PRL_SHEEP
ID PRL_SHEEP Reviewed; 229 AA.
AC P01240; Q28587;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Prolactin;
DE Short=PRL;
DE Flags: Precursor;
GN Name=PRL;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=2911473; DOI=10.1093/nar/17.1.440;
RA Adams T.E., Baker L., Brandon M.R.;
RT "Cloning and nucleotide sequence of an ovine prolactin cDNA.";
RL Nucleic Acids Res. 17:440-440(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=2666265; DOI=10.1016/0378-1119(89)90083-8;
RA Varma S., Kwok S., Ebner K.E.;
RT "Cloning and nucleotide sequence of ovine prolactin cDNA.";
RL Gene 77:349-359(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7969789; DOI=10.1159/000126763;
RA le Provost F., Leroux C., Martin P., Gaye P., Djiane J.;
RT "Prolactin gene expression in ovine and caprine mammary gland.";
RL Neuroendocrinology 60:305-313(1994).
RN [4]
RP PROTEIN SEQUENCE OF 31-229.
RX PubMed=5497153; DOI=10.1016/0003-9861(70)90191-8;
RA Li C.H., Dixon J.S., Lo T.-B., Schmidt K.D., Pankov Y.A.;
RT "Studies on pituitary lactogenic hormone. XXX. The primary structure of the
RT sheep hormone.";
RL Arch. Biochem. Biophys. 141:705-737(1970).
RN [5]
RP SEQUENCE REVISION.
RX PubMed=1270193; DOI=10.1111/j.1399-3011.1976.tb02497.x;
RA Li C.H.;
RT "Studies on pituitary lactogenic hormone. The primary structure of the
RT porcine hormone.";
RL Int. J. Pept. Protein Res. 8:205-224(1976).
CC -!- FUNCTION: Prolactin acts primarily on the mammary gland by promoting
CC lactation, mammogenesis, mitogenesis and osmoregulation.
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=AAA31578.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X13483; CAA31839.1; -; mRNA.
DR EMBL; M27057; AAA31578.1; ALT_INIT; mRNA.
DR EMBL; X76050; CAA53635.1; -; mRNA.
DR PIR; I83983; LCSH.
DR RefSeq; NP_001009306.1; NM_001009306.1.
DR AlphaFoldDB; P01240; -.
DR SMR; P01240; -.
DR STRING; 9940.ENSOARP00000009811; -.
DR iPTMnet; P01240; -.
DR PRIDE; P01240; -.
DR Ensembl; ENSOART00020022305; ENSOARP00020018474; ENSOARG00020014542.
DR Ensembl; ENSOART00020024133; ENSOARP00020020005; ENSOARG00020015585.
DR GeneID; 443317; -.
DR KEGG; oas:443317; -.
DR CTD; 5617; -.
DR eggNOG; ENOG502QYU3; Eukaryota.
DR OrthoDB; 1290070at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISS:AgBase.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0005148; F:prolactin receptor binding; IDA:AgBase.
DR GO; GO:0009058; P:biosynthetic process; ISS:AgBase.
DR GO; GO:0001825; P:blastocyst formation; ISS:AgBase.
DR GO; GO:0007595; P:lactation; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:AgBase.
DR GO; GO:0033685; P:negative regulation of luteinizing hormone secretion; IMP:AgBase.
DR GO; GO:0010751; P:negative regulation of nitric oxide mediated signal transduction; ISS:AgBase.
DR GO; GO:0090278; P:negative regulation of peptide hormone secretion; IDA:AgBase.
DR GO; GO:0030072; P:peptide hormone secretion; IDA:AgBase.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IDA:AgBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
DR GO; GO:1903489; P:positive regulation of lactation; ISS:AgBase.
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; Glycoprotein; Hormone;
KW Lactation; Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:5497153"
FT CHAIN 31..229
FT /note="Prolactin"
FT /id="PRO_0000032926"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01239"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01239"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01239"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine; partial"
FT DISULFID 34..41
FT /evidence="ECO:0000269|PubMed:1270193"
FT DISULFID 88..204
FT /evidence="ECO:0000269|PubMed:1270193"
FT DISULFID 221..229
FT /evidence="ECO:0000269|PubMed:1270193"
FT CONFLICT 40
FT /note="N -> D (in Ref. 2; AAA31578)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 229 AA; 25778 MW; 97FD8AF2991B9B39 CRC64;
MDSKGSAQKG SRLLLLLVVS NLLLCQGVVS TPVCPNGPGN CQVSLRDLFD RAVMVSHYIH
NLSSEMFNEF DKRYAQGKGF ITMALNSCHT SSLPTPEDKE QAQQTHHEVL MSLILGLLRS
WNDPLYHLVT EVRGMKGVPD AILSRAIEIE EENKRLLEGM EMIFGQVIPG AKETEPYPVW
SGLPSLQTKD EDARHSAFYN LLHCLRRDSS KIDTYLKLLN CRIIYNNNC
