COLI_ACITR
ID COLI_ACITR Reviewed; 263 AA.
AC P87352;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Pro-opiomelanocortin;
DE Short=POMC;
DE AltName: Full=Corticotropin-lipotropin;
DE Contains:
DE RecName: Full=NPP;
DE Contains:
DE RecName: Full=Gamma-melanotropin-like segment;
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=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 Acipenser transmontanus (White sturgeon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Chondrostei; Acipenseriformes; Acipenseridae; Acipenser.
OX NCBI_TaxID=7904;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=9016801; DOI=10.1006/bbrc.1996.5987;
RA Amemiya Y., Takahashi A., Dores R.M., Kawauchi H.;
RT "Sturgeon proopiomelanocortin has a remnant of gamma-melanotropin.";
RL Biochem. Biophys. Res. Commun. 230:452-456(1997).
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; D88740; BAA13682.1; -; mRNA.
DR PIR; JC5283; JC5283.
DR AlphaFoldDB; P87352; -.
DR SMR; P87352; -.
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; IPR013531; Mcrtin_ACTH_cent.
DR InterPro; IPR013593; Melanocortin_N.
DR InterPro; IPR013532; Opioid_neuropept.
DR InterPro; IPR001941; PMOC.
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; 2.
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; Disulfide bond; Endorphin;
KW Hormone; Pyrrolidone carboxylic acid; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PEPTIDE 26..137
FT /note="NPP"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025049"
FT PEPTIDE 75..97
FT /note="Gamma-melanotropin-like segment"
FT /id="PRO_0000025050"
FT PEPTIDE 140..178
FT /note="Corticotropin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025051"
FT PEPTIDE 140..152
FT /note="Melanocyte-stimulating hormone alpha"
FT /id="PRO_0000025052"
FT PEPTIDE 158..208
FT /note="Corticotropin-like intermediary peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025053"
FT PEPTIDE 211..227
FT /note="Melanocyte-stimulating hormone beta"
FT /id="PRO_0000025054"
FT PEPTIDE 230..263
FT /note="Beta-endorphin"
FT /id="PRO_0000025055"
FT PEPTIDE 230..234
FT /note="Met-enkephalin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025056"
FT REGION 114..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 26
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT MOD_RES 152
FT /note="Valine amide"
FT /evidence="ECO:0000250"
FT DISULFID 27..49
FT /evidence="ECO:0000250"
FT DISULFID 33..45
FT /evidence="ECO:0000250"
SQ SEQUENCE 263 AA; 30163 MW; 1B1B5F3621DD640A CRC64;
MLHPVWGCVV AVMGVLWFYS SGVQSQCWEH SQCRDLASEA NILECIQACK VDLSAESPLF
PGNGHLQPTS EDIQNYVMSH FHWNTFGQRM NGTPGGSKRE GASTALSVLL EALSQPRDEV
ERESEEEEGL QQHRRDDKRS YSMEHFRWGK PVGRKRRPVK VYPNGVEEES AESYPAEIRR
DLSLKLDYPQ GEELEEVFGG ENDLLNLQKK DGSYKMNHFR WSGPPKDKRY GGFMKSWDER
SQKPLLTLFK NVMIKDGHEK KGQ
