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Database: UniProt
Entry: L5KQU8_PTEAL
LinkDB: L5KQU8_PTEAL
Original site: L5KQU8_PTEAL 
ID   L5KQU8_PTEAL            Unreviewed;       650 AA.
AC   L5KQU8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Inactive N-acetylated-alpha-linked acidic dipeptidase-like protein 2 {ECO:0000313|EMBL:ELK13620.1};
DE   Flags: Fragment;
GN   ORFNames=PAL_GLEAN10012879 {ECO:0000313|EMBL:ELK13620.1};
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:ELK13620.1, 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC       pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC       {ECO:0000256|ARBA:ARBA00005634}.
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DR   EMBL; KB030623; ELK13620.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5KQU8; -.
DR   STRING; 9402.L5KQU8; -.
DR   MEROPS; M28.975; -.
DR   eggNOG; KOG2195; Eukaryota.
DR   InParanoid; L5KQU8; -.
DR   Proteomes; UP000010552; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd03874; M28_PMSA_TfR_like; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 1.20.930.40; Transferrin receptor-like, dimerisation domain; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR007484; Peptidase_M28.
DR   InterPro; IPR039373; Peptidase_M28B.
DR   InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR   PANTHER; PTHR10404:SF32; INACTIVE N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE-LIKE PROTEIN 2; 1.
DR   PANTHER; PTHR10404; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF47672; Transferrin receptor-like dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT   DOMAIN          286..450
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ELK13620.1"
SQ   SEQUENCE   650 AA;  72467 MW;  FAED243CAFA6AE1B CRC64;
     SYRNLVQLYT SEDDTEISKK IETQWTSLGL EDIQFVNYSV LLNLPGPSPS SVTLSSSGQC
     FHPNGQPCSE EARKRNSQDL LYSYAAYSAK GTLEAEVIDV SYGNADDLKR IKKIKNVTNQ
     IALLKLGKLP LLYKLLARGM RDGLIYFKKI NYGMNLITRM QKAVIDLKLS LLEKAGFGGV
     LLYIDPCDLP KTANLSYDTF MVSLNPGGDP STPGYPSVDG SFRQNRPNLT SLLVQPISAS
     LVAKLISPQK DRTRKGVCSP LELPNNEGRI VNMQVQTVTK FKTVTNVVGY LKGLTSPDRY
     IIVGSHHHTA YSYSGQEWAS STAIITAFIQ ALMLRVKRGW RPDRSIVFCS WGGTAFGNIG
     SYEWGEDFKK VLQRNAVAYV SLHSPIRGNS SLYSVASPSL QQLVAEKNNF NCSRRAQCPK
     TNVSSVQIQG DSEYFINHLG VPTVQFAYED IKALQGPSFL SEALFPKHAT KIEEMDPFFT
     LHETITKLSG EVILQIANEP VLPFNALDIA IEVQNSLKGD QPNTHQLLAL ASRLRESAEL
     FQSDEMRPAN DPKERVPIRV RMLNDILQDM EKSFLVQQVP PGFYRNILYH LDKKTSQFSI
     LLEAWEHCKT LASNETLQEA LSEVLHSINS AQVYFKAGLD VFDSVLVGKN
//
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