PAG2_BOVIN
ID PAG2_BOVIN Reviewed; 376 AA.
AC Q28057;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Pregnancy-associated glycoprotein 2;
DE Short=PAG 2;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN Name=PAG2;
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].
RC TISSUE=Placenta;
RX PubMed=7534122; DOI=10.1095/biolreprod51.6.1145;
RA Xie S., Low B.G., Nagel R.J., Beckers J.-F.M.P., Roberts R.M.;
RT "A novel glycoprotein of the aspartic proteinase gene family expressed in
RT bovine placental trophectoderm.";
RL Biol. Reprod. 51:1145-1153(1994).
RN [2]
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: PAG2 or a processed derivative of this molecule might
CC represent a factor that binds the LH receptor.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Trophoblast and placental tissue. Localized to both
CC the mononucleate and binucleate cells of the trophectoderm.
CC -!- DEVELOPMENTAL STAGE: Expression is detected at days 17-19, coinciding
CC with the beginning of implantation, and continues throughout gestation.
CC -!- PTM: N-Glycosylated; the glycans terminate in either N-acetyl-
CC galactosamine (GalNAc) or N-acetyllactosamine (PubMed:17071780).
CC Terminal GalNAc on Asn-linked glycans is greatly reduced prior to
CC parturition while lactosamine-type N-glycans remain unaltered
CC (PubMed:17071780). {ECO:0000269|PubMed:17071780}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; L06151; AAA65822.1; -; mRNA.
DR PIR; I45856; I45856.
DR RefSeq; NP_788787.1; NM_176614.1.
DR AlphaFoldDB; Q28057; -.
DR SMR; Q28057; -.
DR STRING; 9913.ENSBTAP00000016233; -.
DR MEROPS; A01.089; -.
DR iPTMnet; Q28057; -.
DR PaxDb; Q28057; -.
DR Ensembl; ENSBTAT00000025517; ENSBTAP00000025517; ENSBTAG00000033096.
DR GeneID; 337897; -.
DR KEGG; bta:337897; -.
DR CTD; 337897; -.
DR VEuPathDB; HostDB:ENSBTAG00000033096; -.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000153747; -.
DR HOGENOM; CLU_013253_3_0_1; -.
DR InParanoid; Q28057; -.
DR OMA; GHEYAVS; -.
DR OrthoDB; 1619495at2759; -.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000033096; Expressed in conceptus and 24 other tissues.
DR ExpressionAtlas; Q28057; baseline.
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; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Signal; Zymogen.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT PROPEP 16..?
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026101"
FT CHAIN ?..376
FT /note="Pregnancy-associated glycoprotein 2"
FT /id="PRO_0000026102"
FT DOMAIN 68..373
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:17071780"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:17071780"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:17071780"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:17071780"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:17071780"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:17071780"
FT DISULFID 99..104
FT /evidence="ECO:0000250"
FT DISULFID 258..262
FT /evidence="ECO:0000250"
FT DISULFID 300..333
FT /evidence="ECO:0000250"
SQ SEQUENCE 376 AA; 41907 MW; 0B68A5B1E232EE60 CRC64;
MKWLVLLGLV ALSECIVILP LKKMKTLRET LREKNLLNNF LEEQAYRLSK NDSKITIHPL
RNYLDTAYVG NITIGTPPQE FRVVFDTGSA NLWVPCITCT SPACYTHKTF NPQNSSSFRE
VGSPITIFYG SGIIQGFLGS DTVRIGNLVS PEQSFGLSLE EYGFDSLPFD GILGLAFPAM
GIEDTIPIFD NLWSHGAFSE PVFAFYLNTN KPEGSVVMFG GVDHRYYKGE LNWIPVSQTS
HWQISMNNIS MNGTVTACSC GCEALLDTGT SMIYGPTKLV TNIHKLMNAR LENSEYVVSC
DAVKTLPPVI FNINGIDYPL RPQAYIIKIQ NSCRSVFQGG TENSSLNTWI LGDIFLRQYF
SVFDRKNRRI GLAPAV
