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P45446

- RORB_RAT

UniProt

P45446 - RORB_RAT

Protein

Nuclear receptor ROR-beta

Gene

Rorb

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Considered to have intrinsic transcriptional activity, have some natural ligands such as all-trans retinoic acid (ATRA) and other retinoids which act as inverse agonists repressing the transcriptional activity. Required for normal postnatal development of rod and cone photoreceptor cells. Modulates rod photoreceptors differentiation at least by inducing the transcription factor NRL-mediated pathway. In cone photoreceptor cells, regulates transcription of OPN1SW. Involved in the regulation of the period length and stability of the circadian rhythm. May control cytoarchitectural patterning of neocortical neurons during development. May act in a dose-dependent manner to regulate barrel formation upon innervation of layer IV neurons by thalamocortical axons. May play a role in the suppression of osteoblastic differentiation through the inhibition of RUNX2 transcriptional activity.2 Publications
    Isoform 1: Critical for hindlimb motor control and for the differentiation of amacrine and horizontal cells in the retina. Regulates the expression of PTF1A synergistically with FOXN4 By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi18 – 9376Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri21 – 4121NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri57 – 8125NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: InterPro
    2. melatonin receptor activity Source: RGD
    3. sequence-specific DNA binding Source: InterPro
    4. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    5. steroid hormone receptor activity Source: InterPro
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. amacrine cell differentiation Source: UniProtKB
    2. brain development Source: RGD
    3. cellular response to retinoic acid Source: UniProtKB
    4. circadian rhythm Source: RGD
    5. eye photoreceptor cell development Source: UniProtKB
    6. G-protein coupled receptor signaling pathway Source: GOC
    7. negative regulation of osteoblast differentiation Source: UniProtKB
    8. negative regulation of transcription, DNA-templated Source: UniProtKB
    9. positive regulation of transcription, DNA-templated Source: UniProtKB
    10. regulation of circadian rhythm Source: UniProtKB
    11. response to hormone Source: RGD
    12. retina development in camera-type eye Source: UniProtKB
    13. retinal cone cell development Source: UniProtKB
    14. retinal rod cell development Source: UniProtKB
    15. visual perception Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Developmental protein, Receptor

    Keywords - Biological processi

    Biological rhythms, Sensory transduction, Transcription, Transcription regulation, Vision

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear receptor ROR-beta
    Alternative name(s):
    Nuclear receptor RZR-beta
    Nuclear receptor subfamily 1 group F member 2
    Retinoid-related orphan receptor-beta
    Gene namesi
    Name:Rorb
    Synonyms:Nr1f2, Rzrb
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi1306778. Rorb.

    Subcellular locationi

    Nucleus PROSITE-ProRule annotation

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi280 – 2801A → F, V or S: Inhibits transactivation activity. 1 Publication
    Mutagenesisi280 – 2801A → G: No effect on transactivation activity. 1 Publication
    Mutagenesisi457 – 4571Y → A: Inhibits transactivation activity. 1 Publication
    Mutagenesisi459 – 4591E → A: Inhibits transactivation activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 470470Nuclear receptor ROR-betaPRO_0000053516Add
    BLAST

    Proteomic databases

    PaxDbiP45446.

    PTM databases

    PhosphoSiteiP45446.

    Expressioni

    Tissue specificityi

    Isoform 2 expressed with circadian rhythm in eye and pineal gland. Isoform 1 expressed in retina cortex, thalamus, and hypothalamus.2 Publications

    Inductioni

    Isoform 2 oscillates diurnally in eye and pineal gland, with highest levels shortly after midnight.1 Publication

    Gene expression databases

    GenevestigatoriP45446.

    Interactioni

    Subunit structurei

    Monomer. Interacts with CRX.3 Publications

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000018137.

    Structurei

    Secondary structure

    1
    470
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi220 – 23718
    Helixi242 – 2487
    Helixi255 – 2639
    Helixi266 – 28924
    Helixi292 – 2954
    Helixi299 – 31820
    Helixi319 – 3213
    Turni324 – 3274
    Beta strandi328 – 3314
    Beta strandi334 – 3374
    Helixi338 – 3447
    Helixi347 – 36115
    Helixi367 – 37812
    Helixi389 – 41022
    Helixi416 – 4227
    Helixi424 – 44421
    Helixi446 – 4516
    Helixi455 – 4617

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K4WX-ray1.90A212-463[»]
    1N4HX-ray2.10A212-470[»]
    1NQ7X-ray1.50A219-462[»]
    ProteinModelPortaliP45446.
    SMRiP45446. Positions 18-98, 219-462.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP45446.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni94 – 211118HingeSequence AnalysisAdd
    BLAST
    Regioni222 – 470249Ligand-bindingAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi456 – 4616AF-2

    Domaini

    AF-2 (activation function-2) motif is required for recruiting coregulators containing the LXXLL motif, such as NCOA1, and control the transactivational activity (PubMed:8816759 and PubMed:11689423).2 Publications

    Sequence similaritiesi

    Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri21 – 4121NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri57 – 8125NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG324222.
    HOGENOMiHOG000010200.
    HOVERGENiHBG106848.
    InParanoidiP45446.
    PhylomeDBiP45446.

    Family and domain databases

    Gene3Di1.10.565.10. 2 hits.
    3.30.50.10. 1 hit.
    InterProiIPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR003079. ROR_rcpt.
    IPR001723. Str_hrmn_rcpt.
    IPR001628. Znf_hrmn_rcpt.
    IPR013088. Znf_NHR/GATA.
    [Graphical view]
    PfamiPF00104. Hormone_recep. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view]
    PRINTSiPR01293. RORNUCRECPTR.
    PR00398. STRDHORMONER.
    PR00047. STROIDFINGER.
    SMARTiSM00430. HOLI. 1 hit.
    SM00399. ZnF_C4. 1 hit.
    [Graphical view]
    SUPFAMiSSF48508. SSF48508. 1 hit.
    PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative promoter usage. Align

    Isoform 2 (identifier: P45446-2) [UniParc]FASTAAdd to Basket

    Also known as: ROR-beta 2

    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

    MCENQLKTKA DGTAQIEVIP CKICGDKSSG IHYGVITCEG CKGFFRRSQQ    50
    NNASYSCPRQ RNCLIDRTNR NRCQHCRLQK CLALGMSRDA VKFGRMSKKQ 100
    RDSLYAEVQK HQQRLQEQRQ QQSGEAEALA RVYSSSISNG LSNLNTETGG 150
    TYANGHVIDL PKSEGYYNID SGQPSPDQSG LDMTGIKQIK QEPIYDLTSV 200
    HNLFTYSSFN NGQLAPGITM SEIDRIAQNI IKSHLETCQY TMEELHQLAW 250
    QTHTYEEIKA YQSKSREALW QQCAIQITHA IQYVVEFAKR ITGFMELCQN 300
    DQILLLKSGC LEVVLVRMCR AFNPLNNTVL FEGKYGGMQM FKALGSDDLV 350
    NEAFDFAKNL CSLQLTEEEI ALFSSAVLIS PDRAWLLEPR KVQKLQEKIY 400
    FALQHVIQKN HLDDETLAKL IAKIPTITAV CNLHGEKLQV FKQSHPDIVN 450
    TLFPPLYKEL FNPDCAAVCK 470

    Note: Shows a 4-fold higher transcriptional activation of an optimal promoter compared to isoform 1.

    Length:470
    Mass (Da):53,201
    Last modified:January 23, 2007 - v3
    Checksum:iFC31D327410FF310
    GO
    Isoform 1 (identifier: P45446-1) [UniParc]FASTAAdd to Basket

    Also known as: ROR-beta 1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-13: MCENQLKTKADGT → MR

    Show »
    Length:459
    Mass (Da):52,068
    Checksum:iB415C0BDBA61D6D6
    GO

    Sequence cautioni

    The sequence AAA42095.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1313MCENQ…KADGT → MR in isoform 1. CuratedVSP_022577Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L14610 Genomic DNA. Translation: AAA42095.1. Different initiation.
    PIRiI65219.
    UniGeneiRn.231652.

    Genome annotation databases

    UCSCiRGD:1306778. rat. [P45446-2]

    Keywords - Coding sequence diversityi

    Alternative promoter usage

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L14610 Genomic DNA. Translation: AAA42095.1 . Different initiation.
    PIRi I65219.
    UniGenei Rn.231652.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1K4W X-ray 1.90 A 212-463 [» ]
    1N4H X-ray 2.10 A 212-470 [» ]
    1NQ7 X-ray 1.50 A 219-462 [» ]
    ProteinModelPortali P45446.
    SMRi P45446. Positions 18-98, 219-462.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000018137.

    PTM databases

    PhosphoSitei P45446.

    Proteomic databases

    PaxDbi P45446.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:1306778. rat. [P45446-2 ]

    Organism-specific databases

    RGDi 1306778. Rorb.

    Phylogenomic databases

    eggNOGi NOG324222.
    HOGENOMi HOG000010200.
    HOVERGENi HBG106848.
    InParanoidi P45446.
    PhylomeDBi P45446.

    Miscellaneous databases

    EvolutionaryTracei P45446.
    PROi P45446.

    Gene expression databases

    Genevestigatori P45446.

    Family and domain databases

    Gene3Di 1.10.565.10. 2 hits.
    3.30.50.10. 1 hit.
    InterProi IPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR003079. ROR_rcpt.
    IPR001723. Str_hrmn_rcpt.
    IPR001628. Znf_hrmn_rcpt.
    IPR013088. Znf_NHR/GATA.
    [Graphical view ]
    Pfami PF00104. Hormone_recep. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view ]
    PRINTSi PR01293. RORNUCRECPTR.
    PR00398. STRDHORMONER.
    PR00047. STROIDFINGER.
    SMARTi SM00430. HOLI. 1 hit.
    SM00399. ZnF_C4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48508. SSF48508. 1 hit.
    PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "RZRs, a new family of retinoid-related orphan receptors that function as both monomers and homodimers."
      Carlberg C., Hooft van Huijsduijnen R., Staple J.K., Delamarter J.F., Becker-Andre M.
      Mol. Endocrinol. 8:757-770(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
      Strain: Sprague-Dawley.
      Tissue: Brain.
    2. "A novel isoform of the orphan nuclear receptor RORbeta is specifically expressed in pineal gland and retina."
      Andre E., Gawlas K., Becker-Andre M.
      Gene 216:277-283(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION AS TRANSCRIPTION ACTIVATOR (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, DNA-BINDING, INDUCTION.
    3. "Functional analysis of retinoid Z receptor beta, a brain-specific nuclear orphan receptor."
      Greiner E.F., Kirfel J., Greschik H., Doerflinger U., Becker P., Mercep A., Schuele R.
      Proc. Natl. Acad. Sci. U.S.A. 93:10105-10110(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS TRANSCRIPTION MODULATOR, SUBUNIT, DNA-BINDING, DOMAIN.
    4. "Disruption of retinoid-related orphan receptor beta changes circadian behavior, causes retinal degeneration and leads to vacillans phenotype in mice."
      Andre E., Conquet F., Steinmayr M., Stratton S.C., Porciatti V., Becker-Andre M.
      EMBO J. 17:3867-3877(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    5. "X-ray structure of the orphan nuclear receptor RORbeta ligand-binding domain in the active conformation."
      Stehlin C., Wurtz J.-M., Steinmetz A., Greiner E., Schuele R., Moras D., Renaud J.-P.
      EMBO J. 20:5822-5831(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 212-463 IN COMPLEX WITH STEARIC ACID AND NCOA1 PEPTIDE, DOMAIN, MUTAGENESIS OF ALA-280; TYR-457 AND GLU-459.
    6. "All-trans retinoic acid is a ligand for the orphan nuclear receptor ROR beta."
      Stehlin-Gaon C., Willmann D., Zeyer D., Sanglier S., van Dorsselaer A., Renaud J.-P., Moras D., Schule R.
      Nat. Struct. Biol. 10:820-825(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 219-462 IN COMPLEX WITH RETINOIC ACID AND PEPTIDE SRC-1, FUNCTION AS TRANSCRIPTION ACTIVATOR, IDENTIFICATION OF LIGANDS.

    Entry informationi

    Entry nameiRORB_RAT
    AccessioniPrimary (citable) accession number: P45446
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 130 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3