Prolactin precursor - Homo sapiens (Human)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P01236 (PRL_HUMAN)

Last modified June 16, 2009. Version 104. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
Prolactin
Short name=PRL

Gene names

Name:

PRL

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length	227 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

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.

Hide | Top

Ontologies

Keywords
Biological process	Lactation
Cellular component	Secreted
Domain	Signal
Molecular function	Hormone
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell proliferation Traceable author statement. Source: ProtInc cell surface receptor linked signal transduction Traceable author statement. Source: ProtInc female pregnancy Non-traceable author statement. Source: ProtInc lactation Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of JAK-STAT cascade Inferred from direct assay. Source: UniProtKB regulation of multicellular organism growth Inferred from expression pattern. Source: UniProtKB
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	hormone activity Inferred from electronic annotation. Source: UniProtKB-KW prolactin receptor binding Traceable author statement. Source: ProtInc
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

Ref.7 Ref.8

Chain

29 – 227

199

Prolactin

PRO_0000032916

Amino acid modifications

Glycosylation

N-linked (GlcNAc...); partial

Disulfide bond

Disulfide bond

Disulfide bond

Experimental info

Mutagenesis

157

G → D, F, L, N, R, V or Y: Inhibits signaling via PRLR; mutant PRL acts as PRLR antagonist. Ref.11

Sequence conflict

T → A in AAB70858. Ref.6

Sequence conflict

110 – 111

SL → VS AA sequence Ref.7

Sequence conflict

113 – 114

VS → L AA sequence Ref.7

Sequence conflict

118

S → P in AAB70858. Ref.6

Sequence conflict

148

E → Q in BAA00312. Ref.5

Sequence conflict

172

N → D AA sequence Ref.7

Sequence conflict

190 – 191

ES → SE AA sequence Ref.7

Sequence conflict

206

D → H in AAA60173. Ref.5

Sequence conflict

206

D → H in BAA00312. Ref.5

Secondary structure

227

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P01236-1 [UniParc].

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

FASTA

227

25,876

        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

Hide | Top

References

	« Hide 'large scale' referencesShow '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: 6260780] [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: 6325171] [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: 2050267] [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: 15489334] [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: 6146607] [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: 9266104] [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: 925136] [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: 1126929] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-53.
[9]	"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: 12729745] [Abstract] Cited for: STRUCTURE BY NMR OF 29-227.
[10]	"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: 16045928] [Abstract] Cited for: STRUCTURE BY NMR OF 29-227, INTERACTION WITH PRLR.
[11]	"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: 17785459] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 38-227, MUTAGENESIS OF GLY-157.
[12]	"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: 18467331] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 41-227 IN COMPLEX WITH PRLR, MASS SPECTROMETRY, DISULFIDE BONDS.
+	Additional computationally mapped references.

Hide | Top

Web resources

Wikipedia

Prolactin entry

Hide | Top

Cross-references

Sequence databases

V00566 mRNA. Translation: CAA23829.1.
X00540

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.

IPI

IPI00873653.

PIR

A61402.
LCHU. A90998.

RefSeq

NP_000939.1.

UniGene

Hs.1905

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1N9D	NMR	-	A	29-227	[»]
1RW5	NMR	-	A	29-227	[»]
2Q98	X-ray	2.70	A	40-227	[»]
3D48	X-ray	2.50	P	41-227	[»]

ModBase

Search...

PTM databases

PhosphoSite

P01236.

Genome annotation databases

Ensembl

ENSG00000172179. Homo sapiens. [Contig view]

GeneID

5617.

KEGG

hsa:5617.

Organism-specific databases

GeneCards

GC06M022395.

H-InvDB

HIX0005617.

HGNC

HGNC:9445. PRL.

MIM

176760. gene.

PharmGKB

PA33790.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P01236.

Enzyme and pathway databases

Pathway_Interaction_DB

ptp1bpathway. Signaling events mediated by PTP1B.

Gene expression databases

ArrayExpress

P01236.

Bgee

P01236.

CleanEx

HS_PRL.

GermOnline

ENSG00000172179. Homo sapiens.

Family and domain databases

InterPro

IPR012351. 4_helix_cytokine_core.
IPR001400. Somatotropin.
IPR018116. Somatotropin_CS.
[Graphical view]

Gene3D

G3DSA:1.20.1250.10. 4_helix_cytokine_core. 1 hit.

PANTHER

PTHR11417. Somatotropin. 1 hit.

Pfam

PF00103. Hormone_1. 1 hit.
[Graphical view]

PRINTS

PR00836. SOMATOTROPIN.

PROSITE

PS00266. SOMATOTROPIN_1. 1 hit.
PS00338. SOMATOTROPIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

21828.

PMAP-CutDB

P01236.

SOURCE

Search...

Hide | Top

Entry information

Entry name

PRL_HUMAN

Accession

Primary (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:	June 16, 2009
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top