OREX_CANLF
ID OREX_CANLF Reviewed; 130 AA.
AC Q9GLF6;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-30.
RX PubMed=11282968; DOI=10.1101/gr.gr-1610r;
RA Hungs M., Fan J., Lin L., Lin X., Maki R.A., Mignot E.;
RT "Identification and functional analysis of mutations in the hypocretin
RT (orexin) genes of narcoleptic canines.";
RL Genome Res. 11:531-539(2001).
RN [2]
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 [3]
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. Orexin-A binds to both
CC OX1R and OX2R with a high affinity, whereas orexin-B binds only to OX2R
CC with a similar high affinity.
CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum {ECO:0000250}.
CC Cytoplasmic vesicle {ECO:0000250}. Synapse {ECO:0000250}.
CC Note=Associated with perikaryal rough endoplasmic reticulum as well as
CC cytoplasmic large granular vesicles at synapses. {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages at paired basic residues yield the
CC different active peptides.
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; AF285110; AAG13965.1; -; Genomic_DNA.
DR RefSeq; NP_001029166.1; NM_001033994.1.
DR RefSeq; XP_005624415.1; XM_005624358.1.
DR AlphaFoldDB; Q9GLF6; -.
DR STRING; 9615.ENSCAFP00000022949; -.
DR PaxDb; Q9GLF6; -.
DR Ensembl; ENSCAFT00030000402; ENSCAFP00030000352; ENSCAFG00030000255.
DR Ensembl; ENSCAFT00040016053; ENSCAFP00040013910; ENSCAFG00040008609.
DR Ensembl; ENSCAFT00845017785; ENSCAFP00845013852; ENSCAFG00845010112.
DR GeneID; 607641; -.
DR KEGG; cfa:607641; -.
DR CTD; 3060; -.
DR VEuPathDB; HostDB:ENSCAFG00845010112; -.
DR eggNOG; ENOG502S83I; Eukaryota.
DR GeneTree; ENSGT00390000014272; -.
DR HOGENOM; CLU_149027_1_0_1; -.
DR InParanoid; Q9GLF6; -.
DR OMA; HPCPGRR; -.
DR OrthoDB; 1586513at2759; -.
DR TreeFam; TF330756; -.
DR Reactome; R-CFA-389397; Orexin and neuropeptides FF and QRFP bind to their respective receptors.
DR Reactome; R-CFA-416476; G alpha (q) signalling events.
DR Proteomes; UP000002254; Chromosome 9.
DR Bgee; ENSCAFG00000015615; Expressed in smooth muscle tissue and 28 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0005184; F:neuropeptide hormone activity; IBA:GO_Central.
DR GO; GO:0031771; F:type 1 hypocretin receptor binding; IBA:GO_Central.
DR GO; GO:0031772; F:type 2 hypocretin receptor binding; IBA:GO_Central.
DR GO; GO:0042755; P:eating behavior; IBA:GO_Central.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:0051971; P:positive regulation of transmission of nerve impulse; IBA:GO_Central.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IBA:GO_Central.
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; IBA:GO_Central.
DR InterPro; IPR001704; Orexin.
DR PANTHER; PTHR15173; PTHR15173; 1.
DR Pfam; PF02072; Orexin; 1.
DR PIRSF; PIRSF037824; Orexin; 1.
DR PRINTS; PR01091; OREXINPP.
PE 3: Inferred from homology;
KW Amidation; Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW Disulfide bond; Endoplasmic reticulum; Neuropeptide;
KW Pyrrolidone carboxylic acid; Reference proteome; Signal; Synapse.
FT SIGNAL 1..32
FT /evidence="ECO:0000250"
FT PEPTIDE 33..65
FT /note="Orexin-A"
FT /id="PRO_0000020258"
FT PEPTIDE 69..96
FT /note="Orexin-B"
FT /id="PRO_0000020259"
FT PROPEP 97..130
FT /id="PRO_0000020260"
FT MOD_RES 33
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:O55232"
FT MOD_RES 65
FT /note="Leucine amide"
FT /evidence="ECO:0000250"
FT MOD_RES 96
FT /note="Methionine amide"
FT /evidence="ECO:0000250"
FT DISULFID 38..44
FT /evidence="ECO:0000250"
FT DISULFID 39..46
FT /evidence="ECO:0000250"
FT VARIANT 30
FT /note="A -> T"
FT /evidence="ECO:0000269|PubMed:11282968"
SQ SEQUENCE 130 AA; 13328 MW; 2BF59D4C1E422DF3 CRC64;
MNPPSTKVPW AAVTLLLLLL LPPALLSPGA AAQPLPDCCR QKTCSCRLYE LLHGAGNHAA
GILTLGKRRP GPPGLQGRLQ RLLQASGNHA AGILTMGRRA GAEPAPRPCP GRRCPVVAVP
SAAPGGRSGV
