MCH_MOUSE
ID MCH_MOUSE Reviewed; 165 AA.
AC P56942; Q9D220;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Pro-MCH;
DE Contains:
DE RecName: Full=Neuropeptide-glycine-glutamic acid;
DE Short=NGE;
DE Short=Neuropeptide G-E;
DE Contains:
DE RecName: Full=Neuropeptide-glutamic acid-isoleucine;
DE Short=NEI;
DE Short=Neuropeptide E-I;
DE Contains:
DE RecName: Full=Melanin-concentrating hormone;
DE Short=MCH;
DE Flags: Precursor;
GN Name=Pmch; Synonyms=Mch;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RA Breton C., Presse F., Hervieu G., Nahon J.-L.;
RT "Structure and regulation of the mouse melanin-concentrating hormone mRNA
RT and gene.";
RL Mol. Cell. Neurosci. 4:271-284(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=8724342; DOI=10.1095/biolreprod54.6.1161;
RA Hervieu G., Segretain D., Nahon J.-L.;
RT "Developmental and stage-dependent expression of melanin-concentrating
RT hormone in mammalian germ cells.";
RL Biol. Reprod. 54:1161-1172(1996).
RN [6]
RP FUNCTION.
RX PubMed=8637571; DOI=10.1038/380243a0;
RA Qu D., Ludwig D.S., Gammeltoft S., Piper M., Pelleymounter M.A.,
RA Cullen M.J., Mathes W.F., Przypek R., Kanarek R., Maratos-Flier E.;
RT "A role for melanin-concentrating hormone in the central regulation of
RT feeding behaviour.";
RL Nature 380:243-247(1996).
RN [7]
RP PROTEOLYTIC PROCESSING.
RX PubMed=10037747; DOI=10.1074/jbc.274.10.6536;
RA Viale A., Ortola C., Hervieu G., Furuta M., Barbero P., Steiner D.F.,
RA Seidah N.G., Nahon J.-L.;
RT "Cellular localization and role of prohormone convertases in the processing
RT of pro-melanin concentrating hormone in mammals.";
RL J. Biol. Chem. 274:6536-6545(1999).
CC -!- FUNCTION: MCH may act as a neurotransmitter or neuromodulator in a
CC broad array of neuronal functions directed toward the regulation of
CC goal-directed behavior, such as food intake, and general arousal.
CC {ECO:0000269|PubMed:8637571}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in hypothalamus. Also found
CC in heart, intestine, spleen and testis (spermatogonia, early
CC spermatocytes and Sertoli cells). In brain only mature MCH and NEI
CC peptides are present. In peripheral tissues a large product,
CC encompassing the NEI and MCH domains of the precursor, is found
CC predominantly. {ECO:0000269|PubMed:8724342}.
CC -!- DEVELOPMENTAL STAGE: Expression is enhanced between postnatal days 10
CC and 15.
CC -!- PTM: Pro-MCH is processed differentially in the brain and in peripheral
CC organs producing two neuropeptides; NEI and MCH. A third peptide, NGE,
CC may also be produced. Preferential processing in neurons by prohormone
CC convertase 2 (PC2) generates NEI. MCH is generated in neurons of the
CC lateral hypothalmic area by several prohormone convertases including
CC PC1/3, PC2 and PC5/6. {ECO:0000269|PubMed:10037747}.
CC -!- SIMILARITY: Belongs to the MCH family. {ECO:0000305}.
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DR EMBL; AK020723; BAB32189.1; -; mRNA.
DR EMBL; AK138363; BAE23633.1; -; mRNA.
DR EMBL; AC139754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466539; EDL21464.1; -; Genomic_DNA.
DR CCDS; CCDS24105.1; -.
DR RefSeq; NP_084247.1; NM_029971.2.
DR AlphaFoldDB; P56942; -.
DR BioGRID; 225486; 4.
DR IntAct; P56942; 3.
DR MINT; P56942; -.
DR STRING; 10090.ENSMUSP00000044352; -.
DR PaxDb; P56942; -.
DR PRIDE; P56942; -.
DR ProteomicsDB; 252746; -.
DR Antibodypedia; 18038; 156 antibodies from 25 providers.
DR DNASU; 110312; -.
DR Ensembl; ENSMUST00000048621; ENSMUSP00000044352; ENSMUSG00000035383.
DR GeneID; 110312; -.
DR KEGG; mmu:110312; -.
DR UCSC; uc007grc.1; mouse.
DR CTD; 5367; -.
DR MGI; MGI:97629; Pmch.
DR VEuPathDB; HostDB:ENSMUSG00000035383; -.
DR eggNOG; ENOG502RZ12; Eukaryota.
DR GeneTree; ENSGT00390000004984; -.
DR HOGENOM; CLU_1610172_0_0_1; -.
DR InParanoid; P56942; -.
DR OMA; NTFRMGK; -.
DR OrthoDB; 1451976at2759; -.
DR TreeFam; TF330944; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 110312; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Pmch; mouse.
DR PRO; PR:P56942; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P56942; protein.
DR Bgee; ENSMUSG00000035383; Expressed in dorsomedial nucleus of hypothalamus and 58 other tissues.
DR Genevisible; P56942; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0030354; F:melanin-concentrating hormone activity; NAS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; NAS:UniProtKB.
DR GO; GO:0031777; F:type 1 melanin-concentrating hormone receptor binding; ISO:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR GO; GO:0042756; P:drinking behavior; ISO:MGI.
DR GO; GO:0007631; P:feeding behavior; IMP:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; ISO:MGI.
DR GO; GO:0045776; P:negative regulation of blood pressure; ISO:MGI.
DR GO; GO:0032227; P:negative regulation of synaptic transmission, dopaminergic; ISO:MGI.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0046005; P:positive regulation of circadian sleep/wake cycle, REM sleep; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0002027; P:regulation of heart rate; ISO:MGI.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISO:MGI.
DR GO; GO:0009409; P:response to cold; ISO:MGI.
DR InterPro; IPR005456; Prepro-melanin_conc_hormone.
DR PANTHER; PTHR12091; PTHR12091; 1.
DR Pfam; PF05824; Pro-MCH; 1.
DR PRINTS; PR01641; PROMCHFAMILY.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Disulfide bond; Hormone;
KW Neuropeptide; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..165
FT /note="Pro-MCH"
FT /id="PRO_0000019112"
FT PEPTIDE 110..128
FT /note="Neuropeptide-glycine-glutamic acid"
FT /evidence="ECO:0000255"
FT /id="PRO_0000019113"
FT PEPTIDE 131..143
FT /note="Neuropeptide-glutamic acid-isoleucine"
FT /evidence="ECO:0000250"
FT /id="PRO_0000019114"
FT PEPTIDE 147..165
FT /note="Melanin-concentrating hormone"
FT /id="PRO_0000019115"
FT REGION 66..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 143
FT /note="Isoleucine amide"
FT /evidence="ECO:0000250"
FT DISULFID 153..162
FT /evidence="ECO:0000250"
FT CONFLICT 113
FT /note="A -> AV (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="A -> T (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 165 AA; 18516 MW; 1872B6B1D4BEEAC2 CRC64;
MAKMTLSSYM LMLAFSLFSQ GILLSASKSI RNLEDDIVFN TFRMGKAFQK EDTAERSVVA
PSLEQYKNDE SGFMNDDDNK NSKNTGSKQN LVTHGLPLSL AVKPYLALKG SVAFPAENGV
QNAESTQEKR EIGDEENSAK FPIGRRDFDM LRCMLGRVYR PCWQV
