CRF_SHEEP
ID CRF_SHEEP Reviewed; 190 AA.
AC P01142;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Corticoliberin;
DE AltName: Full=Corticotropin-releasing factor;
DE Short=CRF;
DE AltName: Full=Corticotropin-releasing hormone;
DE AltName: Full=Endorpholiberin;
DE Flags: Precursor;
GN Name=CRH;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6600512; DOI=10.1038/301537a0;
RA Furutani Y., Morimoto Y., Shibahara S., Noda M., Takahashi H., Hirose T.,
RA Asai M., Inayama S., Hayashida H., Miyata T., Numa S.;
RT "Cloning and sequence analysis of cDNA for ovine corticotropin-releasing
RT factor precursor.";
RL Nature 301:537-540(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=3265687; DOI=10.1016/0378-1119(88)90059-5;
RA Roche P.J., Crawford R.J., Fernley R.T., Tregear G.W., Coghlan J.P.;
RT "Nucleotide sequence of the gene coding for ovine corticotropin-releasing
RT factor and regulation of its mRNA levels by glucocorticoids.";
RL Gene 71:421-431(1988).
RN [3]
RP PROTEIN SEQUENCE OF 148-188, FUNCTION, AMIDATION AT ALA-188, AND
RP SUBCELLULAR LOCATION.
RX PubMed=6273874; DOI=10.1073/pnas.78.10.6517;
RA Spiess J., Rivier J., Rivier C., Vale W.;
RT "Primary structure of corticotropin-releasing factor from ovine
RT hypothalamus.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:6517-6521(1981).
RN [4]
RP PROTEIN SEQUENCE OF 148-188, SYNTHESIS OF 148-188, AND FUNCTION.
RX PubMed=6267699; DOI=10.1126/science.6267699;
RA Vale W., Spiess J., Rivier C., Rivier J.;
RT "Characterization of a 41-residue ovine hypothalamic peptide that
RT stimulates secretion of corticotropin and beta-endorphin.";
RL Science 213:1394-1397(1981).
RN [5]
RP PROTEIN SEQUENCE OF 148-188.
RX PubMed=2647152; DOI=10.1016/0167-4838(89)90226-4;
RA Audhya T., Hollander C.S., Schlesinger D.H., Hutchinson B.;
RT "Structural characterization and localization of corticotropin-releasing
RT factor in testis.";
RL Biochim. Biophys. Acta 995:10-16(1989).
CC -!- FUNCTION: Hormone regulating the release of corticotropin from
CC pituitary gland (PubMed:6267699, PubMed:6273874). Induces NLRP6 in
CC intestinal epithelial cells, hence may influence gut microbiota profile
CC (By similarity). {ECO:0000250|UniProtKB:Q8CIT0,
CC ECO:0000269|PubMed:6267699, ECO:0000269|PubMed:6273874}.
CC -!- SUBUNIT: Interacts (via C-terminus) with CRFR1 (via N-terminal
CC extracellular domain). {ECO:0000250|UniProtKB:P06850}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6273874}.
CC -!- TISSUE SPECIFICITY: Produced by the hypothalamus.
CC {ECO:0000269|PubMed:3265687}.
CC -!- SIMILARITY: Belongs to the sauvagine/corticotropin-releasing
CC factor/urotensin I family. {ECO:0000305}.
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DR EMBL; J00803; AAA31512.1; -; mRNA.
DR EMBL; M22853; AAA31513.1; -; Genomic_DNA.
DR PIR; JS0030; RHSHCE.
DR AlphaFoldDB; P01142; -.
DR STRING; 9940.ENSOARP00000018668; -.
DR eggNOG; ENOG502S25G; Eukaryota.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; IDA:UniProtKB.
DR GO; GO:0001963; P:synaptic transmission, dopaminergic; IDA:UniProtKB.
DR InterPro; IPR018446; Corticotropin-releasing_fac_CS.
DR InterPro; IPR000187; CRF.
DR InterPro; IPR003620; Urocortin_CRF.
DR PANTHER; PTHR15035; PTHR15035; 1.
DR Pfam; PF00473; CRF; 1.
DR PRINTS; PR01612; CRFFAMILY.
DR SMART; SM00039; CRF; 1.
DR PROSITE; PS00511; CRF; 1.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000305"
FT PROPEP 25..147
FT /evidence="ECO:0000269|PubMed:2647152,
FT ECO:0000269|PubMed:6267699, ECO:0000269|PubMed:6273874"
FT /id="PRO_0000006220"
FT PEPTIDE 148..188
FT /note="Corticoliberin"
FT /evidence="ECO:0000269|PubMed:6273874"
FT /id="PRO_0000006221"
FT REGION 33..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 188
FT /note="Alanine amide"
FT /evidence="ECO:0000269|PubMed:6273874"
FT CONFLICT 127
FT /note="K -> E (in Ref. 2; AAA31513)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 190 AA; 20672 MW; E9599B97E85186FE CRC64;
MRLPLLVSVG VLLVALLPSP PCRALLSRGP IPGARQASQH PQPLSFFQPL PQPQEPQALP
TLLRVGEEYF LRLGNLDETR AAPLSPAASP LASRSSSRLS PDKVAANFFR ALLQPRRPLD
SPAGPAKRGT ENALGSRQEA PAARKRRSQE PPISLDLTFH LLREVLEMTK ADQLAQQAHS
NRKLLDIAGK
