ID W5MGL2_LEPOC Unreviewed; 523 AA.
AC W5MGL2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Aminopeptidase like 1 {ECO:0000313|Ensembl:ENSLOCP00000007521.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000007521.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000007521.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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DR EMBL; AHAT01024342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01024343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006639705.1; XM_006639642.2.
DR AlphaFoldDB; W5MGL2; -.
DR STRING; 7918.ENSLOCP00000007521; -.
DR MEROPS; M17.006; -.
DR Ensembl; ENSLOCT00000007529.1; ENSLOCP00000007521.1; ENSLOCG00000006225.1.
DR GeneID; 102691441; -.
DR KEGG; loc:102691441; -.
DR CTD; 79716; -.
DR eggNOG; KOG2597; Eukaryota.
DR GeneTree; ENSGT00530000063255; -.
DR HOGENOM; CLU_013734_3_1_1; -.
DR InParanoid; W5MGL2; -.
DR OMA; MVCEQSD; -.
DR OrthoDB; 2899215at2759; -.
DR Proteomes; UP000018468; Linkage group LG18.
DR Bgee; ENSLOCG00000006225; Expressed in intestine and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR Gene3D; 3.40.50.10590; Zn-dependent exopeptidases; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR041417; NPEPL1_N.
DR InterPro; IPR000819; Peptidase_M17_C.
DR PANTHER; PTHR11963:SF4; AMINOPEPTIDASE NPEPL1-RELATED; 1.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF18295; Pdase_M17_N2; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 340..347
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
FT REGION 501..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 55626 MW; 39F2099D20ED8ACD CRC64;
MANVVLEFKA AAGDSEPQSR PVLVVGRLAN LQQVTWAEVK GKLQPTVSKE TWQSALSALN
PNPTDSCPLY LSYASVAALP SRVSRHNSPS AAHFLTRLVR SCLPGGASRC IVVVCERSEV
FASACAVARA FPLFSRRSSA SRRADKRLVV VEFVTVGEDN GPLDLGTLEC LSSTADGVRL
AARIVDTPCN EMNTDHFLEE IKAVGNELRI VPVIIRGEEL REKGFGGIYG VGKAAEYPPA
LAVLSHTPEG ATQTIAWVGK GIVYDTGGLS IKGKTTMPGM KRDCGGAAAV LGAFRAAVKQ
GFKDNLHAVF CLAENSVGPN ATRPDDIHTL YSGKTVEINN TDAEGRLVLS DGVAYASRDL
AADIILDMAT LTGAQGISTG KYHAAVMTNS EEWEAACVRA GRSSGDLAHP LVYCPELHFS
EFTSAVADMK NSVADRENAQ SSCAGLFIGS HLGFDWPGVW VHVDIASPVH AGERATGFGV
ALLLALFGQA SEDPLLNLVS PLGGQDRGRP EQMERDCKRR RLV
//