PAG1_BOVIN
ID PAG1_BOVIN Reviewed; 380 AA.
AC Q29432; A7YWR8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Pregnancy-associated glycoprotein 1;
DE Short=PAG 1;
DE EC=3.4.23.-;
DE AltName: Full=Pregnancy-specific protein B;
DE Short=PSP-B;
DE Flags: Precursor;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 54-73.
RC TISSUE=Placenta;
RX PubMed=1946444; DOI=10.1073/pnas.88.22.10247;
RA Xie S., Low B.G., Nagel R.J., Kramer K.K., Anthony R.V., Zoli A.P.,
RA Beckers J.-F.M.P., Roberts R.M.;
RT "Identification of the major pregnancy-specific antigens of cattle and
RT sheep as inactive members of the aspartic proteinase family.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:10247-10251(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7622048; DOI=10.1016/0378-1119(94)00928-l;
RA Xie S., Green J., Beckers J.-F.M.P., Roberts R.M.;
RT "The gene encoding bovine pregnancy-associated glycoprotein-1, an inactive
RT member of the aspartic proteinase family.";
RL Gene 159:193-197(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Placenta;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 54-68, AND GLYCOSYLATION AT ASN-57.
RX PubMed=15822115; DOI=10.1002/mrd.20296;
RA Klisch K., De Sousa N.M., Beckers J.F., Leiser R., Pich A.;
RT "Pregnancy associated glycoprotein-1, -6, -7, and -17 are major products of
RT bovine binucleate trophoblast giant cells at midpregnancy.";
RL Mol. Reprod. Dev. 71:453-460(2005).
RN [5]
RP GLYCOSYLATION.
RX PubMed=17071780; DOI=10.1530/rep-06-0040;
RA Klisch K., Boos A., Friedrich M., Herzog K., Feldmann M., Sousa N.,
RA Beckers J., Leiser R., Schuler G.;
RT "The glycosylation of pregnancy-associated glycoproteins and prolactin-
RT related protein-I in bovine binucleate trophoblast giant cells changes
RT before parturition.";
RL Reproduction 132:791-798(2006).
CC -!- FUNCTION: Appears to be proteolytically inactive.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Trophoblast and placental tissue. Produced
CC specifically in the invasive binucleate cells of the placenta. Becomes
CC detectable in maternal serum soon after implantation.
CC -!- PTM: N-Glycosylated; the glycans terminate in either N-acetyl-
CC galactosamine (GalNAc) or N-acetyllactosamine (PubMed:17071780,
CC PubMed:15822115). Terminal GalNAc on Asn-linked glycans is greatly
CC reduced prior to parturition while lactosamine-type N-glycans remain
CC unaltered (PubMed:17071780). {ECO:0000269|PubMed:15822115,
CC ECO:0000269|PubMed:17071780}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; M73962; AAB53145.1; -; mRNA.
DR EMBL; L27832; AAA96331.1; -; Genomic_DNA.
DR EMBL; L27833; AAA96331.1; JOINED; Genomic_DNA.
DR EMBL; L27834; AAA96331.1; JOINED; Genomic_DNA.
DR EMBL; BC134743; AAI34744.1; -; mRNA.
DR PIR; B41545; B41545.
DR RefSeq; NP_776836.1; NM_174411.2.
DR AlphaFoldDB; Q29432; -.
DR SMR; Q29432; -.
DR STRING; 9913.ENSBTAP00000055271; -.
DR MEROPS; A01.089; -.
DR iPTMnet; Q29432; -.
DR PaxDb; Q29432; -.
DR PRIDE; Q29432; -.
DR GeneID; 281964; -.
DR KEGG; bta:281964; -.
DR CTD; 55824; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_0_1; -.
DR InParanoid; Q29432; -.
DR OrthoDB; 1619495at2759; -.
DR TreeFam; TF314990; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR Gene3D; 2.40.70.10; -; 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; PTHR47966; 1.
DR Pfam; PF07966; A1_Propeptide; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Protease; Reference proteome; Secreted; Signal; Zymogen.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT PROPEP 16..53
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:1946444"
FT /id="PRO_0000026099"
FT CHAIN 54..380
FT /note="Pregnancy-associated glycoprotein 1"
FT /id="PRO_0000026100"
FT DOMAIN 71..377
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15822115"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:15822115"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:15822115"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:15822115"
FT DISULFID 102..107
FT /evidence="ECO:0000250"
FT DISULFID 261..265
FT /evidence="ECO:0000250"
FT DISULFID 303..337
FT /evidence="ECO:0000250"
FT CONFLICT 56
FT /note="S -> H (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 60..61
FT /note="TH -> PG (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="I -> F (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 42847 MW; 77D6FFED68C445B6 CRC64;
MKWLVLLGLV AFSECIVKIP LRRLKTMRNV VSGKNMLNNF LKEHAYSLSQ ISFRGSNLTT
HPLRNIKDLV YMGNITIGTP PQEFQVVFDT ASSDLWVPSD FCTSPACSTH VRFRHLQSST
FRLTNKTFRI TYGSGRMKGV VVHDTVRIGN LVSTDQPFGL SIEEYGFEGR IYDGVLGLNY
PNISFSGAIP IFDKLKNQRA ISEPVFAFYL SKDEREGSVV MFGGVDHRYY EGELNWVPLI
QAGDWSVHMD RISIERKIIA CSDGCKALVD TGTSDIVGPR RLVNNIHRLI GAIPRGSEHY
VPCSEVNTLP SIVFTINGIN YPVPGRAYIL KDDRGRCYTT FQENRVSSST ETWYLGDVFL
RLYFSVFDRG NDRIGLARAV
