ID G3N6B7_GASAC Unreviewed; 892 AA.
AC G3N6B7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000000842.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000000842.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000000842.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR AlphaFoldDB; G3N6B7; -.
DR STRING; 69293.ENSGACP00000000842; -.
DR MEROPS; M01.010; -.
DR Ensembl; ENSGACT00000000842.1; ENSGACP00000000842.1; ENSGACG00000000645.1.
DR eggNOG; KOG1046; Eukaryota.
DR GeneTree; ENSGT00940000155246; -.
DR InParanoid; G3N6B7; -.
DR OMA; MMEYVAI; -.
DR TreeFam; TF300395; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000000645; Expressed in intestinal epithelial cell and 13 other cell types or tissues.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU364040};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 74..259
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 294..511
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 592..890
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 367
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 452
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 892 AA; 99639 MW; 71CFE96884DF516C CRC64;
MLLLLGRRVP LSFVHRLTTC RPPPRPVLLR SALLKLSAIT GATHTTVFVS ATGQHTGTMP
ERRPFVRLPA DVYPVNYGLC LKPDLIDFTF EGKLEALVEV TQATNQIVMN CADIDIITAS
FVLPGGDEIN ATGFNYQNED EKVTLSFPSA LQKGSGTLKV DFVGELNDKM KGFYRSKYTA
PTGEVRYAAV TQFEATDARR AFPCWDEPAI KATFDIALIV PKDRVALSNM NVIDRKPCPE
DANLVEVKFA TTPIMSTYLV AFVIGEYDFV ESQSSDGITV RVYTPVGKAE QGKFALEVAT
KTLPFYKDYF SVPYPLPKID LIAIADFAAG AMENWGLVTY RETALLIDPK NSCSSSRQWV
ALVVGHELAH QWFGNLVTME WWTHLWLNEG FASWIEYLCV DHCFPEYDIW TQFVSADYTR
ALDLDALDSS HPIEVNVGHP SEVDEIFDAI SYSKGASVIR MLHNWTGDED FRKGMNAYLL
KFQHKNASTE DLWECLEQAS GKPIAEVMSS WTKQMGFPII VVEEEKQGDE RILKLSQKKF
CASGPHNGES CPSWMVPVSI CTSEDPKCTK LKVLLDRPET TVTLSGVAPD QWIKINPGTV
GFYRIQYSTA MLESLLPGVR DLSLPPVDRL GLQNDLFSLS RAGMISTVEV LKLMEAFVNE
PNYTVWSDLS SNLGVLSSLL SHTEFHEDIQ EFIRDLFTPI GLELGWDCKP GEGHLDALLR
GLVLGKLGKA GHKPTLEEAR RRFRDHVEGK QVLPADLRSP VYLTVLKHGD SATLDTMMKL
HKLADMQEEK NRIERVLGAI SAPDLIQKVL SFALSEDVRP QDTVFVIGGV AGSSKQGRKA
AWKFVKDNWE ELYNRYQGGF LISQLIKYTV DGFAIDKMAA EFLSFFESHA SP
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