PRL_MONDO
ID PRL_MONDO Reviewed; 228 AA.
AC O62819;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Prolactin;
DE Short=PRL;
DE Flags: Precursor;
GN Name=PRL;
OS Monodelphis domestica (Gray short-tailed opossum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX NCBI_TaxID=13616;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RA Kacsoh B., Soos G.;
RT "Cloning and characterization of pituitary prolactin cDNA from the
RT marsupial Monodelphis domestica.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
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; AF067726; AAC18398.1; -; mRNA.
DR RefSeq; NP_001028166.1; NM_001032994.1.
DR AlphaFoldDB; O62819; -.
DR SMR; O62819; -.
DR STRING; 13616.ENSMODP00000014194; -.
DR GeneID; 100017831; -.
DR KEGG; mdo:100017831; -.
DR CTD; 5617; -.
DR eggNOG; ENOG502QYU3; Eukaryota.
DR InParanoid; O62819; -.
DR OrthoDB; 1290070at2759; -.
DR Proteomes; UP000002280; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0007595; P:lactation; IEA:UniProtKB-KW.
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; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000250"
FT CHAIN 30..228
FT /note="Prolactin"
FT /id="PRO_0000032920"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01239"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01239"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01239"
FT DISULFID 33..40
FT /evidence="ECO:0000250"
FT DISULFID 87..203
FT /evidence="ECO:0000250"
FT DISULFID 220..228
FT /evidence="ECO:0000250"
SQ SEQUENCE 228 AA; 26071 MW; 4DA2D906EF333EA9 CRC64;
MCPKGSSVKG SLLLLLLMSS RFLFKAVESL PICPSGAVNC QVSLSDLFDR AVMLSHYIHS
PSSEMFNEFD ERYAQGRGFI TKAINSCHTS SLSTPEDKEQ AQQIRHEDLL NLVLRVLRSW
SEPLYHLVTE VRSMQEAPDT ILLKAMEIEE QNKRLLEGME KIVGQVHPGD RENEVYSVWS
GLPSLQMADE DTRLFAFYNL LHCLRRDSHK IDNYLKLLKC RLIHDSNC