P45446 (RORB_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Rorb
Synonyms:	Nr1f2, Rzrb

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	470 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Orphan nuclear receptor required for normal postnatal development of rod and cone photoreceptor cells. Regulates transcription of OPN1SW in cone photoreceptor cells by binding the sequence 5'-AGGTCA-3' in the OPN1SW promoter. Ref.2
Subcellular location	Nucleus Probable.
Tissue specificity	Isoform 2 expressed with circadian rhythm in eye and pineal gland with highest levels shortly after midnight. Isoform 1 expressed in cortex, thalamus, and hypothalamus. Ref.2
Sequence similarities	Belongs to the nuclear hormone receptor family. NR1 subfamily. Contains 1 nuclear receptor DNA-binding domain.
Sequence caution	The sequence AAA42095.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Sensory transduction Transcription Transcription regulation Vision
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Developmental protein Receptor
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	brain development Inferred from expression pattern PubMed 8905729. Source: RGD circadian rhythm Inferred from expression pattern PubMed 15781226PubMed 18321474. Source: RGD eye photoreceptor cell development Inferred from sequence or structural similarity. Source: UniProtKB intracellular receptor mediated signaling pathway Inferred from electronic annotation. Source: GOC positive regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB response to hormone stimulus Inferred from expression pattern PubMed 17067745. Source: RGD visual perception Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Inferred from electronic annotation. Source: InterPro melatonin receptor activity Inferred from direct assay PubMed 7961794. Source: RGD sequence-specific DNA binding Inferred from sequence or structural similarity. Source: UniProtKB sequence-specific DNA binding transcription factor activity Inferred from sequence or structural similarity. Source: UniProtKB steroid hormone receptor activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 2 (identifier: P45446-2)

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.

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

Isoform 1 (identifier: P45446-1)

Also known as: ROR-beta 1;

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 470

470

Nuclear receptor ROR-beta

PRO_0000053516

Regions

DNA binding

18 – 93

76

Nuclear receptor

Zinc finger

21 – 41

21

NR C4-type

Zinc finger

57 – 81

25

NR C4-type

Region

94 – 211

118

Hinge Potential

Region

222 – 470

249

Ligand-binding

Region

285 – 289

5

SRC-1-binding

Region

299 – 307

9

SRC-1-binding

Region

455 – 459

5

SRC-1-binding

Natural variations

Alternative sequence

1 – 13

13

MCENQ…KADGT → MR in isoform 1.

VSP_022577

Secondary structure

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470

Helix Strand Turn

Details...

Helix

220 – 237

18

Helix

242 – 248

7

Helix

255 – 263

9

Helix

266 – 289

24

Helix

292 – 295

4

Helix

299 – 318

20

Helix

319 – 321

3

Turn

324 – 327

4

Beta strand

328 – 331

4

Beta strand

334 – 337

4

Helix

338 – 344

7

Helix

347 – 361

15

Helix

367 – 378

12

Helix

389 – 410

22

Helix

416 – 422

7

Helix

424 – 444

21

Helix

446 – 451

6

Helix

455 – 461

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 (ROR-beta 2) [UniParc]. Last modified January 23, 2007. Version 3. Checksum: FC31D327410FF310	FASTA	470	53,201
	10 20 30 40 50 60 MCENQLKTKA DGTAQIEVIP CKICGDKSSG IHYGVITCEG CKGFFRRSQQ NNASYSCPRQ 70 80 90 100 110 120 RNCLIDRTNR NRCQHCRLQK CLALGMSRDA VKFGRMSKKQ RDSLYAEVQK HQQRLQEQRQ 130 140 150 160 170 180 QQSGEAEALA RVYSSSISNG LSNLNTETGG TYANGHVIDL PKSEGYYNID SGQPSPDQSG 190 200 210 220 230 240 LDMTGIKQIK QEPIYDLTSV HNLFTYSSFN NGQLAPGITM SEIDRIAQNI IKSHLETCQY 250 260 270 280 290 300 TMEELHQLAW QTHTYEEIKA YQSKSREALW QQCAIQITHA IQYVVEFAKR ITGFMELCQN 310 320 330 340 350 360 DQILLLKSGC LEVVLVRMCR AFNPLNNTVL FEGKYGGMQM FKALGSDDLV NEAFDFAKNL 370 380 390 400 410 420 CSLQLTEEEI ALFSSAVLIS PDRAWLLEPR KVQKLQEKIY FALQHVIQKN HLDDETLAKL 430 440 450 460 470 IAKIPTITAV CNLHGEKLQV FKQSHPDIVN TLFPPLYKEL FNPDCAAVCK
	Isoform 1 (ROR-beta 1) [UniParc]. Checksum: B415C0BDBA61D6D6	FASTA	459	52,068
	10 20 30 40 50 60 MRAQIEVIPC KICGDKSSGI HYGVITCEGC KGFFRRSQQN NASYSCPRQR NCLIDRTNRN 70 80 90 100 110 120 RCQHCRLQKC LALGMSRDAV KFGRMSKKQR DSLYAEVQKH QQRLQEQRQQ QSGEAEALAR 130 140 150 160 170 180 VYSSSISNGL SNLNTETGGT YANGHVIDLP KSEGYYNIDS GQPSPDQSGL DMTGIKQIKQ 190 200 210 220 230 240 EPIYDLTSVH NLFTYSSFNN GQLAPGITMS EIDRIAQNII KSHLETCQYT MEELHQLAWQ 250 260 270 280 290 300 THTYEEIKAY QSKSREALWQ QCAIQITHAI QYVVEFAKRI TGFMELCQND QILLLKSGCL 310 320 330 340 350 360 EVVLVRMCRA FNPLNNTVLF EGKYGGMQMF KALGSDDLVN EAFDFAKNLC SLQLTEEEIA 370 380 390 400 410 420 LFSSAVLISP DRAWLLEPRK VQKLQEKIYF ALQHVIQKNH LDDETLAKLI AKIPTITAVC 430 440 450 NLHGEKLQVF KQSHPDIVNT LFPPLYKELF NPDCAAVCK

References

[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, TISSUE SPECIFICITY.
[3]	"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 PEPTIDE SRC-1.
[4]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L14610 Genomic DNA. Translation: AAA42095.1. Different initiation.

IPI

IPI00208302.
IPI00829487.

PIR

I65219.

UniGene

Rn.231652.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P45446.

SMR

P45446. Positions 18-98, 219-462.

ModBase

Search...

Protein-protein interaction databases

STRING

10116.ENSRNOP00000018137.

PTM databases

PhosphoSite

P45446.

Proteomic databases

PaxDb

P45446.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

UCSC

RGD:1306778. rat.

Organism-specific databases

RGD

1306778. Rorb.

Phylogenomic databases

eggNOG

NOG324222.

HOGENOM

HOG000010200.

HOVERGEN

HBG106848.

InParanoid

P45446.

OrthoDB

EOG4KH2TT.

Gene expression databases

ArrayExpress

P45446.

Genevestigator

P45446.

GermOnline

ENSRNOG00000013413. Rattus norvegicus.

Family and domain databases

Gene3D

1.10.565.10. 2 hits.
3.30.50.10. 1 hit.

InterPro

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]

Pfam

PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]

PRINTS

PR01293. RORNUCRECPTR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.

SMART

SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]

SUPFAM

SSF48508. Str_ncl_receptor. 1 hit.

PROSITE

PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P45446.

Entry information

Entry name

RORB_RAT

Accession

Primary (citable) accession number: P45446

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 119 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program