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Protein

Prolactin

Gene

PRL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Prolactin acts primarily on the mammary gland by promoting lactation.

GO - Molecular functioni

  • prolactin receptor binding Source: ProtInc

GO - Biological processi

  • cell proliferation Source: ProtInc
  • cell surface receptor signaling pathway Source: ProtInc
  • female pregnancy Source: ProtInc
  • JAK-STAT cascade involved in growth hormone signaling pathway Source: Reactome
  • lactation Source: UniProtKB-KW
  • positive regulation of JAK-STAT cascade Source: BHF-UCL
  • regulation of multicellular organism growth Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hormone

Keywords - Biological processi

Lactation

Enzyme and pathway databases

ReactomeiREACT_111133. Growth hormone receptor signaling.
REACT_115697. Prolactin receptor signaling.
REACT_75925. Amyloids.
SignaLinkiP01236.

Names & Taxonomyi

Protein namesi
Recommended name:
Prolactin
Short name:
PRL
Gene namesi
Name:PRL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:9445. PRL.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi157 – 1571G → D, F, L, N, R, V or Y: Inhibits signaling via PRLR; mutant PRL acts as PRLR antagonist. 1 Publication

Organism-specific databases

PharmGKBiPA33790.

Polymorphism and mutation databases

BioMutaiPRL.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 28282 PublicationsAdd
BLAST
Chaini29 – 227199ProlactinPRO_0000032916Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi32 ↔ 391 Publication
Modified residuei54 – 541PhosphoserineBy similarity
Glycosylationi59 – 591N-linked (GlcNAc...); partial
Modified residuei62 – 621PhosphoserineBy similarity
Disulfide bondi86 ↔ 2021 Publication
Modified residuei118 – 1181PhosphoserineBy similarity
Modified residuei163 – 1631Phosphoserine1 Publication
Modified residuei194 – 1941Phosphoserine1 Publication
Disulfide bondi219 ↔ 2271 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP01236.
PRIDEiP01236.

PTM databases

PhosphoSiteiP01236.

Miscellaneous databases

PMAP-CutDBP01236.

Expressioni

Gene expression databases

BgeeiP01236.
CleanExiHS_PRL.
ExpressionAtlasiP01236. baseline and differential.
GenevisibleiP01236. HS.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
PRLRP16471-74EBI-6903064,EBI-6903057

Protein-protein interaction databases

BioGridi111602. 3 interactions.
DIPiDIP-59635N.
IntActiP01236. 1 interaction.
STRINGi9606.ENSP00000302150.

Structurei

Secondary structure

1
227
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 344Combined sources
Helixi43 – 7230Combined sources
Turni73 – 753Combined sources
Helixi78 – 825Combined sources
Turni87 – 904Combined sources
Helixi97 – 1026Combined sources
Helixi105 – 11814Combined sources
Helixi120 – 13112Combined sources
Beta strandi133 – 1353Combined sources
Helixi138 – 16528Combined sources
Beta strandi166 – 1683Combined sources
Helixi181 – 1855Combined sources
Helixi189 – 22335Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RW5NMR-A29-227[»]
2Q98X-ray2.70A38-227[»]
3D48X-ray2.50P40-227[»]
3EW3X-ray3.80A39-227[»]
3MZGX-ray2.10A43-227[»]
3N06X-ray2.00A43-227[»]
3N0PX-ray2.10A43-227[»]
3NCBX-ray2.10A43-227[»]
3NCCX-ray2.50A43-227[»]
3NCEX-ray2.00A43-227[»]
3NCFX-ray2.80A43-227[»]
3NPZX-ray3.35A29-227[»]
ProteinModelPortaliP01236.
SMRiP01236. Positions 29-227.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01236.

Family & Domainsi

Sequence similaritiesi

Belongs to the somatotropin/prolactin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG47376.
HOGENOMiHOG000264241.
HOVERGENiHBG104895.
InParanoidiP01236.
KOiK05439.
OMAiLHCLRRD.
OrthoDBiEOG74FF24.
PhylomeDBiP01236.
TreeFamiTF332592.

Family and domain databases

Gene3Di1.20.1250.10. 1 hit.
InterProiIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR001400. Somatotropin.
IPR018116. Somatotropin_CS.
[Graphical view]
PANTHERiPTHR11417. PTHR11417. 1 hit.
PfamiPF00103. Hormone_1. 1 hit.
[Graphical view]
PRINTSiPR00836. SOMATOTROPIN.
SUPFAMiSSF47266. SSF47266. 1 hit.
PROSITEiPS00266. SOMATOTROPIN_1. 1 hit.
PS00338. SOMATOTROPIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01236-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIKGSPWKG SLLLLLVSNL LLCQSVAPLP ICPGGAARCQ VTLRDLFDRA
60 70 80 90 100
VVLSHYIHNL SSEMFSEFDK RYTHGRGFIT KAINSCHTSS LATPEDKEQA
110 120 130 140 150
QQMNQKDFLS LIVSILRSWN EPLYHLVTEV RGMQEAPEAI LSKAVEIEEQ
160 170 180 190 200
TKRLLEGMEL IVSQVHPETK ENEIYPVWSG LPSLQMADEE SRLSAYYNLL
210 220
HCLRRDSHKI DNYLKLLKCR IIHNNNC
Length:227
Mass (Da):25,876
Last modified:July 21, 1986 - v1
Checksum:i952BBA1B6A955527
GO

Sequence cautioni

The sequence CAA38264.1 differs from that shown. Reason: Frameshift at position 8. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421T → A in AAB70858 (PubMed:9266104).Curated
Sequence conflicti110 – 1112SL → VS AA sequence (PubMed:925136).Curated
Sequence conflicti113 – 1142VS → L AA sequence (PubMed:925136).Curated
Sequence conflicti118 – 1181S → P in AAB70858 (PubMed:9266104).Curated
Sequence conflicti148 – 1481E → Q in BAA00312 (PubMed:6146607).Curated
Sequence conflicti172 – 1721N → D AA sequence (PubMed:925136).Curated
Sequence conflicti190 – 1912ES → SE AA sequence (PubMed:925136).Curated
Sequence conflicti206 – 2061D → H in AAA60173 (PubMed:6146607).Curated
Sequence conflicti206 – 2061D → H in BAA00312 (PubMed:6146607).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00566 mRNA. Translation: CAA23829.1.
X00540
, X00541, X00543, X00544 Genomic DNA. Translation: CAA25214.1.
X54393 mRNA. Translation: CAA38263.1. Frameshift.
X54393 mRNA. Translation: CAA38264.1. Frameshift.
BC015850 mRNA. Translation: AAH15850.1.
M29386 mRNA. Translation: AAA60173.1.
D00411 mRNA. Translation: BAA00312.1.
U75583 mRNA. Translation: AAB70858.1.
CCDSiCCDS4548.1.
PIRiA61402.
A90998. LCHU.
RefSeqiNP_000939.1. NM_000948.5.
NP_001157030.1. NM_001163558.2.
UniGeneiHs.1905.
Hs.735971.

Genome annotation databases

EnsembliENST00000306482; ENSP00000302150; ENSG00000172179.
GeneIDi5617.
KEGGihsa:5617.
UCSCiuc003ndp.3. human.

Cross-referencesi

Web resourcesi

Wikipedia

Prolactin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00566 mRNA. Translation: CAA23829.1.
X00540
, X00541, X00543, X00544 Genomic DNA. Translation: CAA25214.1.
X54393 mRNA. Translation: CAA38263.1. Frameshift.
X54393 mRNA. Translation: CAA38264.1. Frameshift.
BC015850 mRNA. Translation: AAH15850.1.
M29386 mRNA. Translation: AAA60173.1.
D00411 mRNA. Translation: BAA00312.1.
U75583 mRNA. Translation: AAB70858.1.
CCDSiCCDS4548.1.
PIRiA61402.
A90998. LCHU.
RefSeqiNP_000939.1. NM_000948.5.
NP_001157030.1. NM_001163558.2.
UniGeneiHs.1905.
Hs.735971.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RW5NMR-A29-227[»]
2Q98X-ray2.70A38-227[»]
3D48X-ray2.50P40-227[»]
3EW3X-ray3.80A39-227[»]
3MZGX-ray2.10A43-227[»]
3N06X-ray2.00A43-227[»]
3N0PX-ray2.10A43-227[»]
3NCBX-ray2.10A43-227[»]
3NCCX-ray2.50A43-227[»]
3NCEX-ray2.00A43-227[»]
3NCFX-ray2.80A43-227[»]
3NPZX-ray3.35A29-227[»]
ProteinModelPortaliP01236.
SMRiP01236. Positions 29-227.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111602. 3 interactions.
DIPiDIP-59635N.
IntActiP01236. 1 interaction.
STRINGi9606.ENSP00000302150.

PTM databases

PhosphoSiteiP01236.

Polymorphism and mutation databases

BioMutaiPRL.

Proteomic databases

PaxDbiP01236.
PRIDEiP01236.

Protocols and materials databases

DNASUi5617.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000306482; ENSP00000302150; ENSG00000172179.
GeneIDi5617.
KEGGihsa:5617.
UCSCiuc003ndp.3. human.

Organism-specific databases

CTDi5617.
GeneCardsiGC06M022230.
HGNCiHGNC:9445. PRL.
MIMi176760. gene.
neXtProtiNX_P01236.
PharmGKBiPA33790.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG47376.
HOGENOMiHOG000264241.
HOVERGENiHBG104895.
InParanoidiP01236.
KOiK05439.
OMAiLHCLRRD.
OrthoDBiEOG74FF24.
PhylomeDBiP01236.
TreeFamiTF332592.

Enzyme and pathway databases

ReactomeiREACT_111133. Growth hormone receptor signaling.
REACT_115697. Prolactin receptor signaling.
REACT_75925. Amyloids.
SignaLinkiP01236.

Miscellaneous databases

ChiTaRSiPRL. human.
EvolutionaryTraceiP01236.
GeneWikiiProlactin.
GenomeRNAii5617.
NextBioi21828.
PMAP-CutDBP01236.
PROiP01236.
SOURCEiSearch...

Gene expression databases

BgeeiP01236.
CleanExiHS_PRL.
ExpressionAtlasiP01236. baseline and differential.
GenevisibleiP01236. HS.

Family and domain databases

Gene3Di1.20.1250.10. 1 hit.
InterProiIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR001400. Somatotropin.
IPR018116. Somatotropin_CS.
[Graphical view]
PANTHERiPTHR11417. PTHR11417. 1 hit.
PfamiPF00103. Hormone_1. 1 hit.
[Graphical view]
PRINTSiPR00836. SOMATOTROPIN.
SUPFAMiSSF47266. SSF47266. 1 hit.
PROSITEiPS00266. SOMATOTROPIN_1. 1 hit.
PS00338. SOMATOTROPIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human prolactin. cDNA structural analysis and evolutionary comparisons."
    Cooke N.E., Coit D., Shine J., Baxter J.D., Martial J.A.
    J. Biol. Chem. 256:4007-4016(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Isolation and characterization of the human prolactin gene."
    Truong A.T., Duez C., Belayew A., Renard A., Pictet R.L., Bell G.I., Martial J.A.
    EMBO J. 3:429-437(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  5. "Molecular cloning and nucleotide sequence of DNA complementary to human decidual prolactin mRNA."
    Takahashi H., Nabeshima Y., Nabeshima Y., Ogata K., Takeuchi S.
    J. Biochem. 95:1491-1499(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-227.
  6. "Expression of the prolactin gene in normal and neoplastic human breast tissues and human mammary cell lines: promoter usage and alternative mRNA splicing."
    Shaw-Bruha C.M., Pirrucello S.J., Shull J.D.
    Breast Cancer Res. Treat. 44:243-253(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-201.
    Tissue: Mammary gland.
  7. "Human pituitary prolactin (hPRL): the entire linear amino acid sequence."
    Shome B., Parlow A.F.
    J. Clin. Endocrinol. Metab. 45:1112-1115(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-227.
  8. "High sensitivity automated sequence determination of polypeptides."
    Jacobs J.W., Niall H.D.
    J. Biol. Chem. 250:3629-3636(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-53.
  9. "Immunoglobulin G subclasses and prolactin (PRL) isoforms in macroprolactinemia due to anti-PRL autoantibodies."
    Hattori N., Ikekubo K., Nakaya Y., Kitagawa K., Inagaki C.
    J. Clin. Endocrinol. Metab. 90:3036-3044(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-163 AND SER-194.
  10. "The tertiary structure and backbone dynamics of human prolactin."
    Keeler C., Dannies P.S., Hodsdon M.E.
    J. Mol. Biol. 328:1105-1121(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 29-227.
  11. Cited for: STRUCTURE BY NMR OF 29-227, INTERACTION WITH PRLR.
  12. "Structural and thermodynamic bases for the design of pure prolactin receptor antagonists: X-ray structure of Del1-9-G129R-hPRL."
    Jomain J.-B., Tallet E., Broutin I., Hoos S., van Agthoven J., Ducruix A., Kelly P.A., Kragelund B.B., England P., Goffin V.
    J. Biol. Chem. 282:33118-33131(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 38-227, MUTAGENESIS OF GLY-157.
  13. "Crystal structure of a prolactin receptor antagonist bound to the extracellular domain of the prolactin receptor."
    Svensson L.A., Bondensgaard K., Noerskov-Lauritsen L., Christensen L., Becker P., Andersen M.D., Maltesen M.J., Rand K.D., Breinholt J.
    J. Biol. Chem. 283:19085-19094(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 41-227 IN COMPLEX WITH PRLR, IDENTIFICATION BY MASS SPECTROMETRY, DISULFIDE BONDS.

Entry informationi

Entry nameiPRL_HUMAN
AccessioniPrimary (citable) accession number: P01236
Secondary accession number(s): Q15199, Q92996
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 24, 2015
This is version 159 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.