GenomeNet

Database: UniProt
Entry: P16471
LinkDB: P16471
Original site: P16471 
ID   PRLR_HUMAN              Reviewed;         622 AA.
AC   P16471; B2R882; D1MDP1; Q16354; Q8TD75; Q8TD78; Q96P35; Q96P36; Q9BX87;
AC   Q9UHJ5;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   17-JUN-2020, entry version 220.
DE   RecName: Full=Prolactin receptor;
DE            Short=PRL-R;
DE   Flags: Precursor;
GN   Name=PRLR;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=2558309; DOI=10.1210/mend-3-9-1455;
RA   Boutin J.-M., Edery M., Shirota M., Jolicoeur C., Lesueur L., Ali S.,
RA   Gould D., Djiane J., Kelly P.A.;
RT   "Identification of a cDNA encoding a long form of prolactin receptor in
RT   human hepatoma and breast cancer cells.";
RL   Mol. Endocrinol. 3:1455-1461(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RX   PubMed=10585417; DOI=10.1074/jbc.274.50.35461;
RA   Kline J.B., Roehrs H., Clevenger C.V.;
RT   "Functional characterization of the intermediate isoform of the human
RT   prolactin receptor.";
RL   J. Biol. Chem. 274:35461-35468(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10084611; DOI=10.1210/jcem.84.3.5659;
RA   Hu Z.-Z., Zhuang L., Meng J., Leondires M., Dufau M.L.;
RT   "The human prolactin receptor gene structure and alternative promoter
RT   utilization: the generic promoter hPIII and a novel human promoter hP(N).";
RL   J. Clin. Endocrinol. Metab. 84:1153-1156(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 4 AND 6), INTERACTION WITH GH1,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=11518703; DOI=10.1074/jbc.m102109200;
RA   Hu Z.Z., Meng J., Dufau M.L.;
RT   "Isolation and characterization of two novel forms of the human prolactin
RT   receptor generated by alternative splicing of a newly identified exon 11.";
RL   J. Biol. Chem. 276:41086-41094(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Mammary carcinoma;
RX   PubMed=12351696; DOI=10.1210/me.2001-0033;
RA   Kline J.B., Rycyzyn M.A., Clevenger C.V.;
RT   "Characterization of a novel and functional human prolactin receptor
RT   isoform (deltaS1PRLr) containing only one extracellular fibronectin-like
RT   domain.";
RL   Mol. Endocrinol. 16:2310-2322(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 4; 6; 7 AND 8), FUNCTION,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=12580759; DOI=10.1677/jme.0.0300031;
RA   Trott J.F., Hovey R.C., Koduri S., Vonderhaar B.K.;
RT   "Alternative splicing to exon 11 of human prolactin receptor gene results
RT   in multiple isoforms including a secreted prolactin-binding protein.";
RL   J. Mol. Endocrinol. 30:31-47(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9), AND FUNCTION.
RX   PubMed=20032052; DOI=10.1210/en.2009-0964;
RA   Pujianto D.A., Curry B.J., Aitken R.J.;
RT   "Prolactin exerts a prosurvival effect on human spermatozoa via mechanisms
RT   that involve the stimulation of Akt phosphorylation and suppression of
RT   caspase activation and capacitation.";
RL   Endocrinology 151:1269-1279(2010).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Prostate;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 25-622 (ISOFORM 3).
RC   TISSUE=Mammary carcinoma;
RX   PubMed=7768908; DOI=10.1074/jbc.270.22.13133;
RA   Fuh G., Wells J.A.;
RT   "Prolactin receptor antagonists that inhibit the growth of breast cancer
RT   cell lines.";
RL   J. Biol. Chem. 270:13133-13137(1995).
RN   [13]
RP   INTERACTION WITH NEK3 AND VAV2.
RX   PubMed=15618286; DOI=10.1210/me.2004-0443;
RA   Miller S.L., DeMaria J.E., Freier D.O., Riegel A.M., Clevenger C.V.;
RT   "Novel association of Vav2 and Nek3 modulates signaling through the human
RT   prolactin receptor.";
RL   Mol. Endocrinol. 19:939-949(2005).
RN   [14]
RP   SUBUNIT, AND ZINC-BINDING SITES.
RX   PubMed=16546209; DOI=10.1016/j.jmb.2006.02.038;
RA   Walsh S.T., Kossiakoff A.A.;
RT   "Crystal structure and site 1 binding energetics of human placental
RT   lactogen.";
RL   J. Mol. Biol. 358:773-784(2006).
RN   [15]
RP   INTERACTION WITH SMARCA1.
RX   PubMed=16740656; DOI=10.1210/me.2005-0213;
RA   Lazzaro M.A., Pepin D., Pescador N., Murphy B.D., Vanderhyden B.C.,
RA   Picketts D.J.;
RT   "The imitation switch protein SNF2L regulates steroidogenic acute
RT   regulatory protein expression during terminal differentiation of ovarian
RT   granulosa cells.";
RL   Mol. Endocrinol. 20:2406-2417(2006).
RN   [16]
RP   VARIANT MFAB LEU-170, AND CHARACTERIZATION OF VARIANT MFAB LEU-170.
RX   PubMed=18779591; DOI=10.1073/pnas.0800685105;
RA   Bogorad R.L., Courtillot C., Mestayer C., Bernichtein S., Harutyunyan L.,
RA   Jomain J.B., Bachelot A., Kuttenn F., Kelly P.A., Goffin V., Touraine P.,
RA   Bachelot A., Belaroussi B., Bensimhon J., Berdah J., Blin M.J.,
RA   Boudinet A., Brethon B., Bricaire C., Caby J., Caillaud G., Carel J.C.,
RA   Chabbert-Buffet N., Charitanski H., Chretien C., Clough K., Courtillot C.,
RA   Delattre G., Denys I., Desthieux-Ngo K., Detoeuf M., Dhainault C.,
RA   Duflos C., Fiori O., Genestie C., Gibaud G., Gompel A., Gracia C.,
RA   Grimard A., Hofman C., Hofman H., Kuttenn F., Laki F., Lanty C.,
RA   Lefranc J.P., Le Frere-Belda M.A., Leger D., Martinez F., May A., Meng L.,
RA   Nos C., Pelletier D., Perrin A., Plu-Bureau G., Raccah-Tebbeca B.,
RA   Saiovici J.C., Salmon R., Sibout M., Sigal-Zafrani B., Thalabard J.C.,
RA   Thibaud E., Thoury A., Touraine P., Triana-Rabi K.B., Uzan S., Viriot J.,
RA   Yacoub S.;
RT   "Identification of a gain-of-function mutation of the prolactin receptor in
RT   women with benign breast tumors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:14533-14538(2008).
RN   [17]
RP   VARIANT HPRL ARG-212, AND CHARACTERIZATION OF VARIANT HPRL ARG-212.
RX   PubMed=24195502; DOI=10.1056/nejmoa1307557;
RA   Newey P.J., Gorvin C.M., Cleland S.J., Willberg C.B., Bridge M.,
RA   Azharuddin M., Drummond R.S., van der Merwe P.A., Klenerman P., Bountra C.,
RA   Thakker R.V.;
RT   "Mutant prolactin receptor and familial hyperprolactinemia.";
RL   N. Engl. J. Med. 369:2012-2020(2013).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 25-235.
RX   PubMed=7984244; DOI=10.1038/372478a0;
RA   Somers W., Ultsch M., de Vos A.M., Kossiakoff A.A.;
RT   "The X-ray structure of a growth hormone-prolactin receptor complex.";
RL   Nature 372:478-481(1994).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 25-234 IN COMPLEX WITH PRL,
RP   SUBUNIT, AND DISULFIDE BONDS.
RX   PubMed=18467331; DOI=10.1074/jbc.m801202200;
RA   Svensson L.A., Bondensgaard K., Noerskov-Lauritsen L., Christensen L.,
RA   Becker P., Andersen M.D., Maltesen M.J., Rand K.D., Breinholt J.;
RT   "Crystal structure of a prolactin receptor antagonist bound to the
RT   extracellular domain of the prolactin receptor.";
RL   J. Biol. Chem. 283:19085-19094(2008).
CC   -!- FUNCTION: This is a receptor for the anterior pituitary hormone
CC       prolactin (PRL). Acts as a prosurvival factor for spermatozoa by
CC       inhibiting sperm capacitation through suppression of SRC kinase
CC       activation and stimulation of AKT. Isoform 4 is unable to transduce
CC       prolactin signaling. Isoform 6 is unable to transduce prolactin
CC       signaling. {ECO:0000269|PubMed:12580759, ECO:0000269|PubMed:20032052}.
CC   -!- SUBUNIT: Homodimer upon hormone binding. Interacts with SMARCA1.
CC       Interacts with GH1. Interacts with CSH. Interacts with NEK3 and VAV2
CC       and this interaction is prolactin-dependent.
CC       {ECO:0000269|PubMed:11518703, ECO:0000269|PubMed:15618286,
CC       ECO:0000269|PubMed:16546209, ECO:0000269|PubMed:16740656,
CC       ECO:0000269|PubMed:18467331}.
CC   -!- INTERACTION:
CC       P16471; Q9Y5U4: INSIG2; NbExp=3; IntAct=EBI-476182, EBI-8503746;
CC       P16471; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-476182, EBI-11721828;
CC       P16471; P63104: YWHAZ; NbExp=3; IntAct=EBI-476182, EBI-347088;
CC       P16471-1; P01236: PRL; NbExp=2; IntAct=EBI-15968347, EBI-6903064;
CC       P16471-7; P01236: PRL; NbExp=4; IntAct=EBI-6903057, EBI-6903064;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11518703,
CC       ECO:0000269|PubMed:12580759}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:11518703, ECO:0000269|PubMed:12580759}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 7]: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=9;
CC       Name=1;
CC         IsoId=P16471-1; Sequence=Displayed;
CC       Name=2; Synonyms=Delta-S1;
CC         IsoId=P16471-2; Sequence=VSP_001720;
CC       Name=3;
CC         IsoId=P16471-3; Sequence=VSP_012620, VSP_012621;
CC       Name=4; Synonyms=SF1a, Short form 1a;
CC         IsoId=P16471-4; Sequence=VSP_026537, VSP_026539;
CC       Name=5; Synonyms=Intermediate;
CC         IsoId=P16471-5; Sequence=VSP_026536, VSP_026538;
CC       Name=6; Synonyms=SF1b, Short form 1b;
CC         IsoId=P16471-6; Sequence=VSP_026534, VSP_026535;
CC       Name=7; Synonyms=Delta 7/11;
CC         IsoId=P16471-7; Sequence=VSP_026532, VSP_026533;
CC       Name=8; Synonyms=Delta 4-SF1b;
CC         IsoId=P16471-8; Sequence=VSP_026531, VSP_026534, VSP_026535;
CC       Name=9; Synonyms=SF1c, Short form 1c;
CC         IsoId=P16471-9; Sequence=VSP_047882, VSP_047883;
CC   -!- TISSUE SPECIFICITY: Expressed in breast, placenta, kidney, liver and
CC       pancreas. {ECO:0000269|PubMed:11518703, ECO:0000269|PubMed:12580759}.
CC   -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC       folding and thereby efficient intracellular transport and cell-surface
CC       receptor binding.
CC   -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC       activation.
CC   -!- DISEASE: Multiple fibroadenomas of the breast (MFAB) [MIM:615554]: A
CC       benign breast disease marked by lobuloalveolar growth with abnormally
CC       high proliferation of the epithelium, and characterized by the presence
CC       of more than 3 fibroadenomas in one breast. Fibroadenomas are adenomas
CC       containing fibrous tissue. {ECO:0000269|PubMed:18779591}. Note=The
CC       disease is caused by mutations affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Hyperprolactinemia (HPRL) [MIM:615555]: A disorder
CC       characterized by increased levels of prolactin in the blood not
CC       associated with gestation or the puerperium. HPRL may result in
CC       infertility, hypogonadism, and galactorrhea.
CC       {ECO:0000269|PubMed:24195502}. Note=The disease is caused by mutations
CC       affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: [Isoform 3]: Soluble isoform that appears specific for
CC       the BT-474 breast cancer cell line. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 4]: Includes exon 11. Does not transduce
CC       prolactin signaling. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 5]: Produced by deletion of part of exon 10 and
CC       frameshift. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 6]: Does not transduce prolactin signaling.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 7]: Splices from exon 7 to exon 11.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 8]: SF1b with deletion of exon 4. May be
CC       produced at very low levels due to a premature stop codon in the mRNA,
CC       leading to nonsense-mediated mRNA decay. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 1
CC       subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/PRLRID42891ch5p14.html";
DR   EMBL; M31661; AAA60174.1; -; mRNA.
DR   EMBL; AF166329; AAD49855.1; -; mRNA.
DR   EMBL; AF091870; AAD32032.1; -; Genomic_DNA.
DR   EMBL; AF091863; AAD32032.1; JOINED; Genomic_DNA.
DR   EMBL; AF091864; AAD32032.1; JOINED; Genomic_DNA.
DR   EMBL; AF091865; AAD32032.1; JOINED; Genomic_DNA.
DR   EMBL; AF091866; AAD32032.1; JOINED; Genomic_DNA.
DR   EMBL; AF091867; AAD32032.1; JOINED; Genomic_DNA.
DR   EMBL; AF091868; AAD32032.1; JOINED; Genomic_DNA.
DR   EMBL; AF091869; AAD32032.1; JOINED; Genomic_DNA.
DR   EMBL; AF349939; AAK32703.1; -; mRNA.
DR   EMBL; AF416618; AAL23914.1; -; mRNA.
DR   EMBL; AF416619; AAL23915.1; -; mRNA.
DR   EMBL; AF492470; AAM18048.1; -; mRNA.
DR   EMBL; AF493069; AAM11661.1; -; mRNA.
DR   EMBL; GU133399; ACZ04321.1; -; mRNA.
DR   EMBL; AK313270; BAG36079.1; -; mRNA.
DR   EMBL; AC010368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC091851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471119; EAW55919.1; -; Genomic_DNA.
DR   EMBL; BC059392; AAH59392.1; -; mRNA.
DR   EMBL; S78505; AAB34470.1; -; mRNA.
DR   CCDS; CCDS3909.1; -. [P16471-1]
DR   CCDS; CCDS56358.1; -. [P16471-2]
DR   CCDS; CCDS56359.1; -. [P16471-7]
DR   CCDS; CCDS56360.1; -. [P16471-6]
DR   CCDS; CCDS56361.1; -. [P16471-4]
DR   CCDS; CCDS56362.1; -. [P16471-5]
DR   PIR; A40144; A40144.
DR   PIR; A59405; A59405.
DR   PIR; B59405; B59405.
DR   RefSeq; NP_000940.1; NM_000949.6. [P16471-1]
DR   RefSeq; NP_001191243.1; NM_001204314.2. [P16471-2]
DR   RefSeq; NP_001191244.1; NM_001204315.1. [P16471-5]
DR   RefSeq; NP_001191245.1; NM_001204316.1. [P16471-4]
DR   RefSeq; NP_001191246.1; NM_001204317.1. [P16471-6]
DR   RefSeq; NP_001191247.1; NM_001204318.1. [P16471-7]
DR   RefSeq; XP_006714547.1; XM_006714484.2. [P16471-1]
DR   RefSeq; XP_011512370.1; XM_011514068.2. [P16471-1]
DR   RefSeq; XP_011512371.1; XM_011514069.2. [P16471-1]
DR   RefSeq; XP_016865135.1; XM_017009646.1.
DR   PDB; 1BP3; X-ray; 2.90 A; B=25-235.
DR   PDB; 2LFG; NMR; -; A=123-234.
DR   PDB; 2N7I; NMR; -; A=230-264.
DR   PDB; 3D48; X-ray; 2.50 A; R=25-234.
DR   PDB; 3MZG; X-ray; 2.10 A; B=26-234.
DR   PDB; 3N06; X-ray; 2.00 A; B=26-234.
DR   PDB; 3N0P; X-ray; 2.10 A; B=26-234.
DR   PDB; 3NCB; X-ray; 2.10 A; B=26-234.
DR   PDB; 3NCC; X-ray; 2.50 A; B=26-234.
DR   PDB; 3NCE; X-ray; 2.00 A; B=26-234.
DR   PDB; 3NCF; X-ray; 2.80 A; B=26-234.
DR   PDB; 4I18; X-ray; 3.24 A; C/R=25-235.
DR   PDBsum; 1BP3; -.
DR   PDBsum; 2LFG; -.
DR   PDBsum; 2N7I; -.
DR   PDBsum; 3D48; -.
DR   PDBsum; 3MZG; -.
DR   PDBsum; 3N06; -.
DR   PDBsum; 3N0P; -.
DR   PDBsum; 3NCB; -.
DR   PDBsum; 3NCC; -.
DR   PDBsum; 3NCE; -.
DR   PDBsum; 3NCF; -.
DR   PDBsum; 4I18; -.
DR   SMR; P16471; -.
DR   BioGRID; 111603; 14.
DR   CORUM; P16471; -.
DR   DIP; DIP-288N; -.
DR   ELM; P16471; -.
DR   IntAct; P16471; 8.
DR   MINT; P16471; -.
DR   STRING; 9606.ENSP00000482954; -.
DR   BindingDB; P16471; -.
DR   ChEMBL; CHEMBL5588; -.
DR   DrugBank; DB01185; Fluoxymesterone.
DR   DrugBank; DB00052; Somatotropin.
DR   iPTMnet; P16471; -.
DR   PhosphoSitePlus; P16471; -.
DR   BioMuta; PRLR; -.
DR   DMDM; 130321; -.
DR   jPOST; P16471; -.
DR   PaxDb; P16471; -.
DR   PeptideAtlas; P16471; -.
DR   PRIDE; P16471; -.
DR   ProteomicsDB; 12725; -.
DR   ProteomicsDB; 53366; -. [P16471-1]
DR   ProteomicsDB; 53367; -. [P16471-2]
DR   ProteomicsDB; 53368; -. [P16471-3]
DR   ProteomicsDB; 53369; -. [P16471-4]
DR   ProteomicsDB; 53370; -. [P16471-5]
DR   ProteomicsDB; 53371; -. [P16471-6]
DR   ProteomicsDB; 53372; -. [P16471-7]
DR   ProteomicsDB; 53373; -. [P16471-8]
DR   ABCD; P16471; 42 sequenced antibodies.
DR   Antibodypedia; 10116; 866 antibodies.
DR   DNASU; 5618; -.
DR   Ensembl; ENST00000231423; ENSP00000231423; ENSG00000113494. [P16471-4]
DR   Ensembl; ENST00000310101; ENSP00000309008; ENSG00000113494. [P16471-5]
DR   Ensembl; ENST00000348262; ENSP00000311613; ENSG00000113494. [P16471-7]
DR   Ensembl; ENST00000509140; ENSP00000425300; ENSG00000113494. [P16471-6]
DR   Ensembl; ENST00000511486; ENSP00000422556; ENSG00000113494. [P16471-2]
DR   Ensembl; ENST00000513753; ENSP00000424841; ENSG00000113494. [P16471-6]
DR   Ensembl; ENST00000514088; ENSP00000422935; ENSG00000113494. [P16471-7]
DR   Ensembl; ENST00000542609; ENSP00000441813; ENSG00000113494. [P16471-4]
DR   Ensembl; ENST00000618457; ENSP00000482954; ENSG00000113494. [P16471-1]
DR   Ensembl; ENST00000619676; ENSP00000484768; ENSG00000113494. [P16471-5]
DR   Ensembl; ENST00000620785; ENSP00000482689; ENSG00000113494. [P16471-2]
DR   GeneID; 5618; -.
DR   KEGG; hsa:5618; -.
DR   UCSC; uc003jjg.3; human. [P16471-1]
DR   CTD; 5618; -.
DR   DisGeNET; 5618; -.
DR   EuPathDB; HostDB:ENSG00000113494.16; -.
DR   GeneCards; PRLR; -.
DR   HGNC; HGNC:9446; PRLR.
DR   HPA; ENSG00000113494; Tissue enhanced (brain, placenta, seminal vesicle).
DR   MalaCards; PRLR; -.
DR   MIM; 176761; gene.
DR   MIM; 615554; phenotype.
DR   MIM; 615555; phenotype.
DR   neXtProt; NX_P16471; -.
DR   OpenTargets; ENSG00000113494; -.
DR   Orphanet; 397685; Familial hyperprolactinemia.
DR   PharmGKB; PA33791; -.
DR   eggNOG; ENOG410IUSW; Eukaryota.
DR   eggNOG; ENOG410XRJS; LUCA.
DR   GeneTree; ENSGT00940000154851; -.
DR   HOGENOM; CLU_017892_1_0_1; -.
DR   InParanoid; P16471; -.
DR   KO; K05081; -.
DR   OMA; SCWWKPG; -.
DR   OrthoDB; 346239at2759; -.
DR   PhylomeDB; P16471; -.
DR   TreeFam; TF330851; -.
DR   Reactome; R-HSA-1170546; Prolactin receptor signaling.
DR   Reactome; R-HSA-982772; Growth hormone receptor signaling.
DR   SignaLink; P16471; -.
DR   SIGNOR; P16471; -.
DR   BioGRID-ORCS; 5618; 1 hit in 786 CRISPR screens.
DR   ChiTaRS; PRLR; human.
DR   EvolutionaryTrace; P16471; -.
DR   GenomeRNAi; 5618; -.
DR   Pharos; P16471; Tbio.
DR   PRO; PR:P16471; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; P16471; protein.
DR   Bgee; ENSG00000113494; Expressed in placenta and 139 other tissues.
DR   ExpressionAtlas; P16471; baseline and differential.
DR   Genevisible; P16471; HS.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0031904; C:endosome lumen; TAS:Reactome.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
DR   GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017046; F:peptide hormone binding; IPI:BHF-UCL.
DR   GO; GO:0004925; F:prolactin receptor activity; IDA:UniProtKB.
DR   GO; GO:0042976; P:activation of Janus kinase activity; IDA:UniProtKB.
DR   GO; GO:0007171; P:activation of transmembrane receptor protein tyrosine kinase activity; IDA:UniProtKB.
DR   GO; GO:0007566; P:embryo implantation; TAS:ProtInc.
DR   GO; GO:0060397; P:growth hormone receptor signaling pathway via JAK-STAT; TAS:Reactome.
DR   GO; GO:0007595; P:lactation; TAS:ProtInc.
DR   GO; GO:0060749; P:mammary gland alveolus development; IEA:Ensembl.
DR   GO; GO:0060644; P:mammary gland epithelial cell differentiation; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   GO; GO:0060736; P:prostate gland growth; IEA:Ensembl.
DR   GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR   GO; GO:0030155; P:regulation of cell adhesion; IEA:Ensembl.
DR   GO; GO:0030856; P:regulation of epithelial cell differentiation; IEA:Ensembl.
DR   GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR   GO; GO:0006694; P:steroid biosynthetic process; NAS:UniProtKB.
DR   CDD; cd00063; FN3; 2.
DR   DisProt; DP01106; -.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR015152; Growth/epo_recpt_lig-bind.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003528; Long_hematopoietin_rcpt_CS.
DR   InterPro; IPR033230; PRLR.
DR   PANTHER; PTHR23036:SF86; PTHR23036:SF86; 1.
DR   Pfam; PF09067; EpoR_lig-bind; 1.
DR   SMART; SM00060; FN3; 2.
DR   SUPFAM; SSF49265; SSF49265; 2.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS01352; HEMATOPO_REC_L_F1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Disease mutation; Disulfide bond;
KW   Glycoprotein; Membrane; Metal-binding; Polymorphism; Receptor;
KW   Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW   Transmembrane helix; Zinc.
FT   SIGNAL          1..24
FT   CHAIN           25..622
FT                   /note="Prolactin receptor"
FT                   /id="PRO_0000010977"
FT   TOPO_DOM        25..234
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        259..622
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          27..128
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          129..229
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   MOTIF           215..219
FT                   /note="WSXWS motif"
FT   MOTIF           267..275
FT                   /note="Box 1 motif"
FT   METAL           211
FT                   /note="Zinc"
FT   METAL           212
FT                   /note="Zinc"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        233
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        36..46
FT                   /evidence="ECO:0000269|PubMed:18467331"
FT   DISULFID        75..86
FT                   /evidence="ECO:0000269|PubMed:18467331"
FT   VAR_SEQ         1..71
FT                   /note="Missing (in isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:12580759"
FT                   /id="VSP_026531"
FT   VAR_SEQ         24..124
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12351696"
FT                   /id="VSP_001720"
FT   VAR_SEQ         229..268
FT                   /note="DFTMNDTTVWISVAVLSAVICLIIVWAVALKGYSMVTCIF -> GDPLMLGA
FT                   SHYKNLKSYRPRKISSQGRLAVFTKATLTTVQ (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:12580759"
FT                   /id="VSP_026532"
FT   VAR_SEQ         229..230
FT                   /note="DF -> AW (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:7768908"
FT                   /id="VSP_012620"
FT   VAR_SEQ         231..622
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:7768908"
FT                   /id="VSP_012621"
FT   VAR_SEQ         269..622
FT                   /note="Missing (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:12580759"
FT                   /id="VSP_026533"
FT   VAR_SEQ         286..309
FT                   /note="KGKSEELLSALGCQDFPPTSDYED -> DRLCTPGRCCVSTGLTDLDYSCST
FT                   (in isoform 9)"
FT                   /evidence="ECO:0000303|PubMed:20032052"
FT                   /id="VSP_047882"
FT   VAR_SEQ         286..288
FT                   /note="KGK -> VTP (in isoform 6 and isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:11518703,
FT                   ECO:0000303|PubMed:12580759"
FT                   /id="VSP_026534"
FT   VAR_SEQ         289..622
FT                   /note="Missing (in isoform 6 and isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:11518703,
FT                   ECO:0000303|PubMed:12580759"
FT                   /id="VSP_026535"
FT   VAR_SEQ         310..622
FT                   /note="Missing (in isoform 9)"
FT                   /evidence="ECO:0000303|PubMed:20032052"
FT                   /id="VSP_047883"
FT   VAR_SEQ         337..349
FT                   /note="GMKPTYLDPDTDS -> EREQRQAQEARDS (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:10585417"
FT                   /id="VSP_026536"
FT   VAR_SEQ         338..376
FT                   /note="MKPTYLDPDTDSGRGSCDSPSLLSEKCEEPQANPSTFYD -> DPLMLGASH
FT                   YKNLKSYRPRKISSQGRLAVFTKATLTTVQ (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11518703,
FT                   ECO:0000303|PubMed:12580759"
FT                   /id="VSP_026537"
FT   VAR_SEQ         350..622
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:10585417"
FT                   /id="VSP_026538"
FT   VAR_SEQ         377..622
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11518703,
FT                   ECO:0000303|PubMed:12580759"
FT                   /id="VSP_026539"
FT   VARIANT         100
FT                   /note="I -> V (in dbSNP:rs2228482)"
FT                   /id="VAR_049172"
FT   VARIANT         170
FT                   /note="I -> L (in MFAB; confers constitutive activity;
FT                   dbSNP:rs72478580)"
FT                   /evidence="ECO:0000269|PubMed:18779591"
FT                   /id="VAR_070894"
FT   VARIANT         212
FT                   /note="H -> R (in HPRL; loss of function;
FT                   dbSNP:rs398122522)"
FT                   /evidence="ECO:0000269|PubMed:24195502"
FT                   /id="VAR_070895"
FT   STRAND          32..42
FT                   /evidence="ECO:0000244|PDB:3N06"
FT   STRAND          44..49
FT                   /evidence="ECO:0000244|PDB:3N06"
FT   STRAND          52..54
FT                   /evidence="ECO:0000244|PDB:3N06"
FT   STRAND          58..66
FT                   /evidence="ECO:0000244|PDB:3N06"
FT   TURN            67..69
FT                   /evidence="ECO:0000244|PDB:3NCC"
FT   STRAND          85..88
FT                   /evidence="ECO:0000244|PDB:3N06"
FT   HELIX           90..92
FT                   /evidence="ECO:0000244|PDB:3N06"
FT   STRAND          95..97
FT                   /evidence="ECO:0000244|PDB:3N06"
FT   STRAND          99..107
FT                   /evidence="ECO:0000244|PDB:3N06"
FT   STRAND          110..113
FT                   /evidence="ECO:0000244|PDB:3N06"
FT   STRAND          117..119
FT                   /evidence="ECO:0000244|PDB:3N06"
FT   HELIX           121..123
FT                   /evidence="ECO:0000244|PDB:3N06"
FT   STRAND          131..138
FT                   /evidence="ECO:0000244|PDB:3N06"
FT   STRAND          141..143
FT                   /evidence="ECO:0000244|PDB:3N06"
FT   STRAND          146..152
FT                   /evidence="ECO:0000244|PDB:3N06"
FT   STRAND          155..157
FT                   /evidence="ECO:0000244|PDB:2LFG"
FT   STRAND          162..164
FT                   /evidence="ECO:0000244|PDB:3N0P"
FT   STRAND          166..173
FT                   /evidence="ECO:0000244|PDB:3N06"
FT   STRAND          181..186
FT                   /evidence="ECO:0000244|PDB:3N06"
FT   STRAND          189..193
FT                   /evidence="ECO:0000244|PDB:3N06"
FT   STRAND          201..213
FT                   /evidence="ECO:0000244|PDB:3N06"
FT   STRAND          222..225
FT                   /evidence="ECO:0000244|PDB:3N06"
FT   HELIX           230..232
FT                   /evidence="ECO:0000244|PDB:4I18"
FT   HELIX           234..254
FT                   /evidence="ECO:0000244|PDB:2N7I"
FT   TURN            255..257
FT                   /evidence="ECO:0000244|PDB:2N7I"
FT   STRAND          258..262
FT                   /evidence="ECO:0000244|PDB:2N7I"
SQ   SEQUENCE   622 AA;  69506 MW;  DB7FD0328608C787 CRC64;
     MKENVASATV FTLLLFLNTC LLNGQLPPGK PEIFKCRSPN KETFTCWWRP GTDGGLPTNY
     SLTYHREGET LMHECPDYIT GGPNSCHFGK QYTSMWRTYI MMVNATNQMG SSFSDELYVD
     VTYIVQPDPP LELAVEVKQP EDRKPYLWIK WSPPTLIDLK TGWFTLLYEI RLKPEKAAEW
     EIHFAGQQTE FKILSLHPGQ KYLVQVRCKP DHGYWSAWSP ATFIQIPSDF TMNDTTVWIS
     VAVLSAVICL IIVWAVALKG YSMVTCIFPP VPGPKIKGFD AHLLEKGKSE ELLSALGCQD
     FPPTSDYEDL LVEYLEVDDS EDQHLMSVHS KEHPSQGMKP TYLDPDTDSG RGSCDSPSLL
     SEKCEEPQAN PSTFYDPEVI EKPENPETTH TWDPQCISME GKIPYFHAGG SKCSTWPLPQ
     PSQHNPRSSY HNITDVCELA VGPAGAPATL LNEAGKDALK SSQTIKSREE GKATQQREVE
     SFHSETDQDT PWLLPQEKTP FGSAKPLDYV EIHKVNKDGA LSLLPKQREN SGKPKKPGTP
     ENNKEYAKVS GVMDNNILVL VPDPHAKNVA CFEESAKEAP PSLEQNQAEK ALANFTATSS
     KCRLQLGGLD YLDPACFTHS FH
//
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