ID E3UMT5_BUBBU Unreviewed; 370 AA.
AC E3UMT5;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Pregnancy-associated glycoprotein 9 {ECO:0000313|EMBL:ADO67798.1};
DE Flags: Fragment;
GN Name=PAG9 {ECO:0000313|EMBL:ADO67798.1};
OS Bubalus bubalis (Domestic water buffalo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bubalus.
OX NCBI_TaxID=89462 {ECO:0000313|EMBL:ADO67798.1};
RN [1] {ECO:0000313|EMBL:ADO67798.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Placental cotyledons {ECO:0000313|EMBL:ADO67798.1};
RA Green J.A., Egen T., Kandil O.M., Abdoon A.;
RT "cDNA sequencing of pregnancy associated glycoproteins (PAGs) from water
RT buffalo.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HM468478; ADO67798.1; -; mRNA.
DR AlphaFoldDB; E3UMT5; -.
DR MEROPS; A01.089; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 6.10.140.60; -; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR012848; Aspartic_peptidase_N.
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; PF07966; A1_Propeptide; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 2: Evidence at transcript level;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454}.
FT DOMAIN 68..370
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 86
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 267
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 99..104
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 258..262
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADO67798.1"
FT NON_TER 370
FT /evidence="ECO:0000313|EMBL:ADO67798.1"
SQ SEQUENCE 370 AA; 41311 MW; 7154B63A59266CD0 CRC64;
LVLLGLVAFS ECIVKIPLRR VKTMRKTLSG KNILNNFLKE HAYRLSQISS RASNLTFHPL
RNIKDKLYVG NITIGTPPQE FQVIFDTGSS DLWVPSVFCT SPICSTHVMF RHFDSSTFRP
TKKTFSINYG SGRMKGVVVH DTVRIGNLVS TDQPFGLSMA ELGFDGIPFD GVMGLNYPKL
SFSGAIPIFD KLKNEGAISE PVFAFYLSKD KQEGSVVMFG GVDHHYYKGE LNWIPLIQAG
DWSVHMDRIS MKRKVIACSG GCEAVVDTGT SVIEGPRRLV NNIQKHIGAM PRGSEHYVSC
SAVNTLPPII FTINGIDYPV PAQAYILKDS RGHCYTTFEQ NKVSSSTETW ILGDVFLRWY
FSVFDRGNDR
//
