ID   PAG1_SHEEP              Reviewed;         382 AA.
AC   Q28755; P83496;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Pregnancy-associated glycoprotein 1;
DE            Short=PAG 1;
DE   AltName: Full=Inactive aspartic protease PAG-1;
DE   AltName: Full=Pregnancy-associated glycoprotein 66d;
DE            Short=ovPAG 66d;
DE   Flags: Precursor;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], ABSENCE OF CATALYTIC ACTIVITY, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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   PROTEIN SEQUENCE OF 54-63, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Fetal cotyledon;
RX   PubMed=15460157; DOI=10.1051/rnd:2004025;
RA   El Amiri B., Remy B., De Sousa N.M., Beckers J.F.;
RT   "Isolation and characterization of eight pregnancy-associated glycoproteins
RT   present at high levels in the ovine placenta between day 60 and day 100 of
RT   gestation.";
RL   Reprod. Nutr. Dev. 44:169-181(2004).
RN   [3]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=10819764; DOI=10.1095/biolreprod62.6.1624;
RA   Green J.A., Xie S., Quan X., Bao B., Gan X., Mathialagan N., Beckers J.F.,
RA   Roberts R.M.;
RT   "Pregnancy-associated bovine and ovine glycoproteins exhibit spatially and
RT   temporally distinct expression patterns during pregnancy.";
RL   Biol. Reprod. 62:1624-1631(2000).
CC   -!- FUNCTION: Has no proteolytic activity.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000269|PubMed:1946444}.
CC   -!- TISSUE SPECIFICITY: Trophoblast and placental tissue. Produced
CC       specifically in the invasive binucleate cells of the placenta.
CC       {ECO:0000269|PubMed:10819764, ECO:0000269|PubMed:15460157,
CC       ECO:0000269|PubMed:1946444}.
CC   -!- DEVELOPMENTAL STAGE: Detected in maternal serum soon after implantation
CC       and throughout the gestation period. {ECO:0000269|PubMed:10819764,
CC       ECO:0000269|PubMed:15460157, ECO:0000269|PubMed:1946444}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
CC   -!- CAUTION: Lacks the conserved Asp active site at position 272.
CC       {ECO:0000305|PubMed:1946444}.
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DR   EMBL; M73961; AAB53144.1; -; mRNA.
DR   PIR; A41545; A41545.
DR   AlphaFoldDB; Q28755; -.
DR   SMR; Q28755; -.
DR   STRING; 9940.ENSOARP00000005629; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   PROPEP          16..53
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:15460157"
FT                   /id="PRO_0000026109"
FT   CHAIN           54..382
FT                   /note="Pregnancy-associated glycoprotein 1"
FT                   /id="PRO_0000026110"
FT   DOMAIN          71..379
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   SITE            272
FT                   /note="Ancestral active site"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        102..110
FT                   /evidence="ECO:0000250"
FT   DISULFID        263..267
FT                   /evidence="ECO:0000250"
FT   DISULFID        305..339
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   382 AA;  42980 MW;  D28E4D78BB5BFE8C CRC64;
     MKWLVLLGLV AFSECIVKIP LRRVKTMRNT LSGKKMLNSF LKEHAYRLSQ ISFRASNLTI
     HPLRNIMDML YVGNITIGTP PQEFQVVFDT GSSDLLVPSI NCLSPTKRPC SKQDKFKHHQ
     SSTFRFTNDT FRIYFGSGTM RGFVAHDTVR IGDLVSTDQP FGLIFLESWL DIPFDGILGL
     NYPKISFSGA IPIFDKLKNE GAFSEPVFAF YLNKDKQEGS VVMFGGVDHR YYKGELNWVP
     LIHPGEWSIP LDRISMRRKV IACSGGCEAL VGTGTSLILG PRTVVENIQK HIGATQQCFE
     YFVSCSAVYA LPSIVFTING INYPVPPQAY LVKDSRGQCY SPFQVNRANP SAENWILGDV
     FLRRYFSVFD RGNDRIGLAR AV