MIDN_MOUSE
ID MIDN_MOUSE Reviewed; 465 AA.
AC Q3TPJ7; Q3U3X5; Q9JJJ6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Midnolin;
DE AltName: Full=Midbrain nucleolar protein;
GN Name=Midn;
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] (ISOFORM 2), SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=CNS;
RX PubMed=10974535; DOI=10.1016/s0378-1119(00)00259-6;
RA Tsukahara M., Suemori H., Noguchi S., Ji Z.-S., Tsunoo H.;
RT "Novel nucleolar protein, midnolin, is expressed in the mesencephalon
RT during mouse development.";
RL Gene 254:45-55(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spinal ganglion;
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 MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24187134; DOI=10.1074/jbc.m113.526632;
RA Hofmeister-Brix A., Kollmann K., Langer S., Schultz J., Lenzen S.,
RA Baltrusch S.;
RT "Identification of the ubiquitin-like domain of midnolin as a new
RT glucokinase interaction partner.";
RL J. Biol. Chem. 288:35824-35839(2013).
RN [5]
RP FUNCTION.
RX PubMed=27326929; DOI=10.1016/j.devcel.2016.05.013;
RA Du J., Zhang J., He T., Li Y., Su Y., Tie F., Liu M., Harte P.J., Zhu A.J.;
RT "Stuxnet facilitates the degradation of polycomb protein during
RT development.";
RL Dev. Cell 37:507-519(2016).
CC -!- FUNCTION: Facilitates ubiquitin-independent proteasomal degradation of
CC polycomb protein CBX4 (PubMed:27326929). Plays a role in inhibiting the
CC activity of glucokinase GCK and both glucose-induced and basal insulin
CC secretion (By similarity). {ECO:0000250|UniProtKB:D4AE48,
CC ECO:0000269|PubMed:27326929}.
CC -!- SUBUNIT: Interacts with GCK; the interaction occurs preferentially at
CC low glucose levels. {ECO:0000250|UniProtKB:D4AE48,
CC ECO:0000250|UniProtKB:Q504T8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10974535,
CC ECO:0000269|PubMed:24187134}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:24187134}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:10974535}. Note=Detected in the nucleus and
CC nucleolus with no expression in the cytoplasm (PubMed:10974535).
CC However, a later study finds expression in the nucleus and cytoplasm
CC with no expression in the nucleolus (PubMed:24187134).
CC {ECO:0000269|PubMed:10974535, ECO:0000269|PubMed:24187134}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3TPJ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TPJ7-2; Sequence=VSP_025552;
CC Name=3;
CC IsoId=Q3TPJ7-3; Sequence=VSP_025552, VSP_025553;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain and liver with
CC significantly lower levels in muscle. {ECO:0000269|PubMed:24187134}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed at the mesencephalon (midbrain)
CC of 12.5 dpc embryos. {ECO:0000269|PubMed:10974535}.
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DR EMBL; AB036882; BAB00638.1; -; mRNA.
DR EMBL; AK154535; BAE32660.1; -; mRNA.
DR EMBL; AK164324; BAE37739.1; -; mRNA.
DR EMBL; BC034719; AAH34719.1; -; mRNA.
DR CCDS; CCDS24011.1; -. [Q3TPJ7-2]
DR CCDS; CCDS83727.1; -. [Q3TPJ7-1]
DR RefSeq; NP_001292727.1; NM_001305798.1.
DR RefSeq; NP_001292728.1; NM_001305799.1. [Q3TPJ7-3]
DR RefSeq; NP_001334046.1; NM_001347117.1. [Q3TPJ7-1]
DR RefSeq; NP_067540.1; NM_021565.2. [Q3TPJ7-2]
DR RefSeq; XP_006513976.1; XM_006513913.3. [Q3TPJ7-2]
DR RefSeq; XP_017169524.1; XM_017314035.1. [Q3TPJ7-3]
DR AlphaFoldDB; Q3TPJ7; -.
DR SMR; Q3TPJ7; -.
DR STRING; 10090.ENSMUSP00000046967; -.
DR PhosphoSitePlus; Q3TPJ7; -.
DR EPD; Q3TPJ7; -.
DR MaxQB; Q3TPJ7; -.
DR PeptideAtlas; Q3TPJ7; -.
DR PRIDE; Q3TPJ7; -.
DR ProteomicsDB; 295906; -. [Q3TPJ7-1]
DR ProteomicsDB; 295907; -. [Q3TPJ7-2]
DR ProteomicsDB; 295908; -. [Q3TPJ7-3]
DR Antibodypedia; 22621; 128 antibodies from 18 providers.
DR Ensembl; ENSMUST00000042057; ENSMUSP00000046967; ENSMUSG00000035621. [Q3TPJ7-2]
DR Ensembl; ENSMUST00000099492; ENSMUSP00000097091; ENSMUSG00000035621. [Q3TPJ7-1]
DR GeneID; 59090; -.
DR KEGG; mmu:59090; -.
DR UCSC; uc007gca.2; mouse. [Q3TPJ7-2]
DR UCSC; uc007gcb.2; mouse. [Q3TPJ7-1]
DR UCSC; uc007gcc.2; mouse. [Q3TPJ7-3]
DR CTD; 90007; -.
DR MGI; MGI:1890222; Midn.
DR VEuPathDB; HostDB:ENSMUSG00000035621; -.
DR eggNOG; ENOG502QTDX; Eukaryota.
DR GeneTree; ENSGT00510000049027; -.
DR HOGENOM; CLU_029882_0_0_1; -.
DR InParanoid; Q3TPJ7; -.
DR OMA; EANCSTN; -.
DR OrthoDB; 1159802at2759; -.
DR PhylomeDB; Q3TPJ7; -.
DR TreeFam; TF329735; -.
DR BioGRID-ORCS; 59090; 6 hits in 59 CRISPR screens.
DR ChiTaRS; Midn; mouse.
DR PRO; PR:Q3TPJ7; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q3TPJ7; protein.
DR Bgee; ENSMUSG00000035621; Expressed in ileal epithelium and 255 other tissues.
DR ExpressionAtlas; Q3TPJ7; baseline and differential.
DR Genevisible; Q3TPJ7; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0033132; P:negative regulation of glucokinase activity; ISO:MGI.
DR GO; GO:0046676; P:negative regulation of insulin secretion; ISO:MGI.
DR InterPro; IPR039336; Midnolin.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23010; PTHR23010; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..465
FT /note="Midnolin"
FT /id="PRO_0000287537"
FT DOMAIN 32..106
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 185..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..424
FT /note="Required for nucleolar localization"
FT /evidence="ECO:0000269|PubMed:10974535"
FT REGION 400..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 128
FT /note="T -> TQPPATPGPGRAAGGGFRKYRLILFKRPWHRQGPQSPERGGERP
FT (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10974535,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_025552"
FT VAR_SEQ 236
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025553"
SQ SEQUENCE 465 AA; 49192 MW; F32E5C4D95DEAAD8 CRC64;
MEPQPGGARS CRRGAPGGAC ELNTATESAA PMSLAIHSTT GTRYDLSVPH DETVEGLRKR
LSQRLKVPKE RLALLHKDTR LSSGKLQEFG VGDGSKLTLV PTVEAGLMSQ ASRPEQSVMQ
ALESLTETQV SDFLSGRSPL TLALRVGDHM MFVQLQLAAQ HAPLQHRHVL AAAAAAAAAA
RGDSSVATPV SSPCRPVSSA ARVPPVSSSP SSPVSPSPVT AGSFRSHAAS TTCPEQMDCS
PPASSSSTST PGSSPTPRSR KPGAVIESFV NHAPGVFSGT FSGTLHPNCQ DSSGRPRRDI
GTILQILNDL LSATRHYQGM PPSLTQLRCH AQCSPASPAP DLTPKTTSCE KLAATSSTSL
LQGQSQIRMC KPPGDRLRQT ENRATRCKVE RLQLLLQQKR LRRKARRDAR GPYHWTPSRK
AGRSDSSSSG GGGGPSEATG LGLDFEDSVW KPEVNPDIQS EFVVA
