ID MAP1_CHICK Reviewed; 385 AA.
AC Q5ZIM5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 118.
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; ORFNames=RCJMB04_24o19;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03174};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
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 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}.
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DR EMBL; AJ720759; CAG32418.1; -; mRNA.
DR RefSeq; NP_001026322.1; NM_001031151.1.
DR AlphaFoldDB; Q5ZIM5; -.
DR SMR; Q5ZIM5; -.
DR STRING; 9031.ENSGALP00000019961; -.
DR MEROPS; M24.017; -.
DR PaxDb; 9031-ENSGALP00000040704; -.
DR Ensembl; ENSGALT00000138019; ENSGALP00000083191; ENSGALG00000012239.
DR Ensembl; ENSGALT00010010802.1; ENSGALP00010006215.1; ENSGALG00010004641.1.
DR Ensembl; ENSGALT00015041985; ENSGALP00015024548; ENSGALG00015017171.
DR GeneID; 422704; -.
DR KEGG; gga:422704; -.
DR CTD; 23173; -.
DR VEuPathDB; HostDB:geneid_422704; -.
DR eggNOG; KOG2738; Eukaryota.
DR GeneTree; ENSGT00940000158205; -.
DR HOGENOM; CLU_015857_2_1_1; -.
DR InParanoid; Q5ZIM5; -.
DR OMA; FYGDHAY; -.
DR OrthoDB; 5475502at2759; -.
DR PhylomeDB; Q5ZIM5; -.
DR PRO; PR:Q5ZIM5; -.
DR Proteomes; UP000000539; Chromosome 4.
DR Bgee; ENSGALG00000012239; Expressed in skeletal muscle tissue and 13 other cell types or tissues.
DR ExpressionAtlas; Q5ZIM5; baseline and differential.
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:UniProtKB-KW.
DR CDD; cd01086; MetAP1; 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 Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..385
FT /note="Methionine aminopeptidase 1"
FT /id="PRO_0000323736"
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"
SQ SEQUENCE 385 AA; 43121 MW; F2A223FF82A13DFA CRC64;
MAAVETRVCE TAGCSSEAKL QCPTCLKLGI QGSYFCSQEC FKGSWATHKL LHKKAKDEKA
KREVSSWTLE GDINTNPWSG YRYTGKLRPH YPLTPTRPVP SYIQRPDYAD HPLGMSESEQ
ALKGTSQIKI LSPEDIEGMR VVCRLAREVL DVAAMMVKAG VTTEEIDHAV HLACIARNCY
PSPLNYYNFP KSCCTSVNEV ICHGIPDRRP LQEGDIVNVD ITVYRNGYHG DLNETFYVGE
VDEGAKRLVQ TTYECLMQAI DAVKPGVRYR ELGNIIQKHA QANGFSVVRS YCGHGIHKLF
HTAPNVPHYA KNKAVGVMKP GHVFTIEPMI CEGGWQDETW PDGWTAVTRD GKRSAQFEHT
LLVTDTGCEI LTRRLDSIRP HFMSQ
//
