582; baseline and differential.
DR Genevisible; P53582; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004177; F:aminopeptidase activity; TAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0008235; F:metalloexopeptidase activity; TAS:UniProtKB.
DR GO; GO:0031365; P:N-terminal protein amino acid modification; TAS:HGNC-UCL.
DR GO; GO:0018206; P:peptidyl-methionine modification; TAS:HGNC-UCL.
DR GO; GO:0070527; P:platelet aggregation; HMP:UniProtKB.
DR GO; GO:0035551; P:protein initiator methionine removal involved in protein maturation; IBA:GO_Central.
DR GO; GO:0006417; P:regulation of translation; TAS:HGNC-UCL.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Aminopeptidase; Cytoplasm; Hydrolase;
KW Metal-binding; Protease; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..386
FT /note="Methionine aminopeptidase 1"
FT /id="PRO_0000148967"
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 203
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174,
FT ECO:0000269|PubMed:16724298, ECO:0000269|PubMed:16823043,
FT ECO:0000269|PubMed:17114291"
FT BINDING 220
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 ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298,
FT ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291"
FT BINDING 231
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 ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298,
FT ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291"
FT BINDING 231
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 ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298,
FT ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291"
FT BINDING 294
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 ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298,
FT ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174,
FT ECO:0000269|PubMed:16724298, ECO:0000269|PubMed:16823043,
FT ECO:0000269|PubMed:17114291"
FT BINDING 327
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 ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298,
FT ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291"
FT BINDING 358
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 ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298,
FT ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291"
FT BINDING 358
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 ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298,
FT ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2B3H"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:2B3H"
FT HELIX 117..121
FT /evidence="ECO:0007829|PDB:2B3H"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:2B3H"
FT HELIX 133..155
FT /evidence="ECO:0007829|PDB:2B3H"
FT HELIX 163..176
FT /evidence="ECO:0007829|PDB:2B3H"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:2B3H"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:2B3H"
FT STRAND 191..197
FT /evidence="ECO:0007829|PDB:2B3H"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:2B3H"
FT STRAND 216..225
FT /evidence="ECO:0007829|PDB:2B3H"
FT STRAND 228..237
FT /evidence="ECO:0007829|PDB:2B3H"
FT HELIX 243..261
FT /evidence="ECO:0007829|PDB:2B3H"
FT HELIX 271..282
FT /evidence="ECO:0007829|PDB:2B3H"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:2B3H"
FT STRAND 297..306
FT /evidence="ECO:0007829|PDB:2B3H"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:2B3H"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:2B3H"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:2B3H"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:2B3H"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:2B3H"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:2B3H"
FT STRAND 358..363
FT /evidence="ECO:0007829|PDB:2B3H"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:2B3H"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:2B3H"
SQ SEQUENCE 386 AA; 43215 MW; 372879013C2BB01D CRC64;
MAAVETRVCE TDGCSSEAKL QCPTCIKLGI QGSYFCSQEC FKGSWATHKL LHKKAKDEKA
KREVSSWTVE GDINTDPWAG YRYTGKLRPH YPLMPTRPVP SYIQRPDYAD HPLGMSESEQ
ALKGTSQIKL LSSEDIEGMR LVCRLAREVL DVAAGMIKPG VTTEEIDHAV HLACIARNCY
PSPLNYYNFP KSCCTSVNEV ICHGIPDRRP LQEGDIVNVD ITLYRNGYHG DLNETFFVGE
VDDGARKLVQ TTYECLMQAI DAVKPGVRYR ELGNIIQKHA QANGFSVVRS YCGHGIHKLF
HTAPNVPHYA KNKAVGVMKS GHVFTIEPMI CEGGWQDETW PDGWTAVTRD GKRSAQFEHT
LLVTDTGCEI LTRRLDSARP HFMSQF
