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P45446

- RORB_RAT

UniProt

P45446 - RORB_RAT

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Protein

Nuclear receptor ROR-beta

Gene
Rorb, Nr1f2, Rzrb
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.3 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.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi18 – 9376Nuclear receptor2 PublicationsAdd
BLAST
Zinc fingeri21 – 4121NR C4-typeAdd
BLAST
Zinc fingeri57 – 8125NR C4-typeAdd
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
Complete GO annotation...

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 By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB
Complete GO annotation...

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.1 Publication

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.

Miscellaneous databases

EvolutionaryTraceiP45446.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni94 – 211118Hinge Reviewed predictionAdd
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 (1 Publication and 1 Publication).2 Publications

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri21 – 4121NR C4-typeAdd
BLAST
Zinc fingeri57 – 8125NR C4-typeAdd
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. VSP_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: May 14, 2014
This is version 129 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

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