COLI_PELRI
ID COLI_PELRI Reviewed; 260 AA.
AC P22923;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Pro-opiomelanocortin;
DE Short=POMC;
DE AltName: Full=Corticotropin-lipotropin;
DE Contains:
DE RecName: Full=NPP;
DE Contains:
DE RecName: Full=Melanotropin gamma;
DE AltName: Full=Gamma-MSH;
DE Contains:
DE RecName: Full=Corticotropin;
DE AltName: Full=Adrenocorticotropic hormone;
DE Short=ACTH;
DE Contains:
DE RecName: Full=Melanocyte-stimulating hormone alpha;
DE Short=Alpha-MSH;
DE AltName: Full=Melanotropin alpha;
DE Contains:
DE RecName: Full=Corticotropin-like intermediary peptide;
DE Short=CLIP;
DE Contains:
DE RecName: Full=Lipotropin beta;
DE AltName: Full=Beta-LPH;
DE Contains:
DE RecName: Full=Lipotropin gamma;
DE AltName: Full=Gamma-LPH;
DE Contains:
DE RecName: Full=Melanocyte-stimulating hormone beta;
DE Short=Beta-MSH;
DE AltName: Full=Melanotropin beta;
DE Contains:
DE RecName: Full=Beta-endorphin;
DE Contains:
DE RecName: Full=Met-enkephalin;
DE Flags: Precursor;
GN Name=pomc;
OS Pelophylax ridibundus (Marsh frog) (Rana ridibunda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX NCBI_TaxID=8406;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2260977; DOI=10.1016/s0006-291x(05)80085-3;
RA Hilario E., Lihrmann I., Vaudry H.;
RT "Characterization of the cDNA encoding proopiomelanocortin in the frog Rana
RT ridibunda.";
RL Biochem. Biophys. Res. Commun. 173:653-659(1990).
CC -!- FUNCTION: [Corticotropin]: Stimulates the adrenal glands to release
CC cortisol.
CC -!- FUNCTION: [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide.
CC Increases the pigmentation of skin by increasing melanin production in
CC melanocytes.
CC -!- FUNCTION: [Melanocyte-stimulating hormone beta]: Increases the
CC pigmentation of skin by increasing melanin production in melanocytes.
CC -!- FUNCTION: [Beta-endorphin]: Endogenous orexigenic opiate.
CC -!- FUNCTION: [Met-enkephalin]: Endogenous opiate.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01193}.
CC Note=Melanocyte-stimulating hormone alpha and beta-endorphin are stored
CC in separate granules in hypothalamic POMC neurons, suggesting that
CC secretion may be under the control of different regulatory mechanisms.
CC {ECO:0000250|UniProtKB:P01193}.
CC -!- PTM: Specific enzymatic cleavages at paired basic residues yield the
CC different active peptides.
CC -!- SIMILARITY: Belongs to the POMC family. {ECO:0000305}.
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DR EMBL; M62770; AAA49531.1; -; mRNA.
DR PIR; A36402; A36402.
DR AlphaFoldDB; P22923; -.
DR SMR; P22923; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR032246; ACTH_assoc.
DR InterPro; IPR013531; Mcrtin_ACTH_cent.
DR InterPro; IPR013593; Melanocortin_N.
DR InterPro; IPR013532; Opioid_neuropept.
DR InterPro; IPR001941; PMOC.
DR Pfam; PF16102; ACTH_assoc; 1.
DR Pfam; PF00976; ACTH_domain; 3.
DR Pfam; PF08384; NPP; 1.
DR Pfam; PF08035; Op_neuropeptide; 1.
DR PRINTS; PR00383; MELANOCORTIN.
DR SMART; SM01363; ACTH_domain; 3.
DR SMART; SM01364; NPP; 1.
DR SMART; SM01365; Op_neuropeptide; 1.
PE 2: Evidence at transcript level;
KW Amidation; Cleavage on pair of basic residues; Endorphin; Glycoprotein;
KW Hormone; Pyrrolidone carboxylic acid; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT PEPTIDE 26..101
FT /note="NPP"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025133"
FT PEPTIDE 76..86
FT /note="Melanotropin gamma"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025134"
FT PROPEP 104..138
FT /id="PRO_0000025135"
FT PEPTIDE 141..179
FT /note="Corticotropin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025136"
FT PEPTIDE 141..153
FT /note="Melanocyte-stimulating hormone alpha"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025137"
FT PEPTIDE 159..179
FT /note="Corticotropin-like intermediary peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025138"
FT PEPTIDE 182..260
FT /note="Lipotropin beta"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025139"
FT PEPTIDE 182..227
FT /note="Lipotropin gamma"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025140"
FT PEPTIDE 211..227
FT /note="Melanocyte-stimulating hormone beta"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025141"
FT PEPTIDE 230..260
FT /note="Beta-endorphin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025142"
FT PEPTIDE 230..234
FT /note="Met-enkephalin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025143"
FT MOD_RES 26
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT MOD_RES 86
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250"
FT MOD_RES 153
FT /note="Valine amide"
FT /evidence="ECO:0000250"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 260 AA; 30068 MW; 7B0CA8B5D5666833 CRC64;
MLQPVWSCIL ALLGVFIFHV GEVRSQCWES NKCTDLSSED GILECIKACK MDLSAESPVF
PGNGHMQPLS ENIRKYVMSH FRWNKFGRRN STSNDNNNGG YKREDIANYP ILNLLTGSDN
QNTQQGIMED EAVDRQDSKR SYSMEHFRWG KPVGKKRRPI KVFPTDAEEE SSEIFPLELR
RELSLEFDYP DTNSEEDLDD GELLDGPVKK DRKYKMHHFR WEGPPKDKRY GGFMTPERSQ
TPLMTLFKNA IIKNAHKKGQ