ID   OREX_PIG                Reviewed;         131 AA.
AC   O77668; Q000Y9; Q9TTA6;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   24-JAN-2024, entry version 132.
DE   RecName: Full=Hypocretin neuropeptide precursor {ECO:0000250|UniProtKB:O55232};
DE   AltName: Full=Hypocretin {ECO:0000250|UniProtKB:O55232};
DE            Short=Hcrt {ECO:0000250|UniProtKB:O55232};
DE   AltName: Full=Orexin precursor {ECO:0000250|UniProtKB:O55232};
DE   AltName: Full=Prepro-orexin {ECO:0000303|PubMed:10343916};
DE   AltName: Full=Preprohypocretin {ECO:0000250|UniProtKB:O55232};
DE   Contains:
DE     RecName: Full=Orexin-A {ECO:0000303|PubMed:10343916};
DE     AltName: Full=Hypocretin-1 {ECO:0000250|UniProtKB:O55232};
DE              Short=Hcrt1 {ECO:0000305};
DE   Contains:
DE     RecName: Full=Orexin-B {ECO:0000303|PubMed:10343916};
DE     AltName: Full=Hypocretin-2 {ECO:0000250|UniProtKB:O55232};
DE              Short=Hcrt2 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=HCRT; Synonyms=ORX, OX, PPOX;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SYNTHESIS OF OREXIN-B.
RC   TISSUE=Hypothalamus;
RX   PubMed=10343916; DOI=10.1016/s0739-7240(99)00011-9;
RA   Dyer C.J., Touchette K.J., Carroll J.A., Allee G.L., Matteri R.L.;
RT   "Cloning of porcine prepro-orexin cDNA and effects of an intramuscular
RT   injection of synthetic porcine orexin-B on feed intake in young pigs.";
RL   Domest. Anim. Endocrinol. 16:145-148(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA   Guo H.H., Wang L.X.;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-131.
RX   PubMed=10754114; DOI=10.1007/s003350010064;
RA   Malek M., Marklund S., Dyer C., Matteri R.L., Rothschild M.F.;
RT   "Linkage and physical mapping of the porcine prepro-orexin gene.";
RL   Mamm. Genome 11:342-343(2000).
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.
CC       {ECO:0000250|UniProtKB:O55232}.
CC   -!- FUNCTION: [Orexin-A]: Binds to orexin receptors HCRTR1/OX1R and
CC       HCRTR2/OX2R with a high affinity (By similarity). Stimulates food
CC       intake (By similarity). Modulates pituitary luteinizing hormone
CC       secretion in an ovarian steroid-dependent manner (By similarity).
CC       {ECO:0000250|UniProtKB:O55232}.
CC   -!- FUNCTION: [Orexin-B]: Binds to orexin receptor HCRTR2/OX2R only (By
CC       similarity). Stimulates food intake (By similarity). Modulates
CC       pituitary luteinizing hormone secretion in an ovarian steroid-dependent
CC       manner (By similarity). {ECO:0000250|UniProtKB:O55232}.
CC   -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:O55232}. Cytoplasmic vesicle
CC       {ECO:0000250|UniProtKB:O55232}. Synapse {ECO:0000250|UniProtKB:O55232}.
CC       Note=Associated with perikaryal rough endoplasmic reticulum as well as
CC       cytoplasmic large granular vesicles at synapses.
CC       {ECO:0000250|UniProtKB:O55232}.
CC   -!- PTM: Specific enzymatic cleavages at paired basic residues yield the
CC       different active peptides. {ECO:0000250|UniProtKB:O55232}.
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";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF075241; AAC26827.1; -; mRNA.
DR   EMBL; DQ985365; ABJ15704.1; -; Genomic_DNA.
DR   EMBL; EF434654; ABO15568.1; -; Genomic_DNA.
DR   EMBL; EF434655; ABO15569.1; -; mRNA.
DR   EMBL; AF169352; AAF24216.1; -; Genomic_DNA.
DR   RefSeq; NP_999321.1; NM_214156.2.
DR   RefSeq; XP_013836403.1; XM_013980949.1.
DR   RefSeq; XP_013836404.1; XM_013980950.1.
DR   RefSeq; XP_013836405.1; XM_013980951.1.
DR   AlphaFoldDB; O77668; -.
DR   STRING; 9823.ENSSSCP00000018447; -.
DR   PaxDb; 9823-ENSSSCP00000018447; -.
DR   PeptideAtlas; O77668; -.
DR   Ensembl; ENSSSCT00000018952.5; ENSSSCP00000018447.2; ENSSSCG00000017410.5.
DR   Ensembl; ENSSSCT00015041351.1; ENSSSCP00015016338.1; ENSSSCG00015031170.1.
DR   Ensembl; ENSSSCT00025029933.1; ENSSSCP00025012727.1; ENSSSCG00025021994.1.
DR   Ensembl; ENSSSCT00030094217.1; ENSSSCP00030043432.1; ENSSSCG00030067357.1.
DR   Ensembl; ENSSSCT00035024083.1; ENSSSCP00035009010.1; ENSSSCG00035018642.1.
DR   Ensembl; ENSSSCT00040026553.1; ENSSSCP00040011228.1; ENSSSCG00040019667.1.
DR   Ensembl; ENSSSCT00045066309.1; ENSSSCP00045047015.1; ENSSSCG00045038270.1.
DR   Ensembl; ENSSSCT00050093034.1; ENSSSCP00050040132.1; ENSSSCG00050068177.1.
DR   Ensembl; ENSSSCT00055057785.1; ENSSSCP00055046237.1; ENSSSCG00055029101.1.
DR   Ensembl; ENSSSCT00060078546.1; ENSSSCP00060033937.1; ENSSSCG00060057653.1.
DR   Ensembl; ENSSSCT00065008106.1; ENSSSCP00065003401.1; ENSSSCG00065006053.1.
DR   Ensembl; ENSSSCT00070028107.1; ENSSSCP00070023404.1; ENSSSCG00070014330.1.
DR   GeneID; 397305; -.
DR   KEGG; ssc:397305; -.
DR   CTD; 3060; -.
DR   VGNC; VGNC:88806; HCRT.
DR   eggNOG; ENOG502S83I; Eukaryota.
DR   GeneTree; ENSGT00390000014272; -.
DR   HOGENOM; CLU_149027_1_0_1; -.
DR   InParanoid; O77668; -.
DR   OMA; HPCPGRR; -.
DR   OrthoDB; 5357074at2759; -.
DR   TreeFam; TF330756; -.
DR   Reactome; R-SSC-389397; Orexin and neuropeptides FF and QRFP bind to their respective receptors.
DR   Reactome; R-SSC-416476; G alpha (q) signalling events.
DR   Proteomes; UP000008227; Chromosome 12.
DR   Proteomes; UP000314985; Chromosome 12.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   Bgee; ENSSSCG00000017410; Expressed in oocyte and 25 other cell types or tissues.
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 orexin receptor binding; IBA:GO_Central.
DR   GO; GO:0031772; F:type 2 orexin 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; OREXIN; 1.
DR   PANTHER; PTHR15173:SF2; OREXIN; 1.
DR   Pfam; PF02072; Orexin; 1.
DR   PIRSF; PIRSF037824; Orexin; 1.
DR   PRINTS; PR01091; OREXINPP.
DR   Genevisible; O77668; SS.
PE   2: Evidence at transcript level;
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..33
FT                   /evidence="ECO:0000250|UniProtKB:O55232"
FT   PEPTIDE         34..66
FT                   /note="Orexin-A"
FT                   /evidence="ECO:0000250|UniProtKB:O55232"
FT                   /id="PRO_0000020267"
FT   PEPTIDE         70..97
FT                   /note="Orexin-B"
FT                   /evidence="ECO:0000250|UniProtKB:O55232"
FT                   /id="PRO_0000020268"
FT   PROPEP          98..131
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:O55232"
FT                   /id="PRO_0000020269"
FT   MOD_RES         34
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:O55232"
FT   MOD_RES         66
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000250|UniProtKB:O55232"
FT   MOD_RES         97
FT                   /note="Methionine amide"
FT                   /evidence="ECO:0000250|UniProtKB:O55232"
FT   DISULFID        39..45
FT                   /evidence="ECO:0000250|UniProtKB:O55232"
FT   DISULFID        40..47
FT                   /evidence="ECO:0000250|UniProtKB:O55232"
SQ   SEQUENCE   131 AA;  13457 MW;  665A74448429AB1F CRC64;
     MNPPFAKVSW ATVTLLLLLL LLPPAVLSPG AAAQPLPDCC RQKTCSCRLY ELLHGAGNHA
     AGILTLGKRR PGPPGLQGRL QRLLQASGNH AAGILTMGRR AGAEPAPRLC PGRRCLAAAA
     SSVAPGGRSG I
//