MAP2_BOVIN
ID MAP2_BOVIN Reviewed; 477 AA.
AC Q3ZC89;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Methionine aminopeptidase 2 {ECO:0000255|HAMAP-Rule:MF_03175};
DE Short=MAP 2 {ECO:0000255|HAMAP-Rule:MF_03175};
DE Short=MetAP 2 {ECO:0000255|HAMAP-Rule:MF_03175};
DE EC=3.4.11.18 {ECO:0000255|HAMAP-Rule:MF_03175};
DE AltName: Full=Initiation factor 2-associated 67 kDa glycoprotein {ECO:0000255|HAMAP-Rule:MF_03175};
DE Short=p67 {ECO:0000255|HAMAP-Rule:MF_03175};
DE Short=p67eIF2 {ECO:0000255|HAMAP-Rule:MF_03175};
DE AltName: Full=Peptidase M {ECO:0000255|HAMAP-Rule:MF_03175};
GN Name=METAP2 {ECO:0000255|HAMAP-Rule:MF_03175};
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=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-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_03175}.
CC -!- FUNCTION: Protects eukaryotic initiation factor EIF2S1 from
CC translation-inhibiting phosphorylation by inhibitory kinases such as
CC EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of
CC protein synthesis. {ECO:0000255|HAMAP-Rule:MF_03175}.
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_03175};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
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_03175};
CC -!- SUBUNIT: Binds EIF2S1 at low magnesium concentrations. Interacts
CC strongly with the eIF-2 gamma-subunit EIF2S3. {ECO:0000255|HAMAP-
CC Rule:MF_03175}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=About 30% of expressed METAP2
CC associates with polysomes. {ECO:0000255|HAMAP-Rule:MF_03175}.
CC -!- PTM: Contains approximately 12 O-linked N-acetylglucosamine (GlcNAc)
CC residues. O-glycosylation is required for EIF2S1 binding.
CC {ECO:0000255|HAMAP-Rule:MF_03175}.
CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC aminopeptidase eukaryotic type 2 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03175}.
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DR EMBL; BC102824; AAI02825.1; -; mRNA.
DR RefSeq; NP_001035583.1; NM_001040493.1.
DR AlphaFoldDB; Q3ZC89; -.
DR SMR; Q3ZC89; -.
DR STRING; 9913.ENSBTAP00000026568; -.
DR MEROPS; M24.002; -.
DR PaxDb; Q3ZC89; -.
DR PeptideAtlas; Q3ZC89; -.
DR GeneID; 404150; -.
DR KEGG; bta:404150; -.
DR CTD; 10988; -.
DR eggNOG; KOG2775; Eukaryota.
DR InParanoid; Q3ZC89; -.
DR OrthoDB; 601484at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070084; P:protein initiator methionine removal; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01088; MetAP2; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR HAMAP; MF_03175; MetAP_2_euk; 1.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001714; Pept_M24_MAP.
DR InterPro; IPR002468; Pept_M24A_MAP2.
DR InterPro; IPR018349; Pept_M24A_MAP2_BS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00557; Peptidase_M24; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
DR TIGRFAMs; TIGR00501; met_pdase_II; 1.
DR PROSITE; PS01202; MAP_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Aminopeptidase; Cytoplasm; Glycoprotein; Hydrolase;
KW Metal-binding; Phosphoprotein; Protease; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P50579"
FT CHAIN 2..477
FT /note="Methionine aminopeptidase 2"
FT /id="PRO_0000246091"
FT REGION 1..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
FT BINDING 250
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
FT BINDING 261
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
FT BINDING 261
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_03175"
FT BINDING 330
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_03175"
FT BINDING 338
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
FT BINDING 363
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_03175"
FT BINDING 458
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03175"
FT BINDING 458
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_03175"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P50579"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50579"
FT MOD_RES 62
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P50579"
FT CARBOHYD 62
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 477 AA; 52812 MW; 4D10309613D2F0F1 CRC64;
MAGVEEAASC GSHLNGDLDP DEREEGAAST AEEAAKKKKR KKKKSKGAAT GQQEPDKEAG
ASVDEVTRQL ERQALEEKEK DDDDEDGDGD GDGATGKKKK KKKKKRGPKV QTDPPSVPIC
DLYPNGVFPK GQECEYPPTQ DGRTAAWRTT SEEKKALDQA SEEIWNDFRE AAEAHRQVRK
YVMSWIKPGM TMIEICEKME DCSRKLIKEN GLNAGLAFPT GCSLNNCAAH YTPNAGDTTV
LQYDDICKID FGTHISGRII DCAFTVTFNP KYDTLLKAVK DATNTGIKCA GIDVRLCDVG
EAIQEVMESY EVEIDGKTYQ VKPIRNLNGH SIGPYRIHAG KTVPIVKGGE ATRMEEGEVY
AIETFGSTGK GVVHDDMECS HYMKNFDVGH VPIRLPRTKH LLNVINENFG TLAFCRRWLD
RLGESKYLMA LKNLCDLGIV DPYPPLCDIK GSYTAQFEHT ILLRPTCKEV VSRGDDY
