PRL_PIG
ID PRL_PIG Reviewed; 229 AA.
AC P01238;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 3.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Prolactin;
DE Short=PRL;
DE Flags: Precursor;
GN Name=PRL;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2726463; DOI=10.1093/nar/17.8.3295;
RA Schulz Aellen M.F., Schmid E., Movva R.N.;
RT "Nucleotide sequence of porcine preprolactin cDNA.";
RL Nucleic Acids Res. 17:3295-3295(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2344390; DOI=10.1677/jme.0.0040135;
RA Kato Y., Hirai T., Kato T.;
RT "Molecular cloning of cDNA for porcine prolactin precursor.";
RL J. Mol. Endocrinol. 4:135-142(1990).
RN [3]
RP PROTEIN SEQUENCE OF 31-229.
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.
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; X14068; CAA32231.1; -; mRNA.
DR PIR; S04077; LCPG.
DR RefSeq; NP_999091.1; NM_213926.1.
DR AlphaFoldDB; P01238; -.
DR SMR; P01238; -.
DR STRING; 9823.ENSSSCP00000001152; -.
DR PaxDb; P01238; -.
DR Ensembl; ENSSSCT00005021712; ENSSSCP00005012965; ENSSSCG00005013825.
DR Ensembl; ENSSSCT00025021715; ENSSSCP00025008937; ENSSSCG00025016163.
DR Ensembl; ENSSSCT00030017871; ENSSSCP00030007935; ENSSSCG00030013020.
DR Ensembl; ENSSSCT00035003667; ENSSSCP00035001247; ENSSSCG00035002953.
DR Ensembl; ENSSSCT00040002857; ENSSSCP00040000818; ENSSSCG00040002353.
DR Ensembl; ENSSSCT00045048844; ENSSSCP00045033968; ENSSSCG00045028611.
DR Ensembl; ENSSSCT00050010841; ENSSSCP00050004653; ENSSSCG00050007944.
DR Ensembl; ENSSSCT00055022983; ENSSSCP00055018167; ENSSSCG00055011670.
DR Ensembl; ENSSSCT00060071878; ENSSSCP00060030995; ENSSSCG00060052812.
DR Ensembl; ENSSSCT00065039329; ENSSSCP00065016649; ENSSSCG00065029133.
DR Ensembl; ENSSSCT00070050742; ENSSSCP00070042888; ENSSSCG00070025388.
DR GeneID; 396965; -.
DR KEGG; ssc:396965; -.
DR CTD; 5617; -.
DR eggNOG; ENOG502QYU3; Eukaryota.
DR InParanoid; P01238; -.
DR OrthoDB; 1290070at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 7.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0005179; F:hormone activity; IBA:GO_Central.
DR GO; GO:0005148; F:prolactin receptor binding; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; IMP:AgBase.
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:1904077; P:negative regulation of estrogen biosynthetic process; IMP:AgBase.
DR GO; GO:0010730; P:negative regulation of hydrogen peroxide biosynthetic process; IMP:AgBase.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IMP:AgBase.
DR GO; GO:2000183; P:negative regulation of progesterone biosynthetic process; IMP:AgBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:AgBase.
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:0010575; P:positive regulation of vascular endothelial growth factor production; IMP:AgBase.
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:1270193"
FT CHAIN 31..229
FT /note="Prolactin"
FT /id="PRO_0000032923"
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 DISULFID 88..204
FT DISULFID 221..229
FT CONFLICT 4
FT /note="R -> T (in Ref. 1; CAA32231)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="V -> M (in Ref. 1; CAA32231)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="Q -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="D -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 229 AA; 26141 MW; 9D8507EE6DA33B47 CRC64;
MDNRGSSQKG SLLLLLLLVS NLFLCKSVAS LPICPSGAVN CQVSLRDLFD RAVILSHYIH
NLSSEMFNEF DKRYAQGRGF ITKAINSCHT SSLSTPEDKE QAQQIHHEVL LNLILRVLRS
WNDPLYHLVT EVRGMQEAPD AILSRAIEIE EQNKRLLEGM EKIVGQVHPG IKENEVYSVW
SGLPSLQMAD EDTRLFAFYN LLHCLRRDSH KIDNYLKLLK CRIIYDSNC
