OREX_RAT
ID OREX_RAT Reviewed; 130 AA.
AC O55232;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Orexin;
DE AltName: Full=Hypocretin;
DE Short=Hcrt;
DE Contains:
DE RecName: Full=Orexin-A;
DE AltName: Full=Hypocretin-1;
DE Short=Hcrt1;
DE Contains:
DE RecName: Full=Orexin-B;
DE AltName: Full=Hypocretin-2;
DE Short=Hcrt2;
DE Flags: Precursor;
GN Name=Hcrt; Synonyms=Ox, Ppox;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 33-65 AND 69-96,
RP PYROGLUTAMATE FORMATION AT GLN-33, AMIDATION AT LEU-65 AND MET-96, AND MASS
RP SPECTROMETRY.
RC TISSUE=Brain;
RX PubMed=9491897; DOI=10.1016/s0092-8674(00)80949-6;
RA Sakurai T., Amemiya A., Ishii M., Matsuzaki I., Chemelli R.M., Tanaka H.,
RA Williams S.C., Richardson J.A., Kozlowski G.P., Wilson S., Arch J.R.S.,
RA Buckingham R.E., Haynes A.C., Carr S.A., Annan R.S., McNulty D.E.,
RA Liu W.-S., Terrett J.A., Elshourbagy N.A., Bergsma D.J., Yanagisawa M.;
RT "Orexins and orexin receptors: a family of hypothalamic neuropeptides and G
RT protein-coupled receptors that regulate feeding behavior.";
RL Cell 92:573-585(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=9419374; DOI=10.1073/pnas.95.1.322;
RA de Lecea L., Kilduff T.S., Peyron C., Gao X.-B., Foye P.E., Danielson P.E.,
RA Fukuhara C., Battenberg E.L.F., Gautvik V.T., Bartlett F.S. II,
RA Frankel W.N., van den Pol A.N., Bloom F.E., Gautvik K.M., Sutcliffe J.G.;
RT "The hypocretins: hypothalamus-specific peptides with neuroexcitatory
RT activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:322-327(1998).
RN [3]
RP REVIEW.
RX PubMed=11340621; DOI=10.1002/bies.1058;
RA Hungs M., Mignot E.;
RT "Hypocretin/orexin, sleep and narcolepsy.";
RL Bioessays 23:397-408(2001).
RN [4]
RP REVIEW.
RX PubMed=11283317; DOI=10.1146/annurev.neuro.24.1.429;
RA Willie J.T., Chemelli R.M., Sinton C.M., Yanagisawa M.;
RT "To eat or to sleep? Orexin in the regulation of feeding and wakefulness.";
RL Annu. Rev. Neurosci. 24:429-458(2001).
CC -!- FUNCTION: Neuropeptides that play a significant role in the regulation
CC of food intake and sleep-wakefulness, possibly by coordinating the
CC complex behavioral and physiologic responses of these complementary
CC homeostatic functions. A broader role in the homeostatic regulation of
CC energy metabolism, autonomic function, hormonal balance and the
CC regulation of body fluids, is also suggested. A modulation effect on
CC luteinizing hormone-releasing hormone (LHRH) secretion also suggests a
CC more minor contribution to the regulation of reproductive function.
CC Orexin-A binds to both OX1R and OX2R with a high affinity, whereas
CC orexin-B binds only to OX2R with a similar high affinity.
CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum. Note=Associated with
CC perikaryal rough endoplasmic reticulum as well as cytoplasmic large
CC granular vesicles at synapses.
CC -!- TISSUE SPECIFICITY: Produced by a small group of neurons restricted to
CC the lateral and posterior hypothalamus and perifornical areas. Positive
CC neurons project widely throughout the entire neuroaxis. Particularly
CC abundant projections in the cerebral cortex, olfactory bulb,
CC hippocampus, amygdala, septum, diagonal band of Broca, bed nucleus of
CC the stria terminalis, thalamus, anterior and posterior hypothalamus,
CC midbrain, brainstem, and spinal cord. Immunoreactivity reported in the
CC enteric nervous system and pancreas. In small amount, also detected in
CC the testis.
CC -!- DEVELOPMENTAL STAGE: Detected as early as embryonic day 18, but
CC expression increased dramatically after the third postnatal week.
CC -!- INDUCTION: By nutritional state, up-regulated by fasting, fluid
CC deprivation and insulin-induced hypoglycemia. Orexin-A immunoreactivity
CC varies diurnally and peaks during the dark phase, in the pons and the
CC location of locus coeruleus.
CC -!- PTM: Specific enzymatic cleavages at paired basic residues yield the
CC different active peptides.
CC -!- MASS SPECTROMETRY: [Orexin-A]: Mass=3558.7; Mass_error=0.1;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:9491897};
CC -!- SIMILARITY: Belongs to the orexin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Qui dort dine - Issue 15 of
CC October 2001;
CC URL="https://web.expasy.org/spotlight/back_issues/015";
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DR EMBL; AF041241; AAC40039.1; -; mRNA.
DR EMBL; AF019565; AAC02933.1; -; mRNA.
DR RefSeq; NP_037311.1; NM_013179.2.
DR AlphaFoldDB; O55232; -.
DR STRING; 10116.ENSRNOP00000025547; -.
DR PaxDb; O55232; -.
DR Ensembl; ENSRNOT00000025547; ENSRNOP00000025547; ENSRNOG00000018892.
DR GeneID; 25723; -.
DR KEGG; rno:25723; -.
DR UCSC; RGD:2786; rat.
DR CTD; 3060; -.
DR RGD; 2786; Hcrt.
DR eggNOG; ENOG502S83I; Eukaryota.
DR GeneTree; ENSGT00390000014272; -.
DR HOGENOM; CLU_149027_1_0_1; -.
DR InParanoid; O55232; -.
DR OMA; HPCPGRR; -.
DR OrthoDB; 1586513at2759; -.
DR PhylomeDB; O55232; -.
DR TreeFam; TF330756; -.
DR Reactome; R-RNO-389397; Orexin and neuropeptides FF and QRFP bind to their respective receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR PRO; PR:O55232; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000018892; Expressed in testis and 3 other tissues.
DR Genevisible; O55232; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0005184; F:neuropeptide hormone activity; IDA:RGD.
DR GO; GO:0031771; F:type 1 hypocretin receptor binding; IDA:RGD.
DR GO; GO:0031772; F:type 2 hypocretin receptor binding; IDA:RGD.
DR GO; GO:0001662; P:behavioral fear response; NAS:RGD.
DR GO; GO:0042755; P:eating behavior; IDA:RGD.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IDA:RGD.
DR GO; GO:0007631; P:feeding behavior; NAS:RGD.
DR GO; GO:0008156; P:negative regulation of DNA replication; IDA:RGD.
DR GO; GO:0043267; P:negative regulation of potassium ion transport; IDA:RGD.
DR GO; GO:0051970; P:negative regulation of transmission of nerve impulse; IDA:RGD.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; IMP:RGD.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD.
DR GO; GO:0051971; P:positive regulation of transmission of nerve impulse; IDA:RGD.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IDA:RGD.
DR GO; GO:0042594; P:response to starvation; IBA:GO_Central.
DR GO; GO:0030431; P:sleep; IBA:GO_Central.
DR GO; GO:0001659; P:temperature homeostasis; IDA:RGD.
DR InterPro; IPR001704; Orexin.
DR PANTHER; PTHR15173; PTHR15173; 1.
DR Pfam; PF02072; Orexin; 1.
DR PIRSF; PIRSF037824; Orexin; 1.
DR PRINTS; PR01091; OREXINPP.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Endoplasmic reticulum; Neuropeptide;
KW Pyrrolidone carboxylic acid; Reference proteome; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:9491897"
FT PEPTIDE 33..65
FT /note="Orexin-A"
FT /id="PRO_0000020270"
FT PEPTIDE 69..96
FT /note="Orexin-B"
FT /id="PRO_0000020271"
FT PROPEP 97..130
FT /id="PRO_0000020272"
FT MOD_RES 33
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:9491897"
FT MOD_RES 65
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:9491897"
FT MOD_RES 96
FT /note="Methionine amide"
FT /evidence="ECO:0000269|PubMed:9491897"
FT DISULFID 38..44
FT DISULFID 39..46
SQ SEQUENCE 130 AA; 13645 MW; 00CAB259EDF2A404 CRC64;
MNLPSTKVPW AAVTLLLLLL LPPALLSLGV DAQPLPDCCR QKTCSCRLYE LLHGAGNHAA
GILTLGKRRP GPPGLQGRLQ RLLQANGNHA AGILTMGRRA GAELEPYPCP GRRCPTATAT
ALAPRGGSRV
