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Database: UniProt
Entry: L5K7Z8_PTEAL
LinkDB: L5K7Z8_PTEAL
Original site: L5K7Z8_PTEAL 
ID   L5K7Z8_PTEAL            Unreviewed;       180 AA.
AC   L5K7Z8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Cytosol aminopeptidase {ECO:0000313|EMBL:ELK07487.1};
GN   ORFNames=PAL_GLEAN10000879 {ECO:0000313|EMBL:ELK07487.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK07487.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC       {ECO:0000256|ARBA:ARBA00009528}.
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DR   EMBL; KB030960; ELK07487.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5K7Z8; -.
DR   STRING; 9402.L5K7Z8; -.
DR   MEROPS; M17.001; -.
DR   InParanoid; L5K7Z8; -.
DR   Proteomes; UP000010552; Unassembled WGS sequence.
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   Gene3D; 3.40.630.10; Zn peptidases; 2.
DR   InterPro; IPR011356; Leucine_aapep/pepB.
DR   InterPro; IPR000819; Peptidase_M17_C.
DR   PANTHER; PTHR11963:SF52; CYTOSOL AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR   Pfam; PF00883; Peptidase_M17; 2.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:ELK07487.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          2..104
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00883"
FT   DOMAIN          119..179
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00883"
SQ   SEQUENCE   180 AA;  19474 MW;  FCD6C09F5E9D8768 CRC64;
     METPANEVKP IRFAKSIEKN LKGASSKTEV YIRFKSWIEE QEMGSFLSVA KGSSDPSVFL
     EIHYRGSLDA SEPTLVFVEK GITFDSGGIS IKPSANMDLM RADVFSHCIC SQAQFSHLHT
     KNGKTIQVDS SDVKGRPILA DVLCYAHIFN PKVIINAATL TGAIDIALGS GTTGVFTKSS
//
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