ID L5LVV3_MYODS Unreviewed; 357 AA.
AC L5LVV3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Napsin-A {ECO:0000313|EMBL:ELK30160.1};
GN ORFNames=MDA_GLEAN10005290 {ECO:0000313|EMBL:ELK30160.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK30160.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
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 -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KB107319; ELK30160.1; -; Genomic_DNA.
DR AlphaFoldDB; L5LVV3; -.
DR MEROPS; A01.046; -.
DR eggNOG; KOG1339; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF94; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..357
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003970660"
FT DOMAIN 79..357
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 43..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 97
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 284
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 110..117
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 275..279
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 357 AA; 38129 MW; 465323C3D98A0DF5 CRC64;
MSLPPPPPLL LLLLLPLLTA GPASAALIRI PLHRVYAGSR TPNPLRGWGS PEEPRGLGAP
PPGGKSAFVP LSNYMNAQYY GKIGLGTPPQ NFSVVFDTGS SNLWVPSRRC SFFSLPCWFH
HRFDPKASST FKPNGTKFAI QYGSGQLSGI LSEDKLTIGG IKNASVVFGE ALWEPSLVFV
FAHFDGILGL GFPVLAVGGV RPPLDTMVDQ GLLDKPVFSF YLNRDPEAAE GGELVLGGSD
PAHYIPPLTY VPVTVPAYWQ VHMERVTVGP GLTLCAQGCP AILDTGTSLI TGPTEEIRAL
HRAIGGFPLL GKYIIECSVI PALPPVSFSL GGVWFNLTSQ DYVIQVGSGQ NDVRGTR
//
