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
//