ID Q32U08_AGADC Unreviewed; 174 AA. AC Q32U08; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 29-MAY-2024, entry version 37. DE SubName: Full=Proopiomelanocortin A {ECO:0000313|EMBL:AAX63097.1}; DE Flags: Fragment; GN Name=POMC {ECO:0000313|EMBL:AAX63097.1}; OS Agalychnis dacnicolor (Giant Mexican leaf frog) (Pachymedusa dacnicolor). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae; OC Agalychnis. OX NCBI_TaxID=75988 {ECO:0000313|EMBL:AAX63097.1}; RN [1] {ECO:0000313|EMBL:AAX63097.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16243760; DOI=10.1080/10635150500234625; RA Wiens J.J., Fetzner J.W., Parkinson C.L., Reeder T.W.; RT "Hylid frog phylogeny and sampling strategies for speciose clades."; RL Syst. Biol. 54:778-807(2005). CC -!- FUNCTION: Stimulates the adrenal glands to release cortisol. CC {ECO:0000256|ARBA:ARBA00002965}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}. CC -!- SIMILARITY: Belongs to the POMC family. CC {ECO:0000256|ARBA:ARBA00005832}. 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; AY819152; AAX63097.1; -; Genomic_DNA. DR AlphaFoldDB; Q32U08; -. DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter. DR GO; GO:0030141; C:secretory granule; IEA:TreeGrafter. DR GO; GO:0001664; F:G protein-coupled receptor binding; IEA:TreeGrafter. DR GO; GO:0005184; F:neuropeptide hormone activity; IEA:TreeGrafter. DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:TreeGrafter. DR GO; GO:2000852; P:regulation of corticosterone secretion; IEA:TreeGrafter. DR InterPro; IPR013531; Mcrtin_ACTH_cent. DR InterPro; IPR013593; Melanocortin_N. DR InterPro; IPR001941; PMOC. DR PANTHER; PTHR11416; PRO-OPIOMELANOCORTIN; 1. DR PANTHER; PTHR11416:SF7; PRO-OPIOMELANOCORTIN; 1. DR Pfam; PF00976; ACTH_domain; 3. DR Pfam; PF08384; NPP; 1. DR PRINTS; PR00383; MELANOCORTIN. DR SMART; SM01363; ACTH_domain; 2. PE 3: Inferred from homology; KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Signal {ECO:0000256|ARBA:ARBA00022729}. FT DOMAIN 22..60 FT /note="Pro-opiomelanocortin/corticotropin ACTH central FT region" FT /evidence="ECO:0000259|SMART:SM01363" FT DOMAIN 88..126 FT /note="Pro-opiomelanocortin/corticotropin ACTH central FT region" FT /evidence="ECO:0000259|SMART:SM01363" FT REGION 33..93 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 130..174 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 70..93 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 150..174 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAX63097.1" FT NON_TER 174 FT /evidence="ECO:0000313|EMBL:AAX63097.1" SQ SEQUENCE 174 AA; 20517 MW; 763AC88219FE2D29 CRC64; SAESPVFPGN GHMQPLSENI RKYVMSHFRW NKFGRRNSTN SDSNKAGDKR EDIANYPVFN LFPANDKENA QDGNLEEDAM DRQDNKRSYS MEHFRWGKPV GKKRRPIKVF PSDVEEESSE IYPTEYRREL SVEFDYPETS SEEDLDDSET MESPSKKDRK YKMHHFRWEG PPKD //