LOCUS       NM_000939               1128 bp    mRNA    linear   PRI 11-FEB-2025
DEFINITION  Homo sapiens proopiomelanocortin (POMC), transcript variant 2,
            mRNA.
ACCESSION   NM_000939
VERSION     NM_000939.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (bases 1 to 1128)
  AUTHORS   Santana,C.V.N., Magno,L.A.V., Ramos,A.V., Rios,M.A., Sandrim,V.C.,
            De Marco,L.A., de Miranda,D.M. and Romano-Silva,M.A.
  TITLE     Genetic Variations in AMPK, FOXO3A, and POMC Increase the Risk of
            Extreme Obesity
  JOURNAL   J Obes 2024, 3813621 (2024)
   PUBMED   39484290
  REMARK    GeneRIF: Genetic Variations in AMPK, FOXO3A, and POMC Increase the
            Risk of Extreme Obesity.
            Publication Status: Online-Only
REFERENCE   2  (bases 1 to 1128)
  AUTHORS   Bando,H., Yamamoto,M., Urai,S., Motomura,Y., Sasaki,Y., Ohmachi,Y.,
            Kobatake,M., Tsujimoto,Y., Oi-Yo,Y., Suzuki,M., Yamamoto,N.,
            Takahashi,M., Fukuoka,H., Iguchi,G. and Ogawa,W.
  TITLE     Fluctuations in plasma adrenocorticotropic hormone concentration
            may predict the onset of immune checkpoint inhibitor-related
            hypophysitis
  JOURNAL   J Immunother Cancer 12 (2), e008634 (2024)
   PUBMED   38418395
  REMARK    GeneRIF: Fluctuations in serum adrenocorticotropic hormone
            concentration may predict the onset of immune checkpoint
            inhibitor-related hypophysitis.
            Erratum:[J Immunother Cancer. 2024 Mar 29;12(3):e008634corr1. doi:
            10.1136/jitc-2023-008634corr1.. PMID: 38553010]
            Publication Status: Online-Only
REFERENCE   3  (bases 1 to 1128)
  AUTHORS   Singh,M. and Mukhopadhyay,K.
  TITLE     Alpha-melanocyte stimulating hormone: an emerging anti-inflammatory
            antimicrobial peptide
  JOURNAL   Biomed Res Int 2014, 874610 (2014)
   PUBMED   25140322
  REMARK    Review article
REFERENCE   4  (bases 1 to 1128)
  AUTHORS   Pritchard,L.E. and White,A.
  TITLE     Neuropeptide processing and its impact on melanocortin pathways
  JOURNAL   Endocrinology 148 (9), 4201-4207 (2007)
   PUBMED   17584964
  REMARK    Review article
REFERENCE   5  (bases 1 to 1128)
  AUTHORS   Raffin-Sanson,M.L., de Keyzer,Y. and Bertagna,X.
  TITLE     Proopiomelanocortin, a polypeptide precursor with multiple
            functions: from physiology to pathological conditions
  JOURNAL   Eur J Endocrinol 149 (2), 79-90 (2003)
   PUBMED   12887283
  REMARK    GeneRIF: POMC has become a paradigmatic polypeptide precursor model
            illustrating the variable roles of a single gene and its various
            products in different localities--review
            Review article
REFERENCE   6  (bases 1 to 1128)
  AUTHORS   Challis,B.G. and Millington,G.W.M.
  TITLE     Proopiomelanocortin Deficiency - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24354022
REFERENCE   7  (bases 1 to 1128)
  AUTHORS   Osamura,R.Y.
  TITLE     Processing of proopiomelanocortin (POMC) approached by
            immunoelectron microscopy pre-embedding method
  JOURNAL   Pathol Res Pract 187 (5), 543-545 (1991)
   PUBMED   1656407
REFERENCE   8  (bases 1 to 1128)
  AUTHORS   Takahashi,H., Hakamata,Y., Watanabe,Y., Kikuno,R., Miyata,T. and
            Numa,S.
  TITLE     Complete nucleotide sequence of the human
            corticotropin-beta-lipotropin precursor gene
  JOURNAL   Nucleic Acids Res 11 (19), 6847-6858 (1983)
   PUBMED   6314261
REFERENCE   9  (bases 1 to 1128)
  AUTHORS   Dragon,N., Seidah,N.G., Lis,M., Routhier,R. and Chretien,M.
  TITLE     Primary structure and morphine-like activity of human
            beta-endorphin
  JOURNAL   Can J Biochem 55 (6), 666-670 (1977)
   PUBMED   195688
REFERENCE   10 (bases 1 to 1128)
  AUTHORS   Li,C.H. and Chung,D.
  TITLE     Primary structure of human beta-lipotropin
  JOURNAL   Nature 260 (5552), 622-624 (1976)
   PUBMED   1264228
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY050419.1, CD108235.1,
            BC065832.1 and T29537.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 23, 2018 this sequence version replaced NM_000939.3.
            
            Summary: This gene encodes a preproprotein that undergoes
            extensive, tissue-specific, post-translational processing via
            cleavage by subtilisin-like enzymes known as prohormone
            convertases. There are eight potential cleavage sites within the
            preproprotein and, depending on tissue type and the available
            convertases, processing may yield as many as ten biologically
            active peptides involved in diverse cellular functions. The encoded
            protein is synthesized mainly in corticotroph cells of the anterior
            pituitary where four cleavage sites are used; adrenocorticotrophin,
            essential for normal steroidogenesis and the maintenance of normal
            adrenal weight, and lipotropin beta are the major end products. In
            other tissues, including the hypothalamus, placenta, and
            epithelium, all cleavage sites may be used, giving rise to peptides
            with roles in pain and energy homeostasis, melanocyte stimulation,
            and immune modulation. These include several distinct
            melanotropins, lipotropins, and endorphins that are contained
            within the adrenocorticotrophin and beta-lipotropin peptides. The
            antimicrobial melanotropin alpha peptide exhibits antibacterial and
            antifungal activity. Mutations in this gene have been associated
            with early onset obesity, adrenal insufficiency, and red hair
            pigmentation. Alternatively spliced transcript variants encoding
            the same protein have been described. [provided by RefSeq, Jan
            2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 3. Variants 1-4 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.394204.1, CD513772.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145544
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match                 :: ENST00000395826.7/
                                                  ENSP00000379170.2
            Protein has antimicrobial activity :: PMID: 25140322
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
            COMPLETENESS: full length.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-6                 HY050419.1         271-276
            7-750               CD108235.1         1-744
            751-1067            BC065832.1         734-1050
            1068-1128           T29537.1           122-182
FEATURES             Location/Qualifiers
     source          1..1128
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     gene            1..1128
                     /gene="POMC"
                     /gene_synonym="ACTH; CLIP; LPH; MSH; NPP; OBAIRH; POC"
                     /note="proopiomelanocortin"
                     /db_xref="GeneID:5443"
                     /db_xref="HGNC:HGNC:9201"
                     /db_xref="MIM:176830"
     exon            1..83
                     /gene="POMC"
                     /gene_synonym="ACTH; CLIP; LPH; MSH; NPP; OBAIRH; POC"
                     /inference="alignment:Splign:2.1.0"
     exon            84..235
                     /gene="POMC"
                     /gene_synonym="ACTH; CLIP; LPH; MSH; NPP; OBAIRH; POC"
                     /inference="alignment:Splign:2.1.0"
     CDS             104..907
                     /gene="POMC"
                     /gene_synonym="ACTH; CLIP; LPH; MSH; NPP; OBAIRH; POC"
                     /note="met-enkephalin; melanotropin gamma; gamma-MSH;
                     adrenocorticotropic hormone; melanotropin alpha;
                     alpha-MSH; corticotropin-like intermediary peptide;
                     lipotropin beta; beta-LPH; lipotropin gamma; gamma-LPH;
                     melanotropin beta; beta-MSH; beta-endorphin;
                     alpha-melanocyte-stimulating hormone; pro-ACTH-endorphin;
                     beta-melanocyte-stimulating hormone; adrenocorticotropin;
                     proopiomelanocortin preproprotein;
                     corticotropin-lipotropin; opiomelanocortin prepropeptide"
                     /codon_start=1
                     /product="pro-opiomelanocortin preproprotein"
                     /protein_id="NP_000930.1"
                     /db_xref="CCDS:CCDS1717.1"
                     /db_xref="GeneID:5443"
                     /db_xref="HGNC:HGNC:9201"
                     /db_xref="MIM:176830"
                     /translation="MPRSCCSRSGALLLALLLQASMEVRGWCLESSQCQDLTTESNLL
                     ECIRACKPDLSAETPMFPGNGDEQPLTENPRKYVMGHFRWDRFGRRNSSSSGSSGAGQ
                     KREDVSAGEDCGPLPEGGPEPRSDGAKPGPREGKRSYSMEHFRWGKPVGKKRRPVKVY
                     PNGAEDESAEAFPLEFKRELTGQRLREGDGPDGPADDGAGAQADLEHSLLVAAEKKDE
                     GPYRMEHFRWGSPPKDKRYGGFMTSEKSQTPLVTLFKNAIIKNAYKKGE"
     exon            236..1128
                     /gene="POMC"
                     /gene_synonym="ACTH; CLIP; LPH; MSH; NPP; OBAIRH; POC"
                     /inference="alignment:Splign:2.1.0"
     regulatory      1047..1052
                     /regulatory_class="polyA_signal_sequence"
                     /gene="POMC"
                     /gene_synonym="ACTH; CLIP; LPH; MSH; NPP; OBAIRH; POC"
                     /note="hexamer: AATAAA"
     polyA_site      1067
                     /gene="POMC"
                     /gene_synonym="ACTH; CLIP; LPH; MSH; NPP; OBAIRH; POC"
                     /note="major polyA site"
     regulatory      1106..1111
                     /regulatory_class="polyA_signal_sequence"
                     /gene="POMC"
                     /gene_synonym="ACTH; CLIP; LPH; MSH; NPP; OBAIRH; POC"
                     /note="hexamer: AGTAAA"
     polyA_site      1128
                     /gene="POMC"
                     /gene_synonym="ACTH; CLIP; LPH; MSH; NPP; OBAIRH; POC"
ORIGIN      
        1 ggcggcgaag gaggggaaga agagccgcga ccgagagagg ccgccgagcg tccccgccct
       61 cagagagcag cctcccgaga cagagcctca gcctgcctgg aagatgccga gatcgtgctg
      121 cagccgctcg ggggccctgt tgctggcctt gctgcttcag gcctccatgg aagtgcgtgg
      181 ctggtgcctg gagagcagcc agtgtcagga cctcaccacg gaaagcaacc tgctggagtg
      241 catccgggcc tgcaagcccg acctctcggc cgagactccc atgttcccgg gaaatggcga
      301 cgagcagcct ctgaccgaga acccccggaa gtacgtcatg ggccacttcc gctgggaccg
      361 attcggccgc cgcaacagca gcagcagcgg cagcagcggc gcagggcaga agcgcgagga
      421 cgtctcagcg ggcgaagact gcggcccgct gcctgagggc ggccccgagc cccgcagcga
      481 tggtgccaag ccgggcccgc gcgagggcaa gcgctcctac tccatggagc acttccgctg
      541 gggcaagccg gtgggcaaga agcggcgccc agtgaaggtg taccctaacg gcgccgagga
      601 cgagtcggcc gaggccttcc ccctggagtt caagagggag ctgactggcc agcgactccg
      661 ggagggagat ggccccgacg gccctgccga tgacggcgca ggggcccagg ccgacctgga
      721 gcacagcctg ctggtggcgg ccgagaagaa ggacgagggc ccctacagga tggagcactt
      781 ccgctggggc agcccgccca aggacaagcg ctacggcggt ttcatgacct ccgagaagag
      841 ccagacgccc ctggtgacgc tgttcaaaaa cgccatcatc aagaacgcct acaagaaggg
      901 cgagtgaggg cacagcgggg ccccagggct accctccccc aggaggtcga ccccaaagcc
      961 ccttgctctc ccctgccctg ctgccgcctc ccagcctggg gggtcgtggc agataatcag
     1021 cctcttaaag ctgcctgtag ttaggaaata aaacctttca aatttcacat ccacctctga
     1081 ctttgaatgt aaactgtgtg aataaagtaa aaatacgtag ccgtcaaa
//
