ID E3UMS8_BUBBU Unreviewed; 367 AA.
AC E3UMS8;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Pregnancy-associated glycoprotein 2 variant {ECO:0000313|EMBL:ADO67791.1};
DE Flags: Fragment;
GN Name=PAG2 {ECO:0000313|EMBL:ADO67791.1};
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:ADO67791.1};
RN [1] {ECO:0000313|EMBL:ADO67791.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Placental cotyledons {ECO:0000313|EMBL:ADO67791.1};
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}.
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DR EMBL; HM468471; ADO67791.1; -; mRNA.
DR AlphaFoldDB; E3UMS8; -.
DR SMR; E3UMS8; -.
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; 2.
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 65..367
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 83
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 264
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 96..101
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 255..259
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 297..330
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADO67791.1"
FT NON_TER 367
FT /evidence="ECO:0000313|EMBL:ADO67791.1"
SQ SEQUENCE 367 AA; 40805 MW; FBC138B67E941041 CRC64;
LVLLGLVALS ECIVILPLRK MKTLRETLRE KNLLNNFLEE QTYRLSKNDS KITIHPLRNY
LDTAYVGNIT IGTPPQEFRV VFDTGSANLW VPCITCTSPA CYTHNTFNPQ KSSSFRDAGS
PITIFYGSGI IQGFLGSDTV RIGNLVSPEQ SFGLSLVEYG FDSVPFDGIL GLAFPSMGIK
DTIPIFDNLW SHGAFSEPVF AFYLNTNKPE GSVVMFGGVD HRYYKGELNW IPVSQTSHWQ
ISMNNISMNG NVTACSCGCQ ALLDTGTSLI YGPTELVTNI HKLMNAKPKD SEYVVSCDAV
KTLPPVIFNI NGIDYPLPPQ AYIIKIQNSC RSVFQGGTEN SSLDTWILGD IFLRQYFSVF
DRKNKRI
//
