ID B8JIB1_DANRE Unreviewed; 405 AA.
AC B8JIB1; A0A0R4IWG3; A0A8M1N6S5;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Methionine aminopeptidase {ECO:0000256|RuleBase:RU003653};
DE EC=3.4.11.18 {ECO:0000256|RuleBase:RU003653};
GN Name=metap1 {ECO:0000313|Ensembl:ENSDARP00000113818,
GN ECO:0000313|RefSeq:NP_001020336.2,
GN ECO:0000313|ZFIN:ZDB-GENE-050626-124};
GN Synonyms=fc84e12 {ECO:0000313|RefSeq:NP_001020336.2}, im:7047238
GN {ECO:0000313|RefSeq:NP_001020336.2}, wu:fc84e12
GN {ECO:0000313|RefSeq:NP_001020336.2}, zgc:110093
GN {ECO:0000313|RefSeq:NP_001020336.2};
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 {ECO:0000313|Ensembl:ENSDARP00000113818};
RN [1] {ECO:0000313|RefSeq:NP_001020336.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001020336.2};
RX PubMed=16109975;
RA Woods I.G., Wilson C., Friedlander B., Chang P., Reyes D.K., Nix R.,
RA Kelly P.D., Chu F., Postlethwait J.H., Talbot W.S.;
RT "The zebrafish gene map defines ancestral vertebrate chromosomes.";
RL Genome Res. 15:1307-1314(2005).
RN [2] {ECO:0000313|RefSeq:NP_001020336.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001020336.2};
RX PubMed=18976794;
RA De Wit M., Keil D., Remmerie N., van der Ven K., van den Brandhof E.J.,
RA Knapen D., Witters E., De Coen W.;
RT "Molecular targets of TBBPA in zebrafish analysed through integration of
RT genomic and proteomic approaches.";
RL Chemosphere 74:96-105(2008).
RN [3] {ECO:0000313|RefSeq:NP_001020336.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001020336.2};
RX PubMed=21937698;
RA Ma A.C., Fung T.K., Lin R.H., Chung M.I., Yang D., Ekker S.C., Leung A.Y.;
RT "Methionine aminopeptidase 2 is required for HSC initiation and
RT proliferation.";
RL Blood 118:5448-5457(2011).
RN [4] {ECO:0000313|RefSeq:NP_001020336.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001020336.2};
RX PubMed=22182705;
RA Huang Q., Huang H.Q.;
RT "Alterations of protein profile in zebrafish liver cells exposed to methyl
RT parathion: a membrane proteomics approach.";
RL Chemosphere 87:68-76(2012).
RN [5] {ECO:0000313|RefSeq:NP_001020336.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001020336.2};
RX PubMed=24198278;
RA Recher G., Jouralet J., Brombin A., Heuze A., Mugniery E., Hermel J.M.,
RA Desnoulez S., Savy T., Herbomel P., Bourrat F., Peyrieras N., Jamen F.,
RA Joly J.S.;
RT "Zebrafish midbrain slow-amplifying progenitors exhibit high levels of
RT transcripts for nucleotide and ribosome biogenesis.";
RL Development 140:4860-4869(2013).
RN [6] {ECO:0000313|Ensembl:ENSDARP00000113818, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000113818};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [7] {ECO:0000313|Ensembl:ENSDARP00000113818}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000113818};
RG Ensembl;
RL Submitted (AUG-2013) to UniProtKB.
RN [8] {ECO:0000313|RefSeq:NP_001020336.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001020336.2};
RX PubMed=29914980; DOI=10.1242/dmm.034124;
RA Schultz L.E., Haltom J.A., Almeida M.P., Wierson W.A., Solin S.L.,
RA Weiss T.J., Helmer J.A., Sandquist E.J., Shive H.R., McGrail M.;
RT "Epigenetic regulators Rbbp4 and Hdac1 are overexpressed in a zebrafish
RT model of RB1 embryonal brain tumor, and are required for neural progenitor
RT survival and proliferation. .";
RL Dis. Model. Mech. 11:dmm034124-dmm034124(2018).
RN [9] {ECO:0000313|RefSeq:NP_001020336.2}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001020336.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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).
CC {ECO:0000256|RuleBase:RU003653}.
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:0000256|HAMAP-Rule:MF_03174,
CC ECO:0000256|RuleBase:RU003653};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03174};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03174};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03174};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_03174};
CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC aminopeptidase type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_03174}.
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DR EMBL; CR559943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001020336.2; NM_001025165.2.
DR Ensembl; ENSDART00000140096.3; ENSDARP00000113818.1; ENSDARG00000033440.10.
DR Ensembl; ENSDART00000160997.2; ENSDARP00000141477.2; ENSDARG00000110334.1.
DR GeneID; 503783; -.
DR KEGG; dre:503783; -.
DR AGR; ZFIN:ZDB-GENE-050626-124; -.
DR CTD; 23173; -.
DR ZFIN; ZDB-GENE-050626-124; metap1.
DR HOGENOM; CLU_015857_2_1_1; -.
DR OMA; FYGDHAY; -.
DR OrthoDB; 5475502at2759; -.
DR TreeFam; TF105753; -.
DR Proteomes; UP000000437; Alternate scaffold 13.
DR Proteomes; UP000000437; Chromosome 13.
DR Bgee; ENSDARG00000033440; Expressed in somite and 29 other cell types or tissues.
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; IEA:UniProtKB-UniRule.
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.
PE 1: Evidence at protein level;
KW Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_03174,
KW ECO:0000256|RuleBase:RU003653};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03174};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03174,
KW ECO:0000256|RuleBase:RU003653};
KW Protease {ECO:0000256|HAMAP-Rule:MF_03174, ECO:0000256|RuleBase:RU003653};
KW Proteomics identification {ECO:0007829|PeptideAtlas:B8JIB1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 28..73
FT /note="MYND-like zinc finger"
FT /evidence="ECO:0000259|Pfam:PF15801"
FT DOMAIN 155..383
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT BINDING 238
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT BINDING 249
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT BINDING 249
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT BINDING 312
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT BINDING 345
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT BINDING 376
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
FT BINDING 376
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03174"
SQ SEQUENCE 405 AA; 45392 MW; D215B647C28E04BA CRC64;
MTAAADSSGS LSLTDSSRSM AAVETRECET EGCHSEAKLQ CPTCIKLGIQ GSYFCSQECF
KGSWATHKLL HKKAKEDKTN DEEKNCVEKE VNTDPWPGYR YTGKLRPYYP LTPMRLVPSN
IQRPDYADHP LGMSESEQTM KGTSQIKILN AEEIEGMRVV CKLAREVLDI AAMMVKPGVT
TEEIDHAVHL ACTARNCYPS PLNYYNFPKS CCTSVNEVIC HGIPDRRHLQ EGDILNIDIT
VYHNGYHGDL NETFFVGEVD EGAKRLVQTT YECLMQAIDS VKPGIRYREL GNIIQKHAQA
NGFSVVRSYC GHGIHKLFHT APNVPHYAKN KAVGVMKPGH VFTIEPMICE GGWQDETWPD
GWTAVTRDGK RSAQFEHTLL VTETGCEILT RRLEDNGRAH FLSQM
//
