ID   PRL_MELGA               Reviewed;         229 AA.
AC   P17572;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Prolactin;
DE            Short=PRL;
DE   Flags: Precursor;
GN   Name=PRL;
OS   Meleagris gallopavo (Wild turkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Meleagridinae; Meleagris.
OX   NCBI_TaxID=9103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=8618952; DOI=10.3181/00379727-212-43991;
RA   Xu M., Proudman J.A., Pitts G.R., Wong E.A., Foster D.N., el Halawani M.E.;
RT   "Vasoactive intestinal peptide stimulates prolactin mRNA expression in
RT   turkey pituitary cells: effects of dopaminergic drugs.";
RL   Proc. Soc. Exp. Biol. Med. 212:52-62(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=1879669; DOI=10.1016/0016-6480(91)90101-b;
RA   Wong E.A., Ferrin N.H., Silsby J.L., el Halawani M.E.;
RT   "Cloning of a turkey prolactin cDNA: expression of prolactin mRNA
RT   throughout the reproductive cycle of the domestic turkey (Meleagris
RT   gallopavo).";
RL   Gen. Comp. Endocrinol. 83:18-26(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 66-229.
RC   TISSUE=Pituitary;
RX   PubMed=2349117; DOI=10.1093/nar/18.10.3071;
RA   Karatzas C.N., Zadworny D., Kuhnlein U.;
RT   "Nucleotide sequence of turkey prolactin.";
RL   Nucleic Acids Res. 18:3071-3071(1990).
RN   [4]
RP   PROTEIN SEQUENCE OF 31-70, AND GLYCOSYLATION.
RX   PubMed=1769204; DOI=10.1016/0305-0491(91)90338-e;
RA   Corcoran D.H., Proudman J.A.;
RT   "Isoforms of turkey prolactin: evidence for differences in glycosylation
RT   and in tryptic peptide mapping.";
RL   Comp. Biochem. Physiol. 99B:563-570(1991).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Three forms are found, non-glycosylated, glycosylated and one form
CC       seems to be only O-glycosylated. {ECO:0000269|PubMed:1769204}.
CC   -!- SIMILARITY: Belongs to the somatotropin/prolactin family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U05957; AAB60615.1; -; Genomic_DNA.
DR   EMBL; U05953; AAB60615.1; JOINED; Genomic_DNA.
DR   EMBL; U05954; AAB60615.1; JOINED; Genomic_DNA.
DR   EMBL; U05955; AAB60615.1; JOINED; Genomic_DNA.
DR   EMBL; U05952; AAB60604.1; -; mRNA.
DR   EMBL; X51769; CAA36071.1; -; mRNA.
DR   PIR; A61133; A61133.
DR   RefSeq; NP_001290115.1; NM_001303186.1.
DR   AlphaFoldDB; P17572; -.
DR   SMR; P17572; -.
DR   Ensembl; ENSMGAT00000002760; ENSMGAP00000002087; ENSMGAG00000002476.
DR   GeneID; 100303694; -.
DR   KEGG; mgp:100303694; -.
DR   CTD; 5617; -.
DR   GeneTree; ENSGT00950000182818; -.
DR   HOGENOM; CLU_088274_0_1_1; -.
DR   InParanoid; P17572; -.
DR   OMA; NEVYSRW; -.
DR   OrthoDB; 1290070at2759; -.
DR   TreeFam; TF332592; -.
DR   Proteomes; UP000001645; Chromosome 3.
DR   GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR   GO; GO:0005125; F:cytokine activity; TAS:AgBase.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0006703; P:estrogen biosynthetic process; TAS:AgBase.
DR   GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0009648; P:photoperiodism; TAS:AgBase.
DR   GO; GO:1902895; P:positive regulation of miRNA transcription; IEA:Ensembl.
DR   GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR   GO; GO:0070459; P:prolactin secretion; TAS:AgBase.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0051602; P:response to electrical stimulus; IMP: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   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000269|PubMed:1769204"
FT   CHAIN           31..229
FT                   /note="Prolactin"
FT                   /id="PRO_0000032929"
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        156
FT                   /note="L -> R (in Ref. 2; AAB60604)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   229 AA;  25854 MW;  DEA530EB2301F2B7 CRC64;
     MSNTGASLKG LLLAVLLVSN MLLTKEGVTS LPICSSGSVN CQVSLGELFD RAVRLSHYIH
     FLSSEIFNEF DERYAQGRGF ITKAVNGCHT SSLTTPEDKE QTQQIHHEEL LNLILGVLRS
     WNDPLIHLAS EVQRIKEAPD TILWKAVEIE EQNKRLLEGM EKIVGRIHSG DAGNEVFSQW
     DGLPSLQLAD EDSRLFAFYN LLHCLRRDSH KIDNYLKVLK CRLIHDNNC