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   21-SEP-2011, entry version 63.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Hypothalamus;
RX   MEDLINE=98150861; PubMed=9491897; DOI=10.1016/S0092-8674(00)80949-6;
RA   Sakurai T., Amemiya A., Ishii M., Matsuzaki I., Chemelli R.M.,
RA   Tanaka H., Williams S.C., Richardson J.A., Kozlowski G.P., Wilson S.,
RA   Arch J.R.S., Buckingham R.E., Haynes A.C., Carr S.A., Annan R.S.,
RA   McNulty D.E., Liu W.-S., Terrett J.A., Elshourbagy N.A., Bergsma D.J.,
RA   Yanagisawa M.;
RT   "Orexins and orexin receptors: a family of hypothalamic neuropeptides
RT   and G protein-coupled receptors that regulate feeding behavior.";
RL   Cell 92:573-585(1998).
CC   -!- FUNCTION: Neuropeptides that play a significant role in the
CC       regulation of food intake and sleep-wakefulness, possibly by
CC       coordinating the complex behavioral and physiologic responses of
CC       these complementary homeostatic functions. A broader role in the
CC       homeostatic regulation of energy metabolism, autonomic function,
CC       hormonal balance and the regulation of body fluids, is also
CC       suggested. Orexin-A binds to both OX1R and OX2R with a high
CC       affinity, whereas orexin-B binds only to OX2R with a similar high
CC       affinity (By similarity).
CC   -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum (By similarity).
CC       Cytoplasmic vesicle (By similarity). Cell junction, synapse (By
CC       similarity). Note=Associated with perikaryal rough endoplasmic
CC       reticulum as well as cytoplasmic large granular vesicles at
CC       synapses (By similarity).
CC   -!- SIMILARITY: Belongs to the orexin family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Qui dort dine - Issue
CC       15 of October 2001;
CC       URL="http://web.expasy.org/spotlight/back_issues/sptlt015.shtml";
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DR   IPI; IPI00695657; -.
DR   UniGene; Bt.13040; -.
DR   ProteinModelPortal; P56717; -.
DR   SMR; P56717; 1-33.
DR   STRING; P56717; -.
DR   eggNOG; maNOG21262; -.
DR   InParanoid; P56717; -.
DR   OrthoDB; EOG408N9S; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0007631; P:feeding behavior; IEA:InterPro.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR001704; Orexin.
DR   PANTHER; PTHR15173; Orexin; 1.
DR   Pfam; PF02072; Orexin; 1.
DR   PRINTS; PR01091; OREXINPP.
PE   1: Evidence at protein level;
KW   Amidation; Cell junction; Complete proteome; Cytoplasmic vesicle;
KW   Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW   Neuropeptide; Pyrrolidone carboxylic acid; Reference proteome;
KW   Synapse.
FT   PEPTIDE       1     33       Orexin-A.
FT                                /FTId=PRO_0000044769.
FT   MOD_RES       1      1       Pyrrolidone carboxylic acid (By
FT                                similarity).
FT   MOD_RES      33     33       Leucine amide (By similarity).
FT   DISULFID      6     12       By similarity.
FT   DISULFID      7     14       By similarity.
SQ   SEQUENCE   33 AA;  3583 MW;  8C16A02AA7CBFBD5 CRC64;
     QPLPDCCRQK TCSCRLYELL HGAGNHAAGI LTL
//