ID   CRF_CARAU               Reviewed;         162 AA.
AC   Q9PTS1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Corticoliberin;
DE   AltName: Full=Corticotropin-releasing factor;
DE            Short=CRF;
DE   AltName: Full=Corticotropin-releasing hormone;
DE   Flags: Precursor;
GN   Name=crh; Synonyms=crf;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT PHE-160.
RC   TISSUE=Brain;
RX   PubMed=10603283; DOI=10.1006/gcen.1999.7386;
RA   Bernier N.J., Lin X., Peter R.E.;
RT   "Differential expression of corticotropin-releasing factor (CRF) and
RT   urotensin I precursor genes, and evidence of CRF gene expression regulated
RT   by cortisol in goldfish brain.";
RL   Gen. Comp. Endocrinol. 116:461-477(1999).
CC   -!- FUNCTION: This hormone from hypothalamus regulates the release of
CC       corticotropin from pituitary gland.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the sauvagine/corticotropin-releasing
CC       factor/urotensin I family. {ECO:0000305}.
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DR   EMBL; AF098629; AAF04625.1; -; mRNA.
DR   AlphaFoldDB; Q9PTS1; -.
DR   PRIDE; Q9PTS1; -.
DR   Ensembl; ENSCART00000147578; ENSCARP00000131071; ENSCARG00000068404.
DR   Proteomes; UP000515129; Genome assembly.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
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; Hormone; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..119
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000006224"
FT   PEPTIDE         120..160
FT                   /note="Corticoliberin"
FT                   /id="PRO_0000006225"
FT   MOD_RES         160
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000305|PubMed:10603283"
SQ   SEQUENCE   162 AA;  18418 MW;  FA3A9C817AE94C14 CRC64;
     MKLNFLVTTV ALLVAFPPPY ECRAIEGSSN QPATDPDGER QSPPVLARLG EEYFIRLGNR
     NQNYLRSPAD SFPETSQYSK RALQLQLTQR LLEGKVGNIG RLDGNYALRA LDSVERERRS
     EEPPISLDLT FHLLREVLEM ARAEQMAQQA HSNRKMMEIF GK