PAG1_PIG
ID PAG1_PIG Reviewed; 389 AA.
AC Q29078;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Pregnancy-associated glycoprotein 1;
DE Short=PAG 1;
DE Short=PAG1;
DE EC=3.4.23.-;
DE Flags: Precursor;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7669851; DOI=10.1095/biolreprod53.1.21;
RA Szafranska B., Xie S., Green J., Roberts R.M.;
RT "Porcine pregnancy-associated glycoproteins: new members of the aspartic
RT proteinase gene family expressed in trophectoderm.";
RL Biol. Reprod. 53:21-28(1995).
CC -!- FUNCTION: Appears to be proteolytically inactive.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Expressed throughout the chorion, with the signal
CC localized exclusively over the trophectoderm.
CC -!- DEVELOPMENTAL STAGE: Expression was detected at day 15, coinciding with
CC the beginning of implantation, and continued throughout gestation.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; L34360; AAA81530.1; -; Genomic_DNA.
DR PIR; I46616; I46616.
DR AlphaFoldDB; Q29078; -.
DR SMR; Q29078; -.
DR STRING; 9823.ENSSSCP00000013930; -.
DR MEROPS; A01.971; -.
DR PaxDb; Q29078; -.
DR eggNOG; KOG1339; Eukaryota.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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 2: Evidence at transcript 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_0000026105"
FT CHAIN ?..389
FT /note="Pregnancy-associated glycoprotein 1"
FT /id="PRO_0000026106"
FT DOMAIN 76..386
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 107..112
FT /evidence="ECO:0000250"
FT DISULFID 268..272
FT /evidence="ECO:0000250"
FT DISULFID 311..345
FT /evidence="ECO:0000250"
SQ SEQUENCE 389 AA; 43533 MW; 764A1D2C17A3F416 CRC64;
MKWLVILGLV ALSECLVIIP LTKVKSIREN LREKDLLLNF LKEHPYNMIQ KFGLKGSLCS
PKISCLRLWN YLDMVYVGNI TIGTPPQLFS VIFDTASSDL WVPSNQCHSR ACVTHRSFNP
TLSSTFQSSN RTVKLAPHSG LVSGLLGYDT VQIGRFKSEN QAFGLSQSEP VKELENAFFD
GVLGLGYPSL AIQGTTPVFD NLRKQGQIPE PVFALYLSTN TKKGSVLMIG GVDNNFFTGN
LKWVPLSARN YWQITLDRIT WRGVVVGCTR GCQAILDSGS AFLLGPSRQI SSIQKIIQAR
FIENEYQVRC CARTTLADFI FTINNVQYPV PARAYIRKGS TPRRCYSNFS GGTESLGKEE
TWILGEVFLR LYFTVFDRGQ NRIGLRIAV