COLI_LOXAF
ID COLI_LOXAF Reviewed; 134 AA.
AC P21252;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Pro-opiomelanocortin;
DE Short=POMC;
DE AltName: Full=Corticotropin-lipotropin;
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; Fragment;
GN Name=POMC;
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=2854538; DOI=10.1111/j.1399-3011.1988.tb01389.x;
RA Li C.H., Oosthuizen M.M.J., Chung D.;
RT "Isolation and primary structures of elephant adrenocorticotropin and beta-
RT lipotropin.";
RL Int. J. Pept. Protein Res. 32:573-578(1988).
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 {ECO:0000250|UniProtKB:P01193}.
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 -!- TISSUE SPECIFICITY: ACTH and MSH are produced by the pituitary gland.
CC -!- PTM: Specific enzymatic cleavages at paired basic residues yield the
CC different active peptides.
CC -!- SIMILARITY: Belongs to the POMC family. {ECO:0000305}.
CC -!- CAUTION: X's at positions 40-41 represent paired basic residues
CC (probably Lys-Arg) assumed, by homology with the bovine sequence, to be
CC present in the precursor molecule. {ECO:0000305}.
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 PIR; JK0022; JK0022.
DR BMRB; P21252; -.
DR InParanoid; P21252; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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; IPR013532; Opioid_neuropept.
DR InterPro; IPR001941; PMOC.
DR Pfam; PF00976; ACTH_domain; 2.
DR Pfam; PF08035; Op_neuropeptide; 1.
DR PRINTS; PR00383; MELANOCORTIN.
DR SMART; SM01363; ACTH_domain; 2.
DR SMART; SM01365; Op_neuropeptide; 1.
PE 1: Evidence at protein level;
KW Acetylation; Amidation; Cleavage on pair of basic residues;
KW Direct protein sequencing; Endorphin; Hormone; Phosphoprotein;
KW Reference proteome; Secreted.
FT PEPTIDE 1..39
FT /note="Corticotropin"
FT /id="PRO_0000024977"
FT PEPTIDE 1..13
FT /note="Melanocyte-stimulating hormone alpha"
FT /id="PRO_0000024978"
FT PEPTIDE 19..39
FT /note="Corticotropin-like intermediary peptide"
FT /id="PRO_0000024979"
FT PEPTIDE 42..134
FT /note="Lipotropin beta"
FT /id="PRO_0000024980"
FT PEPTIDE 42..101
FT /note="Lipotropin gamma"
FT /id="PRO_0000024981"
FT PEPTIDE 84..101
FT /note="Melanocyte-stimulating hormone beta"
FT /id="PRO_0000024982"
FT PEPTIDE 104..134
FT /note="Beta-endorphin"
FT /id="PRO_0000024983"
FT PEPTIDE 104..108
FT /note="Met-enkephalin"
FT /id="PRO_0000024984"
FT REGION 34..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P01191"
FT MOD_RES 13
FT /note="Valine amide"
FT /evidence="ECO:0000250|UniProtKB:P01190"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01189"
FT NON_TER 1
SQ SEQUENCE 134 AA; 14935 MW; F3561D74460562D5 CRC64;
SYSMEHFRWG KPVGKKRRPV KVYPNGAEGE SAEAFPLEFX XELARERPEP ARGPEGPDEG
AATQADLDNG LVAEVEATSA EKKDEGPYKM EHFRWGSPAK DKRYGGFMTS EKSQTPLVTL
FKNAIIKNAY KKGH
