COLI_BOVIN
ID COLI_BOVIN Reviewed; 265 AA.
AC P01190; Q05B64; Q28166; Q28167; Q28168;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 160.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=221818; DOI=10.1038/278423a0;
RA Nakanishi S., Inoue A., Kita T., Nakamura M., Chang A.C.Y., Cohen S.N.,
RA Numa S.;
RT "Nucleotide sequence of cloned cDNA for bovine corticotropin-beta-
RT lipotropin precursor.";
RL Nature 278:423-427(1979).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6249166; DOI=10.1111/j.1749-6632.1980.tb47270.x;
RA Cohen S.N., Chang A.C.Y., Nakanishi S., Inoue A., Kita T., Nakamura M.,
RA Numa S.;
RT "Studies of cloned DNA encoding the structure for the bovine corticotropin-
RT beta-lipotropin precursor protein.";
RL Ann. N. Y. Acad. Sci. 343:415-425(1980).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6263630; DOI=10.1111/j.1432-1033.1981.tb06220.x;
RA Nakanishi S., Teranishi Y., Watanabe Y., Notake M., Noda M., Kakidani H.,
RA Jingami H., Numa S.;
RT "Isolation and characterization of the bovine corticotropin/beta-lipotropin
RT precursor gene.";
RL Eur. J. Biochem. 115:429-438(1981).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 75-265.
RA Rubtsov P.M., Chernov B.K., Gorbulev V.G., Parsadanyan A.S.,
RA Sverdlova P.S., Chupeeva V.V., Golova Y.B., Batchikova N.V.,
RA Zhvirblis G.S., Skryabin K.G., Baev A.A.;
RT "Genetic engineering of peptide hormones.";
RL Mol. Biol. (Mosk.) 19:226-235(1985).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 132-200.
RX PubMed=216007; DOI=10.1073/pnas.75.12.6021;
RA Nakanishi G., Inoue A., Kita T., Numa S., Chang A.C.Y., Cohen S.N.,
RA Nunberg J., Schimke R.T.;
RT "Construction of bacterial plasmids that contain the nucleotide sequence
RT for bovine corticotropin-beta-lipotropin precursor.";
RL Proc. Natl. Acad. Sci. U.S.A. 75:6021-6025(1978).
RN [7]
RP PROTEIN SEQUENCE OF 77-87, AND AMIDATION AT PHE-87.
RX PubMed=7274457; DOI=10.1016/0014-5793(81)81081-2;
RA Boehlen P., Esch F., Shibasaki T., Baird A., Ling N., Guillemin R.;
RT "Isolation and characterization of a gamma 1-melanotropin-like peptide from
RT bovine neurointermediate pituitary.";
RL FEBS Lett. 128:67-70(1981).
RN [8]
RP PROTEIN SEQUENCE OF 131-144, AND AMIDATION AT VAL-144.
RX PubMed=13642798;
RA Li C.H.;
RT "The relation of chemical structure to the biologic activity of pituitary
RT hormones.";
RL Lab. Invest. 8:574-587(1959).
RN [9]
RP PROTEIN SEQUENCE OF 132-170.
RA Li C.H., Dixon J.S., Chung D.;
RT "Isolation of melatonin, the pineal gland factor that lightens
RT melanocytes.";
RL J. Am. Chem. Soc. 80:2587-2588(1958).
RN [10]
RP SEQUENCE REVISION (CORTICOTROPIN).
RX PubMed=4344689; DOI=10.1016/0006-291x(72)90486-x;
RA Li C.H.;
RT "Adrenocorticotropin 45. Revised amino acid sequences for sheep and bovine
RT hormones.";
RL Biochem. Biophys. Res. Commun. 49:835-839(1972).
RN [11]
RP PROTEIN SEQUENCE OF 173-265.
RA Pankov Y.A.;
RT "Primary structure of the bovine beta-lipotropic hormone.";
RL Vopr. Med. Khim. 19:330-332(1973).
RN [12]
RP PROTEIN SEQUENCE OF 215-232.
RA Geschwind I.I., Li C.H., Barnafi L.;
RT "The isolation and structure of a melanocyte-stimulating hormone from
RT bovine pituitary glands.";
RL J. Am. Chem. Soc. 79:1003-1004(1957).
RN [13]
RP PROTEIN SEQUENCE OF 215-232.
RX PubMed=13348631; DOI=10.1038/178090a0;
RA Harris J.I., Roos P.;
RT "Amino-acid sequence of a melanophore-stimulating peptide.";
RL Nature 178:90-90(1956).
RN [14]
RP PROTEIN SEQUENCE OF 235-239.
RX PubMed=1065904; DOI=10.1073/pnas.73.7.2515;
RA Simantov R., Snyder S.H.;
RT "Morphine-like peptides in mammalian brain: isolation, structure
RT elucidation, and interactions with the opiate receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 73:2515-2519(1976).
RN [15]
RP GLYCOSYLATION AT THR-71 AND ASN-91, AND DISULFIDE BONDS.
RX PubMed=4030947; DOI=10.1016/s0021-9673(01)87458-6;
RA James S., Bennett H.P.J.;
RT "Use of reversed-phase and ion-exchange batch extraction in the
RT purification of bovine pituitary peptides.";
RL J. Chromatogr. A 326:329-338(1985).
RN [16]
RP SULFATION AT TYR-200, AND PYROGLUTAMATE FORMATION AT GLU-173.
RX PubMed=2266117; DOI=10.1016/s0021-9258(18)45680-3;
RA Bateman A., Solomon S., Bennett H.P.J.;
RT "Post-translational modification of bovine pro-opiomelanocortin. Tyrosine
RT sulfation and pyroglutamate formation, a mass spectrometric study.";
RL J. Biol. Chem. 265:22130-22136(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: [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 -!- SEQUENCE CAUTION:
CC Sequence=AAA30414.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; V00107; CAA23441.1; -; mRNA.
DR EMBL; V00107; CAA23440.1; -; mRNA.
DR EMBL; M25587; AAA30354.1; -; mRNA.
DR EMBL; J00021; AAB59262.1; -; Genomic_DNA.
DR EMBL; J00019; AAB59262.1; JOINED; Genomic_DNA.
DR EMBL; BC122728; AAI22729.1; -; mRNA.
DR EMBL; M23814; AAA30414.1; ALT_INIT; mRNA.
DR EMBL; M10723; AAA30718.1; -; mRNA.
DR PIR; A93206; CTBOP.
DR RefSeq; NP_776576.1; NM_174151.1.
DR RefSeq; XP_005212977.1; XM_005212920.2.
DR AlphaFoldDB; P01190; -.
DR BMRB; P01190; -.
DR SMR; P01190; -.
DR STRING; 9913.ENSBTAP00000010386; -.
DR GlyConnect; 113; 12 N-Linked glycans (1 site), 4 O-Linked glycans (1 site).
DR PaxDb; P01190; -.
DR PRIDE; P01190; -.
DR Ensembl; ENSBTAT00000010386; ENSBTAP00000010386; ENSBTAG00000007897.
DR GeneID; 281416; -.
DR KEGG; bta:281416; -.
DR CTD; 5443; -.
DR VEuPathDB; HostDB:ENSBTAG00000007897; -.
DR VGNC; VGNC:33155; POMC.
DR eggNOG; ENOG502RZNY; Eukaryota.
DR GeneTree; ENSGT00390000016811; -.
DR HOGENOM; CLU_094632_0_0_1; -.
DR InParanoid; P01190; -.
DR OMA; KMHHFRW; -.
DR OrthoDB; 1168862at2759; -.
DR TreeFam; TF333215; -.
DR Reactome; R-BTA-193048; Androgen biosynthesis.
DR Reactome; R-BTA-194002; Glucocorticoid biosynthesis.
DR Reactome; R-BTA-211976; Endogenous sterols.
DR Reactome; R-BTA-375276; Peptide ligand-binding receptors.
DR Reactome; R-BTA-418594; G alpha (i) signalling events.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000007897; Expressed in neurohypophysis and 100 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0070996; F:type 1 melanocortin receptor binding; IEA:Ensembl.
DR GO; GO:0031781; F:type 3 melanocortin receptor binding; IEA:Ensembl.
DR GO; GO:0031782; F:type 4 melanocortin receptor binding; IEA:Ensembl.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:Ensembl.
DR GO; GO:0007267; P:cell-cell signaling; IEA:Ensembl.
DR GO; GO:0033059; P:cellular pigmentation; IEA:Ensembl.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IEA:Ensembl.
DR GO; GO:0140668; P:positive regulation of oxytocin production; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0032098; P:regulation of appetite; IEA:Ensembl.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR GO; GO:2000852; P:regulation of corticosterone secretion; IBA:GO_Central.
DR GO; GO:0070873; P:regulation of glycogen metabolic process; IEA:Ensembl.
DR GO; GO:1990680; P:response to melanocyte-stimulating hormone; IEA:Ensembl.
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; 3.
DR SMART; SM01364; NPP; 1.
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; Disulfide bond; Endorphin; Glycoprotein;
KW Hormone; Phosphoprotein; Pyrrolidone carboxylic acid; Reference proteome;
KW Secreted; Signal; Sulfation.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT PEPTIDE 27..103
FT /note="NPP"
FT /id="PRO_0000024943"
FT PEPTIDE 77..87
FT /note="Melanotropin gamma"
FT /id="PRO_0000024944"
FT PROPEP 106..129
FT /id="PRO_0000024945"
FT PEPTIDE 132..170
FT /note="Corticotropin"
FT /id="PRO_0000024946"
FT PEPTIDE 132..144
FT /note="Melanocyte-stimulating hormone alpha"
FT /id="PRO_0000024947"
FT PEPTIDE 150..170
FT /note="Corticotropin-like intermediary peptide"
FT /id="PRO_0000024948"
FT PEPTIDE 173..265
FT /note="Lipotropin beta"
FT /id="PRO_0000024949"
FT PEPTIDE 173..232
FT /note="Lipotropin gamma"
FT /id="PRO_0000024950"
FT PEPTIDE 215..232
FT /note="Melanocyte-stimulating hormone beta"
FT /id="PRO_0000024951"
FT PEPTIDE 235..265
FT /note="Beta-endorphin"
FT /id="PRO_0000024952"
FT PEPTIDE 235..239
FT /note="Met-enkephalin"
FT /id="PRO_0000024953"
FT REGION 89..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 87
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:7274457"
FT MOD_RES 132
FT /note="N-acetylserine; in Corticotropin"
FT /evidence="ECO:0000250|UniProtKB:P01191"
FT MOD_RES 144
FT /note="Valine amide"
FT /evidence="ECO:0000269|PubMed:13642798"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01189"
FT MOD_RES 173
FT /note="Pyrrolidone carboxylic acid (Glu); partial"
FT /evidence="ECO:0000269|PubMed:2266117"
FT MOD_RES 200
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:2266117"
FT CARBOHYD 71
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:4030947"
FT /id="CAR_000202"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:4030947"
FT /id="CAR_000034"
FT DISULFID 28..50
FT /evidence="ECO:0000269|PubMed:4030947"
FT DISULFID 34..46
FT /evidence="ECO:0000269|PubMed:4030947"
FT CONFLICT 10
FT /note="G -> A (in Ref. 2; AAA30354)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="R -> P (in Ref. 2; AAA30354)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="Missing (in Ref. 6; AAA30718)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="Q -> G (in Ref. 11; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 190..191
FT /note="ES -> D (in Ref. 6; AAA30718)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="A -> P (in Ref. 2; AAA30354)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 265 AA; 29260 MW; 303E9A0BCB073B3F CRC64;
MPRLCSSRSG ALLLALLLQA SMEVRGWCLE SSQCQDLTTE SNLLACIRAC KPDLSAETPV
FPGNGDEQPL TENPRKYVMG HFRWDRFGRR NGSSSSGVGG AAQKREEEVA VGEGPGPRGD
DAETGPREDK RSYSMEHFRW GKPVGKKRRP VKVYPNGAED ESAQAFPLEF KRELTGERLE
QARGPEAQAE SAAARAELEY GLVAEAEAEA AEKKDSGPYK MEHFRWGSPP KDKRYGGFMT
SEKSQTPLVT LFKNAIIKNA HKKGQ
