PRL_RAT
ID PRL_RAT Reviewed; 226 AA.
AC P01237; P70520;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Prolactin;
DE Short=PRL;
DE Flags: Precursor;
GN Name=Prl;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6283362; DOI=10.1038/297603a0;
RA Cooke N.E., Baxter J.D.;
RT "Structural analysis of the prolactin gene suggests a separate origin for
RT its 5' end.";
RL Nature 297:603-606(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6251061; DOI=10.1016/s0021-9258(18)43550-8;
RA Gubbins E.J., Maurer R.A., Lagrimini M., Erwin C.R., Donelson J.E.;
RT "Structure of the rat prolactin gene.";
RL J. Biol. Chem. 255:8655-8662(1980).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6993473; DOI=10.1016/s0021-9258(18)43768-4;
RA Cooke N.E., Coit D.C., Weiner R.I., Baxter J.D., Martial J.A.;
RT "Structure of cloned DNA complementary to rat prolactin messenger RNA.";
RL J. Biol. Chem. 255:6502-6510(1980).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Wistar; TISSUE=Pituitary tumor;
RA Shaw-Bruha C.M., Pennington K.L., Shull J.D.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 1-29 (PRECURSOR PROTEIN).
RX PubMed=728396; DOI=10.1021/bi00617a022;
RA McKean D.J., Maurer R.A.;
RT "Complete amino acid sequence of the precursor region of rat prolactin.";
RL Biochemistry 17:5215-5219(1978).
RN [6]
RP PROTEIN SEQUENCE OF 30-226.
RX PubMed=925136; DOI=10.1210/jcem-45-5-1112;
RA Shome B., Parlow A.F.;
RT "Human pituitary prolactin (hPRL): the entire linear amino acid sequence.";
RL J. Clin. Endocrinol. Metab. 45:1112-1115(1977).
CC -!- FUNCTION: Prolactin acts primarily on the mammary gland by promoting
CC lactation.
CC -!- SUBUNIT: Interacts with PRLR. {ECO:0000250|UniProtKB:P01236}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the somatotropin/prolactin family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=Ref.6; Type=Miscellaneous discrepancy; Note=Differs at a number of positions and in the total number of residues.; Evidence={ECO:0000305};
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DR EMBL; V01244; CAA24561.1; -; Genomic_DNA.
DR EMBL; V01245; CAA24561.1; JOINED; Genomic_DNA.
DR EMBL; V01246; CAA24561.1; JOINED; Genomic_DNA.
DR EMBL; V01247; CAA24561.1; JOINED; Genomic_DNA.
DR EMBL; V01248; CAA24561.1; JOINED; Genomic_DNA.
DR EMBL; J00769; AAA41939.1; -; Genomic_DNA.
DR EMBL; J00766; AAA41939.1; JOINED; Genomic_DNA.
DR EMBL; J00767; AAA41939.1; JOINED; Genomic_DNA.
DR EMBL; J00768; AAA41939.1; JOINED; Genomic_DNA.
DR EMBL; V01249; CAA24562.1; -; mRNA.
DR EMBL; AF022935; AAC78688.1; -; mRNA.
DR PIR; A93279; LCRT.
DR RefSeq; NP_036761.1; NM_012629.1.
DR AlphaFoldDB; P01237; -.
DR SMR; P01237; -.
DR STRING; 10116.ENSRNOP00000023412; -.
DR iPTMnet; P01237; -.
DR PhosphoSitePlus; P01237; -.
DR PaxDb; P01237; -.
DR PRIDE; P01237; -.
DR GeneID; 24683; -.
DR KEGG; rno:24683; -.
DR UCSC; RGD:3403; rat.
DR CTD; 5617; -.
DR RGD; 3403; Prl.
DR VEuPathDB; HostDB:ENSRNOG00000017374; -.
DR eggNOG; ENOG502QYU3; Eukaryota.
DR HOGENOM; CLU_088274_0_1_1; -.
DR InParanoid; P01237; -.
DR OMA; NEVYSRW; -.
DR OrthoDB; 1290070at2759; -.
DR PhylomeDB; P01237; -.
DR TreeFam; TF332592; -.
DR Reactome; R-RNO-1170546; Prolactin receptor signaling.
DR Reactome; R-RNO-982772; Growth hormone receptor signaling.
DR PRO; PR:P01237; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000017374; Expressed in Ammon's horn.
DR ExpressionAtlas; P01237; baseline and differential.
DR Genevisible; P01237; RN.
DR GO; GO:0005576; C:extracellular region; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0005179; F:hormone activity; IBA:GO_Central.
DR GO; GO:0005148; F:prolactin receptor binding; IBA:GO_Central.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
DR GO; GO:0007623; P:circadian rhythm; IEP:RGD.
DR GO; GO:0007565; P:female pregnancy; IBA:GO_Central.
DR GO; GO:0007595; P:lactation; TAS:RGD.
DR GO; GO:0030879; P:mammary gland development; ISO:RGD.
DR GO; GO:0042711; P:maternal behavior; ISO:RGD.
DR GO; GO:0033555; P:multicellular organismal response to stress; IEP:RGD.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:RGD.
DR GO; GO:0042698; P:ovulation cycle; IEP:RGD.
DR GO; GO:0007567; P:parturition; IEP:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:RGD.
DR GO; GO:1903489; P:positive regulation of lactation; IBA:GO_Central.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:RGD.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISO:RGD.
DR GO; GO:0040014; P:regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0030278; P:regulation of ossification; IMP:RGD.
DR GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; ISO:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IBA:GO_Central.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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 Direct protein sequencing; Disulfide bond; Hormone; Lactation;
KW Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:728396,
FT ECO:0000269|PubMed:925136"
FT CHAIN 30..226
FT /note="Prolactin"
FT /id="PRO_0000032925"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01239"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01239"
FT DISULFID 33..38
FT /evidence="ECO:0000250"
FT DISULFID 85..201
FT /evidence="ECO:0000250"
FT DISULFID 218..226
FT /evidence="ECO:0000250"
FT CONFLICT 10
FT /note="Missing (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="S -> G (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="Q -> QE (in Ref. 1; CAA24561)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 226 AA; 25753 MW; 755E2874A26862C7 CRC64;
MNSQVSARKA GTLLLLMMSN LLFCQNVQTL PVCSGGDCQT PLPELFDRVV MLSHYIHTLY
TDMFIEFDKQ YVQDREFIAK AINDCPTSSL ATPEDKEQAQ KVPPEVLLNL ILSLVHSWND
PLFQLITGLG GIHEAPDAII SRAKEIEEQN KRLLEGIEKI ISQAYPEAKG NEIYLVWSQL
PSLQGVDEES KDLAFYNNIR CLRRDSHKVD NYLKFLRCQI VHKNNC
