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Protein

Prolactin receptor

Gene

PRLR

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

Functioni

This is a receptor for the anterior pituitary hormone prolactin (PRL). Acts as a prosurvival factor for spermatozoa by inhibiting sperm capacitation through suppression of SRC kinase activation and stimulation of AKT. Isoform 4 is unable to transduce prolactin signaling. Isoform 6 is unable to transduce prolactin signaling.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi211 – 2111Zinc
Metal bindingi212 – 2121Zinc

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • ornithine decarboxylase activator activity Source: UniProtKB
  • peptide hormone binding Source: BHF-UCL
  • prolactin receptor activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • activation of JAK2 kinase activity Source: UniProtKB
  • activation of transmembrane receptor protein tyrosine kinase activity Source: UniProtKB
  • cell surface receptor signaling pathway Source: UniProtKB
  • embryo implantation Source: ProtInc
  • JAK-STAT cascade involved in growth hormone signaling pathway Source: Reactome
  • lactation Source: UniProtKB
  • mammary gland alveolus development Source: Ensembl
  • mammary gland epithelial cell differentiation Source: Ensembl
  • negative regulation of apoptotic process Source: UniProtKB
  • prostate gland growth Source: Ensembl
  • regulation of cell adhesion Source: Ensembl
  • regulation of epithelial cell differentiation Source: Ensembl
  • steroid biosynthetic process Source: UniProtKB
  • T cell activation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_111133. Growth hormone receptor signaling.
REACT_115697. Prolactin receptor signaling.
SignaLinkiP16471.

Names & Taxonomyi

Protein namesi
Recommended name:
Prolactin receptor
Short name:
PRL-R
Gene namesi
Name:PRLR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:9446. PRLR.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 234210ExtracellularSequence AnalysisAdd
BLAST
Transmembranei235 – 25824HelicalSequence AnalysisAdd
BLAST
Topological domaini259 – 622364CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Multiple fibroadenomas of the breast (MFAB)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA benign breast disease marked by lobuloalveolar growth with abnormally high proliferation of the epithelium, and characterized by the presence of more than 3 fibroadenomas in one breast. Fibroadenomas are adenomas containing fibrous tissue.

See also OMIM:615554
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti170 – 1701I → L in MFAB; confers constitutive activity. 1 Publication
VAR_070894
Hyperprolactinemia (HPRL)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder characterized by increased levels of prolactin in the blood not associated with gestation or the puerperium. HPRL may result in infertility, hypogonadism, and galactorrhea.

See also OMIM:615555
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti212 – 2121H → R in HPRL; loss of function. 1 Publication
VAR_070895

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615554. phenotype.
615555. phenotype.
Orphaneti397685. Familial hyperprolactinemia.
50920. Multiple fibroadenoma of the breast.
PharmGKBiPA33791.

Chemistry

DrugBankiDB01185. Fluoxymesterone.
DB00052. Somatropin recombinant.

Polymorphism and mutation databases

BioMutaiPRLR.
DMDMi130321.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Add
BLAST
Chaini25 – 622598Prolactin receptorPRO_0000010977Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi36 ↔ 461 Publication
Glycosylationi59 – 591N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi75 ↔ 861 Publication
Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP16471.
PRIDEiP16471.

PTM databases

PhosphoSiteiP16471.

Expressioni

Tissue specificityi

Expressed in breast, placenta, kidney, liver and pancreas.2 Publications

Gene expression databases

BgeeiP16471.
CleanExiHS_PRLR.
ExpressionAtlasiP16471. baseline and differential.
GenevestigatoriP16471.

Interactioni

Subunit structurei

Homodimer upon hormone binding. Interacts with SMARCA1. Interacts with GH1. Interacts with CSH. Interacts with NEK3 and VAV2 and this interaction is prolactin-dependent.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PRLP012364EBI-6903057,EBI-6903064

Protein-protein interaction databases

BioGridi111603. 14 interactions.
DIPiDIP-288N.
IntActiP16471. 4 interactions.
MINTiMINT-268499.

Structurei

Secondary structure

1
622
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 4211Combined sources
Beta strandi44 – 496Combined sources
Beta strandi52 – 543Combined sources
Beta strandi58 – 669Combined sources
Turni67 – 693Combined sources
Beta strandi85 – 884Combined sources
Helixi90 – 923Combined sources
Beta strandi95 – 973Combined sources
Beta strandi99 – 1079Combined sources
Beta strandi110 – 1134Combined sources
Beta strandi117 – 1193Combined sources
Helixi121 – 1233Combined sources
Beta strandi131 – 1388Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi146 – 1527Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi162 – 1643Combined sources
Beta strandi166 – 1738Combined sources
Beta strandi181 – 1866Combined sources
Beta strandi189 – 1935Combined sources
Beta strandi201 – 21313Combined sources
Beta strandi222 – 2254Combined sources
Helixi230 – 2323Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BP3X-ray2.90B25-235[»]
2LFGNMR-A123-234[»]
3D48X-ray2.50R25-234[»]
3MZGX-ray2.10B26-234[»]
3N06X-ray2.00B26-234[»]
3N0PX-ray2.10B26-234[»]
3NCBX-ray2.10B26-234[»]
3NCCX-ray2.50B26-234[»]
3NCEX-ray2.00B26-234[»]
3NCFX-ray2.80B26-234[»]
4I18X-ray3.24C/R25-235[»]
ProteinModelPortaliP16471.
SMRiP16471. Positions 26-230.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16471.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 128102Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini129 – 229101Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi215 – 2195WSXWS motif
Motifi267 – 2759Box 1 motif

Domaini

The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
The box 1 motif is required for JAK interaction and/or activation.

Sequence similaritiesi

Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG29671.
GeneTreeiENSGT00530000063112.
HOGENOMiHOG000059569.
HOVERGENiHBG007314.
InParanoidiP16471.
KOiK05081.
OMAiSGPNSCY.
OrthoDBiEOG7Q5HCH.
PhylomeDBiP16471.
TreeFamiTF330851.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR003961. FN3_dom.
IPR015152. Growth/epo_recpt_lig-bind.
IPR013783. Ig-like_fold.
IPR003528. Long_hematopoietin_rcpt_CS.
[Graphical view]
PfamiPF09067. EpoR_lig-bind. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 2 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 2 hits.
PS01352. HEMATOPO_REC_L_F1. 1 hit.
[Graphical view]

Sequences (9)i

Sequence statusi: Complete.

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

This entry describes 9 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P16471-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKENVASATV FTLLLFLNTC LLNGQLPPGK PEIFKCRSPN KETFTCWWRP
60 70 80 90 100
GTDGGLPTNY SLTYHREGET LMHECPDYIT GGPNSCHFGK QYTSMWRTYI
110 120 130 140 150
MMVNATNQMG SSFSDELYVD VTYIVQPDPP LELAVEVKQP EDRKPYLWIK
160 170 180 190 200
WSPPTLIDLK TGWFTLLYEI RLKPEKAAEW EIHFAGQQTE FKILSLHPGQ
210 220 230 240 250
KYLVQVRCKP DHGYWSAWSP ATFIQIPSDF TMNDTTVWIS VAVLSAVICL
260 270 280 290 300
IIVWAVALKG YSMVTCIFPP VPGPKIKGFD AHLLEKGKSE ELLSALGCQD
310 320 330 340 350
FPPTSDYEDL LVEYLEVDDS EDQHLMSVHS KEHPSQGMKP TYLDPDTDSG
360 370 380 390 400
RGSCDSPSLL SEKCEEPQAN PSTFYDPEVI EKPENPETTH TWDPQCISME
410 420 430 440 450
GKIPYFHAGG SKCSTWPLPQ PSQHNPRSSY HNITDVCELA VGPAGAPATL
460 470 480 490 500
LNEAGKDALK SSQTIKSREE GKATQQREVE SFHSETDQDT PWLLPQEKTP
510 520 530 540 550
FGSAKPLDYV EIHKVNKDGA LSLLPKQREN SGKPKKPGTP ENNKEYAKVS
560 570 580 590 600
GVMDNNILVL VPDPHAKNVA CFEESAKEAP PSLEQNQAEK ALANFTATSS
610 620
KCRLQLGGLD YLDPACFTHS FH
Length:622
Mass (Da):69,506
Last modified:August 1, 1990 - v1
Checksum:iDB7FD0328608C787
GO
Isoform 2 (identifier: P16471-2) [UniParc]FASTAAdd to basket

Also known as: Delta-S1

The sequence of this isoform differs from the canonical sequence as follows:
     24-124: Missing.

Show »
Length:521
Mass (Da):57,953
Checksum:i1CF312424037E85B
GO
Isoform 3 (identifier: P16471-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     229-230: DF → AW
     231-622: Missing.

Note: Soluble isoform that appears specific for the BT-474 breast cancer cell line.

Show »
Length:230
Mass (Da):26,545
Checksum:i5288BCF71248D291
GO
Isoform 4 (identifier: P16471-4) [UniParc]FASTAAdd to basket

Also known as: SF1a, Short form 1a

The sequence of this isoform differs from the canonical sequence as follows:
     338-376: MKPTYLDPDT...PQANPSTFYD → DPLMLGASHY...FTKATLTTVQ
     377-622: Missing.

Note: Includes exon 11. Does not transduce prolactin signaling.

Show »
Length:376
Mass (Da):42,639
Checksum:i112DC2555FBC4601
GO
Isoform 5 (identifier: P16471-5) [UniParc]FASTAAdd to basket

Also known as: Intermediate

The sequence of this isoform differs from the canonical sequence as follows:
     337-349: GMKPTYLDPDTDS → EREQRQAQEARDS
     350-622: Missing.

Note: Produced by deletion of part of exon 10 and frameshift.

Show »
Length:349
Mass (Da):39,806
Checksum:i932F200E850CDD27
GO
Isoform 6 (identifier: P16471-6) [UniParc]FASTAAdd to basket

Also known as: SF1b, Short form 1b

The sequence of this isoform differs from the canonical sequence as follows:
     286-288: KGK → VTP
     289-622: Missing.

Note: Does not transduce prolactin signaling.

Show »
Length:288
Mass (Da):32,760
Checksum:iB45203EC045EB417
GO
Isoform 7 (identifier: P16471-7) [UniParc]FASTAAdd to basket

Also known as: Delta 7/11

The sequence of this isoform differs from the canonical sequence as follows:
     229-268: DFTMNDTTVW...KGYSMVTCIF → GDPLMLGASH...FTKATLTTVQ
     269-622: Missing.

Note: Splices from exon 7 to exon 11.

Show »
Length:268
Mass (Da):30,705
Checksum:iFBB498AB649A078C
GO
Isoform 8 (identifier: P16471-8) [UniParc]FASTAAdd to basket

Also known as: Delta 4-SF1b

The sequence of this isoform differs from the canonical sequence as follows:
     1-71: Missing.
     286-288: KGK → VTP
     289-622: Missing.

Note: SF1b with deletion of exon 4. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Show »
Length:217
Mass (Da):24,773
Checksum:iE59A9BB9016C3397
GO
Isoform 9 (identifier: P16471-9) [UniParc]FASTAAdd to basket

Also known as: SF1c, Short form 1c

The sequence of this isoform differs from the canonical sequence as follows:
     286-309: KGKSEELLSALGCQDFPPTSDYED → DRLCTPGRCCVSTGLTDLDYSCST
     310-622: Missing.

Show »
Length:309
Mass (Da):35,011
Checksum:i1FC88E4E2F4E9DEB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti100 – 1001I → V.
Corresponds to variant rs2228482 [ dbSNP | Ensembl ].
VAR_049172
Natural varianti170 – 1701I → L in MFAB; confers constitutive activity. 1 Publication
VAR_070894
Natural varianti212 – 2121H → R in HPRL; loss of function. 1 Publication
VAR_070895

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7171Missing in isoform 8. 1 PublicationVSP_026531Add
BLAST
Alternative sequencei24 – 124101Missing in isoform 2. 1 PublicationVSP_001720Add
BLAST
Alternative sequencei229 – 26840DFTMN…VTCIF → GDPLMLGASHYKNLKSYRPR KISSQGRLAVFTKATLTTVQ in isoform 7. 1 PublicationVSP_026532Add
BLAST
Alternative sequencei229 – 2302DF → AW in isoform 3. 1 PublicationVSP_012620
Alternative sequencei231 – 622392Missing in isoform 3. 1 PublicationVSP_012621Add
BLAST
Alternative sequencei269 – 622354Missing in isoform 7. 1 PublicationVSP_026533Add
BLAST
Alternative sequencei286 – 30924KGKSE…SDYED → DRLCTPGRCCVSTGLTDLDY SCST in isoform 9. 1 PublicationVSP_047882Add
BLAST
Alternative sequencei286 – 2883KGK → VTP in isoform 6 and isoform 8. 2 PublicationsVSP_026534
Alternative sequencei289 – 622334Missing in isoform 6 and isoform 8. 2 PublicationsVSP_026535Add
BLAST
Alternative sequencei310 – 622313Missing in isoform 9. 1 PublicationVSP_047883Add
BLAST
Alternative sequencei337 – 34913GMKPT…PDTDS → EREQRQAQEARDS in isoform 5. 1 PublicationVSP_026536Add
BLAST
Alternative sequencei338 – 37639MKPTY…STFYD → DPLMLGASHYKNLKSYRPRK ISSQGRLAVFTKATLTTVQ in isoform 4. 2 PublicationsVSP_026537Add
BLAST
Alternative sequencei350 – 622273Missing in isoform 5. 1 PublicationVSP_026538Add
BLAST
Alternative sequencei377 – 622246Missing in isoform 4. 2 PublicationsVSP_026539Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31661 mRNA. Translation: AAA60174.1.
AF166329 mRNA. Translation: AAD49855.1.
AF091870
, AF091863, AF091864, AF091865, AF091866, AF091867, AF091868, AF091869 Genomic DNA. Translation: AAD32032.1.
AF349939 mRNA. Translation: AAK32703.1.
AF416618 mRNA. Translation: AAL23914.1.
AF416619 mRNA. Translation: AAL23915.1.
AF492470 mRNA. Translation: AAM18048.1.
AF493069 mRNA. Translation: AAM11661.1.
GU133399 mRNA. Translation: ACZ04321.1.
AK313270 mRNA. Translation: BAG36079.1.
AC010368 Genomic DNA. No translation available.
AC091851 Genomic DNA. No translation available.
CH471119 Genomic DNA. Translation: EAW55919.1.
BC059392 mRNA. Translation: AAH59392.1.
S78505 mRNA. Translation: AAB34470.1.
CCDSiCCDS3909.1. [P16471-1]
CCDS56358.1. [P16471-2]
CCDS56359.1. [P16471-7]
CCDS56360.1. [P16471-6]
CCDS56361.1. [P16471-4]
CCDS56362.1. [P16471-5]
PIRiA40144.
A59405.
B59405.
RefSeqiNP_000940.1. NM_000949.6. [P16471-1]
NP_001191243.1. NM_001204314.2. [P16471-2]
NP_001191244.1. NM_001204315.1. [P16471-5]
NP_001191245.1. NM_001204316.1. [P16471-4]
NP_001191246.1. NM_001204317.1. [P16471-6]
NP_001191247.1. NM_001204318.1. [P16471-7]
XP_006714547.1. XM_006714484.1. [P16471-1]
UniGeneiHs.368587.
Hs.602914.

Genome annotation databases

EnsembliENST00000231423; ENSP00000231423; ENSG00000113494. [P16471-4]
ENST00000310101; ENSP00000309008; ENSG00000113494. [P16471-5]
ENST00000348262; ENSP00000311613; ENSG00000113494. [P16471-7]
ENST00000509140; ENSP00000425300; ENSG00000113494. [P16471-6]
ENST00000511486; ENSP00000422556; ENSG00000113494. [P16471-2]
ENST00000513753; ENSP00000424841; ENSG00000113494. [P16471-6]
ENST00000514088; ENSP00000422935; ENSG00000113494. [P16471-7]
ENST00000542609; ENSP00000441813; ENSG00000113494. [P16471-4]
ENST00000618457; ENSP00000482954; ENSG00000113494. [P16471-1]
ENST00000619676; ENSP00000484768; ENSG00000113494. [P16471-5]
ENST00000620785; ENSP00000482689; ENSG00000113494. [P16471-2]
GeneIDi5618.
KEGGihsa:5618.
UCSCiuc003jjg.2. human. [P16471-4]
uc003jjh.2. human. [P16471-6]
uc003jji.2. human. [P16471-8]
uc003jjj.2. human. [P16471-7]
uc003jjl.4. human. [P16471-2]
uc003jjm.3. human. [P16471-1]
uc010iuw.1. human. [P16471-3]
uc021xxl.1. human. [P16471-5]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31661 mRNA. Translation: AAA60174.1.
AF166329 mRNA. Translation: AAD49855.1.
AF091870
, AF091863, AF091864, AF091865, AF091866, AF091867, AF091868, AF091869 Genomic DNA. Translation: AAD32032.1.
AF349939 mRNA. Translation: AAK32703.1.
AF416618 mRNA. Translation: AAL23914.1.
AF416619 mRNA. Translation: AAL23915.1.
AF492470 mRNA. Translation: AAM18048.1.
AF493069 mRNA. Translation: AAM11661.1.
GU133399 mRNA. Translation: ACZ04321.1.
AK313270 mRNA. Translation: BAG36079.1.
AC010368 Genomic DNA. No translation available.
AC091851 Genomic DNA. No translation available.
CH471119 Genomic DNA. Translation: EAW55919.1.
BC059392 mRNA. Translation: AAH59392.1.
S78505 mRNA. Translation: AAB34470.1.
CCDSiCCDS3909.1. [P16471-1]
CCDS56358.1. [P16471-2]
CCDS56359.1. [P16471-7]
CCDS56360.1. [P16471-6]
CCDS56361.1. [P16471-4]
CCDS56362.1. [P16471-5]
PIRiA40144.
A59405.
B59405.
RefSeqiNP_000940.1. NM_000949.6. [P16471-1]
NP_001191243.1. NM_001204314.2. [P16471-2]
NP_001191244.1. NM_001204315.1. [P16471-5]
NP_001191245.1. NM_001204316.1. [P16471-4]
NP_001191246.1. NM_001204317.1. [P16471-6]
NP_001191247.1. NM_001204318.1. [P16471-7]
XP_006714547.1. XM_006714484.1. [P16471-1]
UniGeneiHs.368587.
Hs.602914.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BP3X-ray2.90B25-235[»]
2LFGNMR-A123-234[»]
3D48X-ray2.50R25-234[»]
3MZGX-ray2.10B26-234[»]
3N06X-ray2.00B26-234[»]
3N0PX-ray2.10B26-234[»]
3NCBX-ray2.10B26-234[»]
3NCCX-ray2.50B26-234[»]
3NCEX-ray2.00B26-234[»]
3NCFX-ray2.80B26-234[»]
4I18X-ray3.24C/R25-235[»]
ProteinModelPortaliP16471.
SMRiP16471. Positions 26-230.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111603. 14 interactions.
DIPiDIP-288N.
IntActiP16471. 4 interactions.
MINTiMINT-268499.

Chemistry

BindingDBiP16471.
ChEMBLiCHEMBL5588.
DrugBankiDB01185. Fluoxymesterone.
DB00052. Somatropin recombinant.
GuidetoPHARMACOLOGYi1721.

PTM databases

PhosphoSiteiP16471.

Polymorphism and mutation databases

BioMutaiPRLR.
DMDMi130321.

Proteomic databases

PaxDbiP16471.
PRIDEiP16471.

Protocols and materials databases

DNASUi5618.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000231423; ENSP00000231423; ENSG00000113494. [P16471-4]
ENST00000310101; ENSP00000309008; ENSG00000113494. [P16471-5]
ENST00000348262; ENSP00000311613; ENSG00000113494. [P16471-7]
ENST00000509140; ENSP00000425300; ENSG00000113494. [P16471-6]
ENST00000511486; ENSP00000422556; ENSG00000113494. [P16471-2]
ENST00000513753; ENSP00000424841; ENSG00000113494. [P16471-6]
ENST00000514088; ENSP00000422935; ENSG00000113494. [P16471-7]
ENST00000542609; ENSP00000441813; ENSG00000113494. [P16471-4]
ENST00000618457; ENSP00000482954; ENSG00000113494. [P16471-1]
ENST00000619676; ENSP00000484768; ENSG00000113494. [P16471-5]
ENST00000620785; ENSP00000482689; ENSG00000113494. [P16471-2]
GeneIDi5618.
KEGGihsa:5618.
UCSCiuc003jjg.2. human. [P16471-4]
uc003jjh.2. human. [P16471-6]
uc003jji.2. human. [P16471-8]
uc003jjj.2. human. [P16471-7]
uc003jjl.4. human. [P16471-2]
uc003jjm.3. human. [P16471-1]
uc010iuw.1. human. [P16471-3]
uc021xxl.1. human. [P16471-5]

Organism-specific databases

CTDi5618.
GeneCardsiGC05M035084.
HGNCiHGNC:9446. PRLR.
MIMi176761. gene.
615554. phenotype.
615555. phenotype.
neXtProtiNX_P16471.
Orphaneti397685. Familial hyperprolactinemia.
50920. Multiple fibroadenoma of the breast.
PharmGKBiPA33791.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG29671.
GeneTreeiENSGT00530000063112.
HOGENOMiHOG000059569.
HOVERGENiHBG007314.
InParanoidiP16471.
KOiK05081.
OMAiSGPNSCY.
OrthoDBiEOG7Q5HCH.
PhylomeDBiP16471.
TreeFamiTF330851.

Enzyme and pathway databases

ReactomeiREACT_111133. Growth hormone receptor signaling.
REACT_115697. Prolactin receptor signaling.
SignaLinkiP16471.

Miscellaneous databases

ChiTaRSiPRLR. human.
EvolutionaryTraceiP16471.
GenomeRNAii5618.
NextBioi21832.
PROiP16471.
SOURCEiSearch...

Gene expression databases

BgeeiP16471.
CleanExiHS_PRLR.
ExpressionAtlasiP16471. baseline and differential.
GenevestigatoriP16471.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR003961. FN3_dom.
IPR015152. Growth/epo_recpt_lig-bind.
IPR013783. Ig-like_fold.
IPR003528. Long_hematopoietin_rcpt_CS.
[Graphical view]
PfamiPF09067. EpoR_lig-bind. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 2 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 2 hits.
PS01352. HEMATOPO_REC_L_F1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a cDNA encoding a long form of prolactin receptor in human hepatoma and breast cancer cells."
    Boutin J.-M., Edery M., Shirota M., Jolicoeur C., Lesueur L., Ali S., Gould D., Djiane J., Kelly P.A.
    Mol. Endocrinol. 3:1455-1461(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Functional characterization of the intermediate isoform of the human prolactin receptor."
    Kline J.B., Roehrs H., Clevenger C.V.
    J. Biol. Chem. 274:35461-35468(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
  3. "The human prolactin receptor gene structure and alternative promoter utilization: the generic promoter hPIII and a novel human promoter hP(N)."
    Hu Z.-Z., Zhuang L., Meng J., Leondires M., Dufau M.L.
    J. Clin. Endocrinol. Metab. 84:1153-1156(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Isolation and characterization of two novel forms of the human prolactin receptor generated by alternative splicing of a newly identified exon 11."
    Hu Z.Z., Meng J., Dufau M.L.
    J. Biol. Chem. 276:41086-41094(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 4 AND 6), INTERACTION WITH GH1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  5. "Characterization of a novel and functional human prolactin receptor isoform (deltaS1PRLr) containing only one extracellular fibronectin-like domain."
    Kline J.B., Rycyzyn M.A., Clevenger C.V.
    Mol. Endocrinol. 16:2310-2322(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Mammary carcinoma.
  6. "Alternative splicing to exon 11 of human prolactin receptor gene results in multiple isoforms including a secreted prolactin-binding protein."
    Trott J.F., Hovey R.C., Koduri S., Vonderhaar B.K.
    J. Mol. Endocrinol. 30:31-47(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 4; 6; 7 AND 8), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. "Prolactin exerts a prosurvival effect on human spermatozoa via mechanisms that involve the stimulation of Akt phosphorylation and suppression of caspase activation and capacitation."
    Pujianto D.A., Curry B.J., Aitken R.J.
    Endocrinology 151:1269-1279(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9), FUNCTION.
  8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Prostate.
  9. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "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] (ISOFORM 1).
    Tissue: Placenta.
  12. "Prolactin receptor antagonists that inhibit the growth of breast cancer cell lines."
    Fuh G., Wells J.A.
    J. Biol. Chem. 270:13133-13137(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-622 (ISOFORM 3).
    Tissue: Mammary carcinoma.
  13. "Novel association of Vav2 and Nek3 modulates signaling through the human prolactin receptor."
    Miller S.L., DeMaria J.E., Freier D.O., Riegel A.M., Clevenger C.V.
    Mol. Endocrinol. 19:939-949(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NEK3 AND VAV2.
  14. "Crystal structure and site 1 binding energetics of human placental lactogen."
    Walsh S.T., Kossiakoff A.A.
    J. Mol. Biol. 358:773-784(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, ZINC-BINDING SITES.
  15. "The imitation switch protein SNF2L regulates steroidogenic acute regulatory protein expression during terminal differentiation of ovarian granulosa cells."
    Lazzaro M.A., Pepin D., Pescador N., Murphy B.D., Vanderhyden B.C., Picketts D.J.
    Mol. Endocrinol. 20:2406-2417(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMARCA1.
  16. "Identification of a gain-of-function mutation of the prolactin receptor in women with benign breast tumors."
    Bogorad R.L., Courtillot C., Mestayer C., Bernichtein S., Harutyunyan L., Jomain J.B., Bachelot A., Kuttenn F., Kelly P.A., Goffin V., Touraine P., Bachelot A., Belaroussi B., Bensimhon J., Berdah J., Blin M.J., Boudinet A., Brethon B.
    , Bricaire C., Caby J., Caillaud G., Carel J.C., Chabbert-Buffet N., Charitanski H., Chretien C., Clough K., Courtillot C., Delattre G., Denys I., Desthieux-Ngo K., Detoeuf M., Dhainault C., Duflos C., Fiori O., Genestie C., Gibaud G., Gompel A., Gracia C., Grimard A., Hofman C., Hofman H., Kuttenn F., Laki F., Lanty C., Lefranc J.P., Le Frere-Belda M.A., Leger D., Martinez F., May A., Meng L., Nos C., Pelletier D., Perrin A., Plu-Bureau G., Raccah-Tebbeca B., Saiovici J.C., Salmon R., Sibout M., Sigal-Zafrani B., Thalabard J.C., Thibaud E., Thoury A., Touraine P., Triana-Rabi K.B., Uzan S., Viriot J., Yacoub S.
    Proc. Natl. Acad. Sci. U.S.A. 105:14533-14538(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MFAB LEU-170, CHARACTERIZATION OF VARIANT MFAB LEU-170.
  17. Cited for: VARIANT HPRL ARG-212, CHARACTERIZATION OF VARIANT HPRL ARG-212.
  18. "The X-ray structure of a growth hormone-prolactin receptor complex."
    Somers W., Ultsch M., de Vos A.M., Kossiakoff A.A.
    Nature 372:478-481(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 25-235.
  19. "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 25-234 IN COMPLEX WITH PRL, SUBUNIT, DISULFIDE BONDS.

Entry informationi

Entry nameiPRLR_HUMAN
AccessioniPrimary (citable) accession number: P16471
Secondary accession number(s): B2R882
, D1MDP1, Q16354, Q8TD75, Q8TD78, Q96P35, Q96P36, Q9BX87, Q9UHJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: April 29, 2015
This is version 175 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, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.