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Prolactin (PRL)

 PRL_BOVIN               Reviewed;         229 AA.
P01239; A6QLX8; Q29417; Q95112;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
23-MAY-2018, entry version 139.
RecName: Full=Prolactin;
Short=PRL;
Flags: Precursor;
Name=PRL;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6274859;
Sasavage N.L., Nilson J.H., Horowitz S., Rottman F.M.;
"Nucleotide sequence of bovine prolactin messenger RNA. Evidence for
sequence polymorphism.";
J. Biol. Chem. 257:678-681(1982).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Blood;
PubMed=12561222;
Cao X., Wang Q., Yan J.B., Yang F.K., Huang S.Z., Zeng Y.T.;
"Molecular cloning and analysis of bovine prolactin full-long genomic
as well as cDNA sequences.";
Yi Chuan Xue Bao 29:768-773(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Fetal medulla;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-68 AND 96-229.
Rubtsov P.M., Oganesyan R.G., Gorbulev V.G., Skryabin K.G., Baev A.A.;
"Genetic engineering of peptide hormones. II. Possible polymorphism of
preprolactin in cattle. Data of molecular cloning.";
Mol. Biol. (Mosk.) 22:117-127(1988).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-38.
PubMed=6086257; DOI=10.1089/dna.1.1984.3.237;
Camper S.A., Luck D.N., Yao Y., Woychik R.P., Goodwin R.G.,
Lyons R.H., Rottman F.M.;
"Characterization of the bovine prolactin gene.";
DNA 3:237-249(1984).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 21-229.
PubMed=6299665; DOI=10.1089/dna.1.1981.1.37;
Miller W.L., Coit D., Baxter J.D., Martial J.A.;
"Cloning of bovine prolactin cDNA and evolutionary implications of its
sequence.";
DNA 1:37-50(1981).
[7]
SEQUENCE REVISION.
PubMed=6897772; DOI=10.1089/dna.1.1982.1.313;
Miller W.L., Coit D., Baxter J.D., Martial J.A.;
"Bovine prolactin: corrected cDNA sequence and genetic
polymorphisms.";
DNA 1:313-314(1982).
[8]
PRELIMINARY PROTEIN SEQUENCE OF 31-229.
PubMed=4608931; DOI=10.1016/0014-5793(74)80726-X;
Wallis M.;
"The primary structure of bovine prolactin.";
FEBS Lett. 44:205-208(1974).
[9]
PROTEIN SEQUENCE OF 31-46.
PubMed=5507606;
Graf L., Cseh G., Nagy I., Kurcz M.;
"An evidence for deamidation of prolactin monomer.";
Acta Biochim. Biophys. Acad. Sci. Hung. 5:299-303(1970).
[10]
PROTEIN SEQUENCE OF 52-72 AND 120-133, AND PHOSPHORYLATION AT SER-56;
SER-64 AND SER-120.
TISSUE=Pituitary;
PubMed=8250856; DOI=10.1042/bj2960041;
Kim B.G., Brooks C.L.;
"Isolation and characterization of phosphorylated bovine prolactin.";
Biochem. J. 296:41-47(1993).
-!- FUNCTION: Prolactin acts primarily on the mammary gland by
promoting lactation.
-!- SUBCELLULAR LOCATION: Secreted.
-!- SIMILARITY: Belongs to the somatotropin/prolactin family.
{ECO:0000305}.
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EMBL; V00112; CAA23446.1; -; mRNA.
EMBL; BC148124; AAI48125.1; -; mRNA.
EMBL; AF426315; AAL28075.1; -; Genomic_DNA.
EMBL; M36873; AAA30737.1; -; mRNA.
EMBL; M36874; AAA30738.1; -; mRNA.
EMBL; X14320; CAA32500.1; -; mRNA.
EMBL; X14321; CAA32501.1; -; mRNA.
EMBL; X01452; CAB57794.1; -; Genomic_DNA.
EMBL; X01744; CAA25880.1; -; Genomic_DNA.
PIR; A92378; LCBO.
RefSeq; NP_776378.2; NM_173953.2.
UniGene; Bt.7197; -.
PDB; 3JC2; EM; 3.60 A; w=12-30.
PDBsum; 3JC2; -.
ProteinModelPortal; P01239; -.
SMR; P01239; -.
STRING; 9913.ENSBTAP00000020313; -.
iPTMnet; P01239; -.
PaxDb; P01239; -.
PRIDE; P01239; -.
Ensembl; ENSBTAT00000020313; ENSBTAP00000020313; ENSBTAG00000015274.
GeneID; 280901; -.
KEGG; bta:280901; -.
CTD; 5617; -.
eggNOG; ENOG410II74; Eukaryota.
eggNOG; ENOG410XU1S; LUCA.
GeneTree; ENSGT00730000110805; -.
HOGENOM; HOG000264241; -.
HOVERGEN; HBG104895; -.
InParanoid; P01239; -.
KO; K05439; -.
OMA; DSHKIDN; -.
OrthoDB; EOG091G0O08; -.
TreeFam; TF332592; -.
Reactome; R-BTA-1170546; Prolactin receptor signaling.
Reactome; R-BTA-982772; Growth hormone receptor signaling.
Proteomes; UP000009136; Chromosome 23.
Bgee; ENSBTAG00000015274; -.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:AgBase.
GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
GO; GO:0005148; F:prolactin receptor binding; ISS:AgBase.
GO; GO:0009058; P:biosynthetic process; IDA:AgBase.
GO; GO:0001825; P:blastocyst formation; IDA:AgBase.
GO; GO:0007595; P:lactation; IEA:UniProtKB-KW.
GO; GO:0048571; P:long-day photoperiodism; IDA:AgBase.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:AgBase.
GO; GO:0010629; P:negative regulation of gene expression; IMP:AgBase.
GO; GO:0010751; P:negative regulation of nitric oxide mediated signal transduction; IMP:AgBase.
GO; GO:0030072; P:peptide hormone secretion; ISS:AgBase.
GO; GO:0045807; P:positive regulation of endocytosis; IMP:AgBase.
GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; ISS:AgBase.
GO; GO:0010628; P:positive regulation of gene expression; IMP:AgBase.
GO; GO:1903489; P:positive regulation of lactation; IMP:AgBase.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:AgBase.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IMP:AgBase.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:AgBase.
GO; GO:1903538; P:regulation of meiotic cell cycle process involved in oocyte maturation; IDA:AgBase.
GO; GO:0043207; P:response to external biotic stimulus; IDA:AgBase.
GO; GO:0032094; P:response to food; IDA:AgBase.
GO; GO:1903576; P:response to L-arginine; IDA:AgBase.
GO; GO:0009612; P:response to mechanical stimulus; IDA:AgBase.
GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IMP:AgBase.
InterPro; IPR009079; 4_helix_cytokine-like_core.
InterPro; IPR001400; Somatotropin/Prolactin.
InterPro; IPR018116; Somatotropin_CS.
PANTHER; PTHR11417; PTHR11417; 1.
Pfam; PF00103; Hormone_1; 1.
PRINTS; PR00836; SOMATOTROPIN.
SUPFAM; SSF47266; SSF47266; 1.
PROSITE; PS00266; SOMATOTROPIN_1; 1.
PROSITE; PS00338; SOMATOTROPIN_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Hormone; Lactation; Phosphoprotein;
Reference proteome; Secreted; Signal.
SIGNAL 1 30 {ECO:0000269|PubMed:5507606}.
CHAIN 31 229 Prolactin.
/FTId=PRO_0000032911.
MOD_RES 56 56 Phosphoserine.
{ECO:0000269|PubMed:8250856}.
MOD_RES 64 64 Phosphoserine.
{ECO:0000269|PubMed:8250856}.
MOD_RES 120 120 Phosphoserine.
{ECO:0000269|PubMed:8250856}.
DISULFID 34 41 {ECO:0000269|PubMed:4608931}.
DISULFID 88 204 {ECO:0000269|PubMed:4608931}.
DISULFID 221 229 {ECO:0000269|PubMed:4608931}.
CONFLICT 61 61 D -> N (in Ref. 8; AA sequence).
{ECO:0000305}.
SEQUENCE 229 AA; 25793 MW; E7E9BB6655A26F3D CRC64;
MDSKGSSQKG SRLLLLLVVS NLLLCQGVVS TPVCPNGPGN CQVSLRDLFD RAVMVSHYIH
DLSSEMFNEF DKRYAQGKGF ITMALNSCHT SSLPTPEDKE QAQQTHHEVL MSLILGLLRS
WNDPLYHLVT EVRGMKGAPD AILSRAIEIE EENKRLLEGM EMIFGQVIPG AKETEPYPVW
SGLPSLQTKD EDARYSAFYN LLHCLRRDSS KIDTYLKLLN CRIIYNNNC


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