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O55232 (OREX_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Orexin
Alternative name(s):
Hypocretin
Short name=Hcrt

Cleaved into the following 2 chains:

  1. Orexin-A
    Alternative name(s):
    Hypocretin-1
    Short name=Hcrt1
  2. Orexin-B
    Alternative name(s):
    Hypocretin-2
    Short name=Hcrt2
Gene names
Name:Hcrt
Synonyms:Ox, Ppox
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length130 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Neuropeptides that play a significant role in the regulation of food intake and sleep-wakefulness, possibly by coordinating the complex behavioral and physiologic responses of these complementary homeostatic functions. A broader role in the homeostatic regulation of energy metabolism, autonomic function, hormonal balance and the regulation of body fluids, is also suggested. A modulation effect on luteinizing hormone-releasing hormone (LHRH) secretion also suggests a more minor contribution to the regulation of reproductive function. Orexin-A binds to both OX1R and OX2R with a high affinity, whereas orexin-B binds only to OX2R with a similar high affinity.

Subcellular location

Rough endoplasmic reticulum. Note: Associated with perikaryal rough endoplasmic reticulum as well as cytoplasmic large granular vesicles at synapses.

Tissue specificity

Produced by a small group of neurons restricted to the lateral and posterior hypothalamus and perifornical areas. Positive neurons project widely throughout the entire neuroaxis. Particularly abundant projections in the cerebral cortex, olfactory bulb, hippocampus, amygdala, septum, diagonal band of Broca, bed nucleus of the stria terminalis, thalamus, anterior and posterior hypothalamus, midbrain, brainstem, and spinal cord. Immunoreactivity reported in the enteric nervous system and pancreas. In small amount, also detected in the testis.

Developmental stage

Detected as early as embryonic day 18, but expression increased dramatically after the third postnatal week.

Induction

By nutritional state, up-regulated by fasting, fluid deprivation and insulin-induced hypoglycemia. Orexin-A immunoreactivity varies diurnally and peaks during the dark phase, in the pons and the location of locus coeruleus.

Post-translational modification

Specific enzymatic cleavages at paired basic residues yield the different active peptides.

Sequence similarities

Belongs to the orexin family.

Mass spectrometry

Molecular mass is 3558.7±0.1 Da from positions 33 - 65. Determined by MALDI. Ref.1

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   DomainSignal
   Molecular functionNeuropeptide
   PTMAmidation
Cleavage on pair of basic residues
Disulfide bond
Pyrrolidone carboxylic acid
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbehavioral fear response

Non-traceable author statement PubMed 14614918. Source: RGD

eating behavior

Inferred from direct assay PubMed 15961555. Source: RGD

feeding behavior

Non-traceable author statement PubMed 12679367. Source: RGD

negative regulation of DNA replication

Inferred from direct assay PubMed 16141395. Source: RGD

negative regulation of potassium ion transport

Inferred from direct assay PubMed 16247802. Source: RGD

negative regulation of transmission of nerve impulse

Inferred from direct assay PubMed 15746258. Source: RGD

neuropeptide signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

phospholipase C-activating G-protein coupled receptor signaling pathway

Inferred from mutant phenotype PubMed 16247802. Source: RGD

positive regulation of calcium ion transport

Inferred from mutant phenotype PubMed 15858425. Source: RGD

positive regulation of cytosolic calcium ion concentration

Inferred from direct assay PubMed 15858425. Source: RGD

positive regulation of transmission of nerve impulse

Inferred from direct assay PubMed 15746258. Source: RGD

protein kinase C-activating G-protein coupled receptor signaling pathway

Inferred from mutant phenotype PubMed 16247802. Source: RGD

regulation of excitatory postsynaptic membrane potential

Inferred from direct assay PubMed 16247802. Source: RGD

regulation of neurotransmitter secretion

Inferred from direct assay PubMed 15664710. Source: RGD

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 16141395. Source: RGD

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

rough endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

secretory granule

Inferred from direct assay Ref.2. Source: RGD

   Molecular_functionneuropeptide hormone activity

Inferred from direct assay PubMed 16247802. Source: RGD

type 1 hypocretin receptor binding

Inferred from direct assay PubMed 12890892. Source: RGD

type 2 hypocretin receptor binding

Inferred from direct assay PubMed 12890892. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Ref.1
Peptide33 – 6533Orexin-A Ref.1
PRO_0000020270
Peptide69 – 9628Orexin-B
PRO_0000020271
Propeptide97 – 13034
PRO_0000020272

Amino acid modifications

Modified residue331Pyrrolidone carboxylic acid
Modified residue651Leucine amide
Modified residue961Methionine amide
Disulfide bond38 ↔ 44
Disulfide bond39 ↔ 46

Sequences

Sequence LengthMass (Da)Tools
O55232 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 00CAB259EDF2A404

FASTA13013,645
        10         20         30         40         50         60 
MNLPSTKVPW AAVTLLLLLL LPPALLSLGV DAQPLPDCCR QKTCSCRLYE LLHGAGNHAA 

        70         80         90        100        110        120 
GILTLGKRRP GPPGLQGRLQ RLLQANGNHA AGILTMGRRA GAELEPYPCP GRRCPTATAT 

       130 
ALAPRGGSRV 

« Hide

References

[1]"Orexins and orexin receptors: a family of hypothalamic neuropeptides and G protein-coupled receptors that regulate feeding behavior."
Sakurai T., Amemiya A., Ishii M., Matsuzaki I., Chemelli R.M., Tanaka H., Williams S.C., Richardson J.A., Kozlowski G.P., Wilson S., Arch J.R.S., Buckingham R.E., Haynes A.C., Carr S.A., Annan R.S., McNulty D.E., Liu W.-S., Terrett J.A. expand/collapse author list , Elshourbagy N.A., Bergsma D.J., Yanagisawa M.
Cell 92:573-585(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 33-65 AND 69-96, MASS SPECTROMETRY.
Tissue: Brain.
[2]"The hypocretins: hypothalamus-specific peptides with neuroexcitatory activity."
de Lecea L., Kilduff T.S., Peyron C., Gao X.-B., Foye P.E., Danielson P.E., Fukuhara C., Battenberg E.L.F., Gautvik V.T., Bartlett F.S. II, Frankel W.N., van den Pol A.N., Bloom F.E., Gautvik K.M., Sutcliffe J.G.
Proc. Natl. Acad. Sci. U.S.A. 95:322-327(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
[3]"Hypocretin/orexin, sleep and narcolepsy."
Hungs M., Mignot E.
Bioessays 23:397-408(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[4]"To eat or to sleep? Orexin in the regulation of feeding and wakefulness."
Willie J.T., Chemelli R.M., Sinton C.M., Yanagisawa M.
Annu. Rev. Neurosci. 24:429-458(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Qui dort dine - Issue 15 of October 2001

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF041241 mRNA. Translation: AAC40039.1.
AF019565 mRNA. Translation: AAC02933.1.
RefSeqNP_037311.1. NM_013179.2.
UniGeneRn.7628.

3D structure databases

ProteinModelPortalO55232.
SMRO55232. Positions 33-65, 71-96.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000025547.

Proteomic databases

PRIDEO55232.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000025547; ENSRNOP00000025547; ENSRNOG00000018892.
GeneID25723.
KEGGrno:25723.
UCSCRGD:2786. rat.

Organism-specific databases

CTD3060.
RGD2786. Hcrt.

Phylogenomic databases

eggNOGNOG70925.
GeneTreeENSGT00390000014272.
HOGENOMHOG000230990.
HOVERGENHBG000256.
InParanoidO55232.
KOK05246.
OMAKVSWATV.
OrthoDBEOG7XSTHD.
PhylomeDBO55232.
TreeFamTF330756.

Gene expression databases

GenevestigatorO55232.

Family and domain databases

InterProIPR001704. Orexin.
[Graphical view]
PANTHERPTHR15173. PTHR15173. 1 hit.
PfamPF02072. Orexin. 1 hit.
[Graphical view]
PIRSFPIRSF037824. Orexin. 1 hit.
PRINTSPR01091. OREXINPP.
ProtoNetSearch...

Other

NextBio607825.
PROO55232.

Entry information

Entry nameOREX_RAT
AccessionPrimary (citable) accession number: O55232
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: April 16, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries