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P01236 (PRL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prolactin

Short name=PRL
Gene names
Name:PRL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length227 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Prolactin acts primarily on the mammary gland by promoting lactation.

Subcellular location

Secreted.

Sequence similarities

Belongs to the somatotropin/prolactin family.

Sequence caution

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRLRP16471-74EBI-6903064,EBI-6903057

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Ref.7 Ref.8
Chain29 – 227199Prolactin
PRO_0000032916

Amino acid modifications

Modified residue541Phosphoserine By similarity
Modified residue621Phosphoserine By similarity
Modified residue1181Phosphoserine By similarity
Modified residue1631Phosphoserine Ref.9
Modified residue1941Phosphoserine Ref.9
Glycosylation591N-linked (GlcNAc...); partial
Disulfide bond32 ↔ 39 Ref.13
Disulfide bond86 ↔ 202 Ref.13
Disulfide bond219 ↔ 227 Ref.13

Experimental info

Mutagenesis1571G → D, F, L, N, R, V or Y: Inhibits signaling via PRLR; mutant PRL acts as PRLR antagonist. Ref.12
Sequence conflict421T → A in AAB70858. Ref.6
Sequence conflict110 – 1112SL → VS AA sequence Ref.7
Sequence conflict113 – 1142VS → L AA sequence Ref.7
Sequence conflict1181S → P in AAB70858. Ref.6
Sequence conflict1481E → Q in BAA00312. Ref.5
Sequence conflict1721N → D AA sequence Ref.7
Sequence conflict190 – 1912ES → SE AA sequence Ref.7
Sequence conflict2061D → H in AAA60173. Ref.5
Sequence conflict2061D → H in BAA00312. Ref.5

Secondary structure

......................... 227
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01236 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 952BBA1B6A955527

FASTA22725,876
        10         20         30         40         50         60 
MNIKGSPWKG SLLLLLVSNL LLCQSVAPLP ICPGGAARCQ VTLRDLFDRA VVLSHYIHNL 

        70         80         90        100        110        120 
SSEMFSEFDK RYTHGRGFIT KAINSCHTSS LATPEDKEQA QQMNQKDFLS LIVSILRSWN 

       130        140        150        160        170        180 
EPLYHLVTEV RGMQEAPEAI LSKAVEIEEQ TKRLLEGMEL IVSQVHPETK ENEIYPVWSG 

       190        200        210        220 
LPSLQMADEE SRLSAYYNLL HCLRRDSHKI DNYLKLLKCR IIHNNNC 

« Hide

References

« Hide 'large scale' references
[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]"A placenta-specific 5'non-coding exon of human prolactin."
Hiraoka Y., Tatsumi K., Shiozawa M., Aiso S., Fukasawa T., Yasuda K., Miyai K.
Mol. Cell. Endocrinol. 75:71-80(1991) [PubMed] [Europe PMC] [Abstract]
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]"Solution structure of human prolactin."
Teilum K., Hoch J.C., Goffin V., Kinet S., Martial J.A., Kragelund B.B.
J. Mol. Biol. 351:810-823(2005) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Wikipedia

Prolactin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00566 mRNA. Translation: CAA23829.1.
X00540 expand/collapse EMBL AC list , 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.
CCDSCCDS4548.1.
PIRA61402.
LCHU. A90998.
RefSeqNP_000939.1. NM_000948.5.
NP_001157030.1. NM_001163558.2.
UniGeneHs.1905.
Hs.735971.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP01236.
SMRP01236. Positions 29-227.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111602. 2 interactions.
DIPDIP-59635N.
IntActP01236. 1 interaction.
STRING9606.ENSP00000302150.

PTM databases

PhosphoSiteP01236.

Proteomic databases

PaxDbP01236.
PRIDEP01236.

Protocols and materials databases

DNASU5617.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306482; ENSP00000302150; ENSG00000172179.
GeneID5617.
KEGGhsa:5617.
UCSCuc003ndp.3. human.

Organism-specific databases

CTD5617.
GeneCardsGC06M022230.
HGNCHGNC:9445. PRL.
HPACAB023353.
MIM176760. gene.
neXtProtNX_P01236.
PharmGKBPA33790.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47376.
HOGENOMHOG000264241.
HOVERGENHBG104895.
KOK05439.
OMAYSVWSGL.
OrthoDBEOG74FF24.
PhylomeDBP01236.
TreeFamTF332592.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkP01236.

Gene expression databases

ArrayExpressP01236.
BgeeP01236.
CleanExHS_PRL.
GenevestigatorP01236.

Family and domain databases

Gene3D1.20.1250.10. 1 hit.
InterProIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR001400. Somatotropin.
IPR018116. Somatotropin_CS.
[Graphical view]
PANTHERPTHR11417. PTHR11417. 1 hit.
PfamPF00103. Hormone_1. 1 hit.
[Graphical view]
PRINTSPR00836. SOMATOTROPIN.
SUPFAMSSF47266. SSF47266. 1 hit.
PROSITEPS00266. SOMATOTROPIN_1. 1 hit.
PS00338. SOMATOTROPIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRL. human.
EvolutionaryTraceP01236.
GeneWikiProlactin.
GenomeRNAi5617.
NextBio21828.
PMAP-CutDBP01236.
PROP01236.
SOURCESearch...

Entry information

Entry namePRL_HUMAN
AccessionPrimary (citable) accession number: P01236
Secondary accession number(s): Q15199, Q92996
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM