PRL_HORSE
ID PRL_HORSE Reviewed; 229 AA.
AC P12420; Q6UBP9;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Prolactin;
DE Short=PRL;
DE Flags: Precursor;
GN Name=PRL;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
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).
RN [2]
RP PROTEIN SEQUENCE OF 31-229.
RC TISSUE=Pituitary;
RX PubMed=3045032; DOI=10.1111/j.1399-3011.1988.tb00913.x;
RA Lehrman S.R., Lahm H.W., Miedel M.C., Hulmes J.D., Li C.H.;
RT "Primary structure of equine pituitary prolactin.";
RL Int. J. Pept. Protein Res. 31:544-554(1988).
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; AY373339; AAQ76548.1; -; mRNA.
DR PIR; JK0016; LCHO.
DR RefSeq; NP_001075365.1; NM_001081896.1.
DR AlphaFoldDB; P12420; -.
DR SMR; P12420; -.
DR STRING; 9796.ENSECAP00000000120; -.
DR PaxDb; P12420; -.
DR GeneID; 100034034; -.
DR KEGG; ecb:100034034; -.
DR CTD; 5617; -.
DR HOGENOM; CLU_088274_0_1_1; -.
DR InParanoid; P12420; -.
DR Proteomes; UP000002281; 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:0007595; P:lactation; IEA:UniProtKB-KW.
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: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 Direct protein sequencing; Disulfide bond; Glycoprotein; Hormone;
KW Lactation; Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:3045032"
FT CHAIN 31..229
FT /note="Prolactin"
FT /id="PRO_0000032915"
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:0000250"
FT DISULFID 88..204
FT /evidence="ECO:0000250"
FT DISULFID 221..229
FT /evidence="ECO:0000250"
FT CONFLICT 119
FT /note="R -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 229 AA; 26256 MW; A7B891BA9ADE737C CRC64;
MDKKRSSLKG SLLLLLLLVS DLLLCKSVAS LPICPSGAVN CQVSLRELFD RAVILSHYIH
NLSSEMFNEF DKRYAQGRGF VTKAINSCHT SSLSTPEDKE QAQQIHHEDL LNLILRVLRS
WNDPLYHLVS EVRGMQEAPE AILSKAIEIE EQNRRLLEGM EKIVGQVQPR IKENEVYSVW
SGLPSLQMAD EDSRLFAFYN LLHCLRRDSH KIDNYLKLLK CRIVYDSNC