ID A0A3P9PED1_POERE Unreviewed; 411 AA.
AC A0A3P9PED1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Aminopeptidase like 1 {ECO:0000313|Ensembl:ENSPREP00000020261.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000020261.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000020261.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000020261.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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DR AlphaFoldDB; A0A3P9PED1; -.
DR STRING; 8081.ENSPREP00000020261; -.
DR Ensembl; ENSPRET00000020475.1; ENSPREP00000020261.1; ENSPREG00000013703.1.
DR GeneTree; ENSGT00530000063255; -.
DR OMA; MVCEQSD; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000013703; Expressed in head and 1 other cell type or tissue.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR000819; Peptidase_M17_C.
DR PANTHER; PTHR11963:SF4; AMINOPEPTIDASE NPEPL1-RELATED; 1.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 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:UP000242638}.
FT DOMAIN 228..235
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
FT REGION 387..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 43590 MW; 07F72F266482930D CRC64;
VVCERSDVFA SACAVARAFP LFTRRSASSR RTEKKHVTVE FVVVNNDGGL LDDAELKCLS
NAADGVRLAA RIVDTPCSEM NTDHFLDEIK VVGSELGITP VIIRGEELKQ RGFGGIYGVG
KAAEHPPALA VLSHTPDGAT QTIAWVGKGI VYDTGGLSIK GKTTMPGMKR DCGGAAAILG
AFKATIKQGF KDNLHAVFCL AENSVGPTAT RPDDIHTLYS GKTVEINNTD AEGRLVLADG
VVYASKDLSA DIILDMATLT GAQGISTGKY HAAVMTNSEQ WEGACVRAGR SSGDLAHPLV
YCPELHFSEF TSAVADMKNS VADRENAQSS CAGLFIGSHL GFDWPGVWVH VDIASPVHAG
ERATGFGVAL LMALFGQASD DSMLNQVSPL GAPTNKPEDQ MERDCKRRRL V
//