ID A0A3Q3S8N2_9TELE Unreviewed; 1035 AA.
AC A0A3Q3S8N2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Leucyl/cystinyl aminopeptidase {ECO:0000313|Ensembl:ENSMAMP00000019635.1};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000019635.1, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000019635.1}
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 Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3Q3S8N2; -.
DR STRING; 205130.ENSMAMP00000019635; -.
DR Ensembl; ENSMAMT00000020151.2; ENSMAMP00000019635.1; ENSMAMG00000013218.2.
DR GeneTree; ENSGT00940000157902; -.
DR InParanoid; A0A3Q3S8N2; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000261640; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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:SF42; LEUCYL-CYSTINYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 184..368
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 402..622
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 699..1018
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 474
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 473
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 477
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 496
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 558
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 1035 AA; 117047 MW; B2D51EFB0A41BF26 CRC64;
MDPFDSSSTE RANLPRNMIE NSMFEEEPDI VDLAKDSTAF PTFPALDPDE VVYEPRSSRL
LVRGLGENDM DEDEEDCESS ARLLGMSFMN RSSALRSSSS PYTRQAPPSS CSRPSARTMV
VCVFVLVIVA SVTMALYFLP GCTFTKTGCR KPNKTTPLEP VYPLSTNGEL FPWAQLRLPH
SIRPLSYDLT LNPDLDSMTF TGHTVIQMSV LHSTKIIVLH SANLNIIKAT FKLGDEAARD
VTVLEYKPRQ QIAVKFPEEL KTGQYCVLTL DYSANLSHTY DGFYNSSYID KAGNKRVLAA
TQFEPLSARK AFPCFDEPAF KATFLIKISR KPNYMTLSNM PKAKSTPLSN GLMQDEFEKT
SVNMSTYLVA FIVANFTPIS KNASKTLVSV YSVPEKKEYT DYAMDAASKL LEFYNKFFDI
DYPLEKLDLV AIPDFLAGAM ENWGLITFRE TSLLVGKESS PLEKRVVATI IAHELAHQWF
GNMVTMSWWN DLWLNEGFAT YMEFMSVQTV FPELDIGNLF LAVRFRAMDK DALNSSHAVS
TEVNTSEQVE EMFDSVSYEK GASILLMLNA SLPWNQQFTK GIIQYLKQFN GLNTGTDDLW
NSLTQVDIST QRQNVSEMMH SWTSQKGFPL VTVSRKGNQV TLMQEHFLLT SDNGTLTSSL
WNIPVTYVND SCSLAPECRQ VFTLKTKSGT LKLPGNVKWL KLNYRNTGFY IVHYGDEGWA
ALIEALSTNV TVLTPEDRAS LIHNIFALSR LGRVSFHQVL NVLKYMSKET ETSPVTEALL
QLNIIYRLLD KRLEHDLAAR MKSYILDNFG PLMDKQTWGV EENVSKQELR SALLGMACSL
NQDKCIQQAK ALFKEYVKSN GTTRIPDDLQ QVVFTVAAQS EEDWSTLLGL FSATTYDAEK
RKMLRGLAST QNAWHIVWIL QAGLKGDIIQ TQELPLVINT VCNGFTGYLF AWDFIQENWD
RLIEKFSVGS YAMQIIIKSA TSQFSTKAHF DQVYGFFSSL KERGSQMRSV QEALETIRLN
QRWMDQNLPT LQKWL
//
