MIDN_RAT
ID MIDN_RAT Reviewed; 505 AA.
AC D4AE48;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Midnolin {ECO:0000303|PubMed:24187134};
DE AltName: Full=Midbrain nucleolar protein {ECO:0000250|UniProtKB:Q3TPJ7};
GN Name=Midn {ECO:0000303|PubMed:24187134, ECO:0000312|RGD:1309629};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|Proteomes:UP000002494};
RN [1] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH GCK, SUBCELLULAR LOCATION, AND INDUCTION.
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).
CC -!- FUNCTION: Facilitates ubiquitin-independent proteasomal degradation of
CC polycomb protein CBX4 (By similarity). Plays a role in inhibiting the
CC activity of glucokinase GCK and both glucose-induced and basal insulin
CC secretion (PubMed:24187134). {ECO:0000250|UniProtKB:Q3TPJ7,
CC ECO:0000269|PubMed:24187134}.
CC -!- SUBUNIT: Interacts with glucokinase GCK; the interaction occurs
CC preferentially at low glucose levels. {ECO:0000269|PubMed:24187134}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24187134}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:24187134}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q3TPJ7}. Note=Detected in the nucleus and
CC nucleolus with no expression in the cytoplasm (By similarity). However,
CC a later study finds expression in the nucleus and cytoplasm with no
CC expression in the nucleolus (PubMed:24187134).
CC {ECO:0000250|UniProtKB:Q3TPJ7, ECO:0000269|PubMed:24187134}.
CC -!- INDUCTION: Down-regulated at high glucose levels of 10 and 25
CC mmol/liter glucose with highest expression at low glucose levels of 3
CC mmol/liter. {ECO:0000269|PubMed:24187134}.
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DR EMBL; AC141331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001178506.1; NM_001191577.1.
DR RefSeq; XP_006240973.1; XM_006240911.3.
DR RefSeq; XP_006240974.1; XM_006240912.3.
DR AlphaFoldDB; D4AE48; -.
DR SMR; D4AE48; -.
DR STRING; 10116.ENSRNOP00000057429; -.
DR iPTMnet; D4AE48; -.
DR PhosphoSitePlus; D4AE48; -.
DR PaxDb; D4AE48; -.
DR Ensembl; ENSRNOT00000060698; ENSRNOP00000057429; ENSRNOG00000015434.
DR GeneID; 314623; -.
DR KEGG; rno:314623; -.
DR UCSC; RGD:1309629; rat.
DR CTD; 90007; -.
DR RGD; 1309629; Midn.
DR eggNOG; ENOG502QTDX; Eukaryota.
DR GeneTree; ENSGT00510000049027; -.
DR HOGENOM; CLU_029882_0_0_1; -.
DR InParanoid; D4AE48; -.
DR OMA; EANCSTN; -.
DR OrthoDB; 1159802at2759; -.
DR PhylomeDB; D4AE48; -.
DR TreeFam; TF329735; -.
DR PRO; PR:D4AE48; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000015434; Expressed in thymus and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0019900; F:kinase binding; IPI:MGI.
DR GO; GO:0033132; P:negative regulation of glucokinase activity; IDA:MGI.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IDA:MGI.
DR InterPro; IPR039336; Midnolin.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23010; PTHR23010; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..505
FT /note="Midnolin"
FT /id="PRO_0000438876"
FT DOMAIN 32..106
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 155..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 505 AA; 53679 MW; 78D087F1CD24DB22 CRC64;
MEPQPGGARS CRRGAPGGAC ELSTTAESAA PMSLAIHSTT GTRYDLSVPH DETVEGLRKR
LSQRLKVPKE RLALLHKDTR LSSGKLQEFG VGDGSKLTLV PTVEAGLMSQ ASRPEQSVMQ
ALESLTETQP PATPGPGRAA GGGFRKYRLI LFKRPWHRQG PQSPERGGER PQVSDFLSGR
SPLTLALRVG DHMMFVQLQL AAQHAPLQHR HVLAAAAAAA AAARGDSSIA TPVSSPCRPV
SSAARVPPVS SSPSSPVSPS PVTAGTFQSH AASTTCPEQT DCSPPASSNT TSTPGSSPTP
RSRKPGAVIE SFVNHAPGVF SGTFSGTLHP NCQDSSGRPR RDIGTILQIL NDLLSATRHY
QGMPASLTQL RCHAQCSPAS PAPDLTPKTT SCEKLATPSL LQGQSQIRMC KPPGDRLRQT
ENRATRCKVE RLQLLLQQKR LRRKARRDAR GPYHWTPSRK AGRSDSSSSG GGGSPSEATG
LGLDFEDSVW KPEVNPDIQS EFVVA