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Database: UniProt
Entry: L5LBL8_MYODS
LinkDB: L5LBL8_MYODS
Original site: L5LBL8_MYODS 
ID   L5LBL8_MYODS            Unreviewed;       320 AA.
AC   L5LBL8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Pregnancy-associated glycoprotein {ECO:0000313|EMBL:ELK23415.1};
GN   ORFNames=MDA_GLEAN10009048 {ECO:0000313|EMBL:ELK23415.1};
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:ELK23415.1, 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   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000256|ARBA:ARBA00004239}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; KB113693; ELK23415.1; -; Genomic_DNA.
DR   MEROPS; A01.051; -.
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; 3.
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:SF49; PEPSIN A-5; 1.
DR   Pfam; PF00026; Asp; 3.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 3.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
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}.
FT   DOMAIN          3..316
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        21
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        209
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        34..39
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        200..204
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        243..277
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   320 AA;  34486 MW;  86E071016B6AB40B CRC64;
     MYYVGTISIG TPPQKFKVVF DTGSADLWVP SIYCSSPACV THKTFNPLRS STFQSTDRPI
     QLLYGSASMT GLLGYDDVRY IVSCEAVQSL PDIVFTINGI AYPVPASAYI QRLRVPNLPM
     RPPSXXXXXX XXAFGLSTTE PSKSLEFAAF DGILGLAYPS LALKDTTPVF DSLWEQGLLP
     ENLFAFYLSS ISMNGTVVAC PGGCQAIMDT GTSLVIGPLS PVLNILKSIN ARTTSTGEYI
     VSCEAVQSLP DIVFTINGIA YPVPASAYIR REQTGICFSN VDIDTSGSSS LWVLGDVFLR
     LYFTVFDRAN NRIGLAPAVA
//
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