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P16471

- PRLR_HUMAN

UniProt

P16471 - PRLR_HUMAN

Protein

Prolactin receptor

Gene

PRLR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 1 (01 Aug 1990)
      Previous versions | rss
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    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

    1. metal ion binding Source: UniProtKB-KW
    2. ornithine decarboxylase activator activity Source: UniProtKB
    3. peptide hormone binding Source: BHF-UCL
    4. prolactin receptor activity Source: UniProtKB
    5. protein binding Source: IntAct
    6. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. activation of JAK2 kinase activity Source: UniProtKB
    2. activation of transmembrane receptor protein tyrosine kinase activity Source: UniProtKB
    3. cell surface receptor signaling pathway Source: UniProtKB
    4. embryo implantation Source: ProtInc
    5. JAK-STAT cascade involved in growth hormone signaling pathway Source: Reactome
    6. lactation Source: UniProtKB
    7. negative regulation of apoptotic process Source: UniProtKB
    8. prolactin signaling pathway Source: GOC
    9. steroid biosynthetic process Source: UniProtKB
    10. T cell activation Source: UniProtKB

    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: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:9446. PRLR.

    Subcellular locationi

    Membrane 2 Publications; Single-pass type I membrane protein 2 Publications

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. endosome lumen Source: Reactome
    3. extracellular region Source: UniProtKB-SubCell
    4. integral component of membrane Source: UniProtKB-KW
    5. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Multiple fibroadenomas of the breast (MFAB) [MIM:615554]: A 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti170 – 1701I → L in MFAB; confers constitutive activity. 1 Publication
    VAR_070894
    Hyperprolactinemia (HPRL) [MIM:615555]: A 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.
    PharmGKBiPA33791.

    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

    ArrayExpressiP16471.
    BgeeiP16471.
    CleanExiHS_PRLR.
    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 – 4211
    Beta strandi44 – 496
    Beta strandi52 – 543
    Beta strandi58 – 669
    Turni67 – 693
    Beta strandi85 – 884
    Helixi90 – 923
    Beta strandi95 – 973
    Beta strandi99 – 1079
    Beta strandi110 – 1134
    Beta strandi117 – 1193
    Helixi121 – 1233
    Beta strandi131 – 1388
    Beta strandi141 – 1433
    Beta strandi146 – 1527
    Beta strandi155 – 1573
    Beta strandi162 – 1643
    Beta strandi166 – 1738
    Beta strandi181 – 1866
    Beta strandi189 – 1935
    Beta strandi201 – 21313
    Beta strandi222 – 2254
    Helixi230 – 2323

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei235 – 25824HelicalSequence AnalysisAdd
    BLAST

    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.
    HOVERGENiHBG007314.
    InParanoidiP16471.
    KOiK05081.
    OMAiGASHYKN.
    OrthoDBiEOG7Q5HCH.
    PhylomeDBiP16471.
    TreeFamiTF330851.

    Family and domain databases

    Gene3Di2.60.40.10. 2 hits.
    InterProiIPR003961. Fibronectin_type3.
    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. Align

    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

    MKENVASATV FTLLLFLNTC LLNGQLPPGK PEIFKCRSPN KETFTCWWRP    50
    GTDGGLPTNY SLTYHREGET LMHECPDYIT GGPNSCHFGK QYTSMWRTYI 100
    MMVNATNQMG SSFSDELYVD VTYIVQPDPP LELAVEVKQP EDRKPYLWIK 150
    WSPPTLIDLK TGWFTLLYEI RLKPEKAAEW EIHFAGQQTE FKILSLHPGQ 200
    KYLVQVRCKP DHGYWSAWSP ATFIQIPSDF TMNDTTVWIS VAVLSAVICL 250
    IIVWAVALKG YSMVTCIFPP VPGPKIKGFD AHLLEKGKSE ELLSALGCQD 300
    FPPTSDYEDL LVEYLEVDDS EDQHLMSVHS KEHPSQGMKP TYLDPDTDSG 350
    RGSCDSPSLL SEKCEEPQAN PSTFYDPEVI EKPENPETTH TWDPQCISME 400
    GKIPYFHAGG SKCSTWPLPQ PSQHNPRSSY HNITDVCELA VGPAGAPATL 450
    LNEAGKDALK SSQTIKSREE GKATQQREVE SFHSETDQDT PWLLPQEKTP 500
    FGSAKPLDYV EIHKVNKDGA LSLLPKQREN SGKPKKPGTP ENNKEYAKVS 550
    GVMDNNILVL VPDPHAKNVA CFEESAKEAP PSLEQNQAEK ALANFTATSS 600
    KCRLQLGGLD YLDPACFTHS FH 622
    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:
    EMBL
    GenBank
    DDBJ
    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]
    ENST00000511486; ENSP00000422556; ENSG00000113494. [P16471-2]
    ENST00000513753; ENSP00000424841; ENSG00000113494. [P16471-6]
    ENST00000542609; ENSP00000441813; ENSG00000113494. [P16471-9]
    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]

    Polymorphism databases

    DMDMi130321.

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS3909.1. [P16471-1 ]
    CCDS56358.1. [P16471-2 ]
    CCDS56359.1. [P16471-7 ]
    CCDS56360.1. [P16471-6 ]
    CCDS56361.1. [P16471-4 ]
    CCDS56362.1. [P16471-5 ]
    PIRi A40144.
    A59405.
    B59405.
    RefSeqi NP_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 ]
    UniGenei Hs.368587.
    Hs.602914.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BP3 X-ray 2.90 B 25-235 [» ]
    2LFG NMR - A 123-234 [» ]
    3D48 X-ray 2.50 R 25-234 [» ]
    3MZG X-ray 2.10 B 26-234 [» ]
    3N06 X-ray 2.00 B 26-234 [» ]
    3N0P X-ray 2.10 B 26-234 [» ]
    3NCB X-ray 2.10 B 26-234 [» ]
    3NCC X-ray 2.50 B 26-234 [» ]
    3NCE X-ray 2.00 B 26-234 [» ]
    3NCF X-ray 2.80 B 26-234 [» ]
    4I18 X-ray 3.24 C/R 25-235 [» ]
    ProteinModelPortali P16471.
    SMRi P16471. Positions 26-230.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111603. 14 interactions.
    DIPi DIP-288N.
    IntActi P16471. 4 interactions.
    MINTi MINT-268499.

    Chemistry

    BindingDBi P16471.
    ChEMBLi CHEMBL5588.
    DrugBanki DB00858. Dromostanolone.
    DB01185. Fluoxymesterone.
    DB00082. Pegvisomant.
    DB00052. Somatropin recombinant.
    GuidetoPHARMACOLOGYi 1721.

    PTM databases

    PhosphoSitei P16471.

    Polymorphism databases

    DMDMi 130321.

    Proteomic databases

    PaxDbi P16471.
    PRIDEi P16471.

    Protocols and materials databases

    DNASUi 5618.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000231423 ; ENSP00000231423 ; ENSG00000113494 . [P16471-4 ]
    ENST00000310101 ; ENSP00000309008 ; ENSG00000113494 . [P16471-5 ]
    ENST00000348262 ; ENSP00000311613 ; ENSG00000113494 . [P16471-7 ]
    ENST00000511486 ; ENSP00000422556 ; ENSG00000113494 . [P16471-2 ]
    ENST00000513753 ; ENSP00000424841 ; ENSG00000113494 . [P16471-6 ]
    ENST00000542609 ; ENSP00000441813 ; ENSG00000113494 . [P16471-9 ]
    GeneIDi 5618.
    KEGGi hsa:5618.
    UCSCi uc003jjg.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

    CTDi 5618.
    GeneCardsi GC05M035084.
    HGNCi HGNC:9446. PRLR.
    MIMi 176761. gene.
    615554. phenotype.
    615555. phenotype.
    neXtProti NX_P16471.
    PharmGKBi PA33791.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG29671.
    HOVERGENi HBG007314.
    InParanoidi P16471.
    KOi K05081.
    OMAi GASHYKN.
    OrthoDBi EOG7Q5HCH.
    PhylomeDBi P16471.
    TreeFami TF330851.

    Enzyme and pathway databases

    Reactomei REACT_111133. Growth hormone receptor signaling.
    REACT_115697. Prolactin receptor signaling.
    SignaLinki P16471.

    Miscellaneous databases

    EvolutionaryTracei P16471.
    GenomeRNAii 5618.
    NextBioi 21832.
    PROi P16471.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16471.
    Bgeei P16471.
    CleanExi HS_PRLR.
    Genevestigatori P16471.

    Family and domain databases

    Gene3Di 2.60.40.10. 2 hits.
    InterProi IPR003961. Fibronectin_type3.
    IPR015152. Growth/epo_recpt_lig-bind.
    IPR013783. Ig-like_fold.
    IPR003528. Long_hematopoietin_rcpt_CS.
    [Graphical view ]
    Pfami PF09067. EpoR_lig-bind. 1 hit.
    [Graphical view ]
    SMARTi SM00060. FN3. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 2 hits.
    PROSITEi PS50853. FN3. 2 hits.
    PS01352. HEMATOPO_REC_L_F1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 169 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