ID   OREX_BOVIN              Reviewed;          33 AA.
AC   P56717;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Orexin-A;
DE   AltName: Full=Hypocretin-1;
DE            Short=Hcrt1;
GN   Name=HCRT; Synonyms=OX, PPOX;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Hypothalamus;
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).
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 (By similarity). {ECO:0000250}.
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   -!- 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   AlphaFoldDB; P56717; -.
DR   STRING; 9913.ENSBTAP00000000875; -.
DR   PaxDb; P56717; -.
DR   eggNOG; ENOG502S83I; Eukaryota.
DR   HOGENOM; CLU_149027_1_0_1; -.
DR   Proteomes; UP000009136; Unplaced.
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: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   PRINTS; PR01091; OREXINPP.
PE   1: Evidence at protein level;
KW   Amidation; Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond;
KW   Endoplasmic reticulum; Neuropeptide; Pyrrolidone carboxylic acid;
KW   Reference proteome; Synapse.
FT   PEPTIDE         1..33
FT                   /note="Orexin-A"
FT                   /id="PRO_0000044769"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:O55232"
FT   MOD_RES         33
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        6..12
FT                   /evidence="ECO:0000250"
FT   DISULFID        7..14
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   33 AA;  3583 MW;  8C16A02AA7CBFBD5 CRC64;
     QPLPDCCRQK TCSCRLYELL HGAGNHAAGI LTL