ID   PLRP1_BOVIN             Reviewed;         238 AA.
AC   P05402; A6QPR5;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Placental prolactin-related protein 1;
DE            Short=PRC-I;
DE   AltName: Full=bPRCI;
DE   Flags: Precursor;
GN   Name=PRP1;
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=3475696; DOI=10.1073/pnas.84.16.5650;
RA   Schuler L.A., Hurley W.L.;
RT   "Molecular cloning of a prolactin-related mRNA expressed in bovine
RT   placenta.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:5650-5654(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2721368; DOI=10.1089/dna.1.1989.8.161;
RA   Ebbitt D.M., Hurley W.L., Kessler M.A., McDonald D.J., Schuler L.A.;
RT   "Characterization of the gene corresponding to bovine placental prolactin-
RT   related cDNA I: evolutionary implications.";
RL   DNA 8:161-169(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Placenta;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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: Placental prolactin-related proteins may play a specific role
CC       during gestation.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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 somatotropin/prolactin family.
CC       {ECO:0000305}.
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DR   EMBL; J02944; AAA30726.1; -; mRNA.
DR   EMBL; M25494; AAA30727.1; -; Genomic_DNA.
DR   EMBL; M25491; AAA30727.1; JOINED; Genomic_DNA.
DR   EMBL; M25492; AAA30727.1; JOINED; Genomic_DNA.
DR   EMBL; M25493; AAA30727.1; JOINED; Genomic_DNA.
DR   EMBL; BC149446; AAI49447.1; -; mRNA.
DR   PIR; A31417; A31417.
DR   RefSeq; NP_776584.1; NM_174159.2.
DR   AlphaFoldDB; P05402; -.
DR   SMR; P05402; -.
DR   STRING; 9913.ENSBTAP00000045299; -.
DR   iPTMnet; P05402; -.
DR   PaxDb; P05402; -.
DR   GeneID; 281429; -.
DR   KEGG; bta:281429; -.
DR   CTD; 373417; -.
DR   eggNOG; ENOG502QYU3; Eukaryota.
DR   HOGENOM; CLU_088274_0_1_1; -.
DR   InParanoid; P05402; -.
DR   OrthoDB; 1290070at2759; -.
DR   TreeFam; TF332592; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005179; F:hormone activity; IBA:GO_Central.
DR   GO; GO:0005148; F:prolactin receptor binding; IBA:GO_Central.
DR   GO; GO:0007565; P:female pregnancy; IBA:GO_Central.
DR   GO; GO:0030879; P:mammary gland development; IBA:GO_Central.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:1903489; P:positive regulation of lactation; IBA:GO_Central.
DR   GO; GO:0009893; P:positive regulation of metabolic process; IEA:UniProt.
DR   GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR   GO; GO:0031667; P:response to nutrient levels; IBA:GO_Central.
DR   Gene3D; 1.20.1250.10; -; 1.
DR   InterPro; IPR009079; 4_helix_cytokine-like_core.
DR   InterPro; IPR001400; Somatotropin/Prolactin.
DR   InterPro; IPR018116; Somatotropin_CS.
DR   PANTHER; PTHR11417; PTHR11417; 1.
DR   Pfam; PF00103; Hormone_1; 1.
DR   PRINTS; PR00836; SOMATOTROPIN.
DR   SUPFAM; SSF47266; SSF47266; 1.
DR   PROSITE; PS00266; SOMATOTROPIN_1; 1.
DR   PROSITE; PS00338; SOMATOTROPIN_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Hormone; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000255"
FT   CHAIN           37..238
FT                   /note="Placental prolactin-related protein 1"
FT                   /id="PRO_0000032949"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305|PubMed:17071780"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305|PubMed:17071780"
FT   DISULFID        97..215
FT                   /evidence="ECO:0000250"
FT   DISULFID        232..238
FT                   /evidence="ECO:0000250"
FT   CONFLICT        201
FT                   /note="D -> A (in Ref. 1; AAA30726)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   238 AA;  27719 MW;  AD3609F025B9FF78 CRC64;
     MAPAPSFRGH QWTYNPVRGS CLLLLLLMSN LLLCQGKSCP SCGPDVFVSL RKSFTDRFMN
     AASLSHDFYN LSTIMFNEFD EKYAQGKLYY INVTKSCHTN SFHAPEERDI VQQTNIEDLS
     KWTLVLLYSW NNPLHHLVTE LQHMKELSNA FLSSATRFEN MSEKLQAFIE RQFSKIIVPV
     LNTMIQARSS WTGLPSLMSS DEDRRHSEFY NLFYCLRRDS RKVDMYIKIL TCRTHKTC