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PRL_CEREL
ID   PRL_CEREL               Reviewed;         229 AA.
AC   Q6UC74;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Prolactin;
DE            Short=PRL;
DE   Flags: Precursor;
GN   Name=PRL;
OS   Cervus elaphus (Red deer).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC   Cervinae; Cervus.
OX   NCBI_TaxID=9860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=12742553; DOI=10.1016/s0739-7240(03)00013-4;
RA   Clark R.J., Valderrama X.P., Furlan M.A., Chedrese P.J.;
RT   "Cloning and nucleotide sequence of the equine and elk pituitary pre-
RT   prolactin cDNA.";
RL   Domest. Anim. Endocrinol. 24:367-376(2003).
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}.
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DR   EMBL; AY373035; AAQ76549.1; -; mRNA.
DR   AlphaFoldDB; Q6UC74; -.
DR   SMR; Q6UC74; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0005148; F:prolactin receptor binding; ISS:AgBase.
DR   GO; GO:0007595; P:lactation; IEA:UniProtKB-KW.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:AgBase.
DR   GO; GO:0030072; P:peptide hormone secretion; ISS:AgBase.
DR   GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; ISS:AgBase.
DR   GO; GO:0010628; P:positive regulation of gene expression; 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   2: Evidence at transcript level;
KW   Disulfide bond; Hormone; Lactation; Phosphoprotein; Secreted; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000250"
FT   CHAIN           31..229
FT                   /note="Prolactin"
FT                   /id="PRO_0000032913"
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   DISULFID        34..41
FT                   /evidence="ECO:0000250"
FT   DISULFID        88..204
FT                   /evidence="ECO:0000250"
FT   DISULFID        221..229
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   229 AA;  25794 MW;  0E3F2F021136E4F1 CRC64;
     MDSKVSSQKG SRLLLLLVVS NLLLCQGVVS TPVCPNGAGN CQVSLRDLFD RAVMVSHYIH
     NLSSEMFNEF DKRYAQGKGF ITMALNSCHT SSLPTPEDKE QAQQTHHEVL MSLILGLLRS
     WNDPLYHLVT EVRGMKGAPD GILSRAIEIE EENKRLLEGM EMIFGQVLPG AKETEPYPVW
     SGLPSLQTKD EDARYSAFYN LLHCLRRDSS KIDTYLKLLN CRIIYNNNC
 
 
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