MCIN_RAT
ID MCIN_RAT Reviewed; 379 AA.
AC D3ZDX9; D4AE60;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Multicilin;
DE AltName: Full=Multiciliate differentiation and DNA synthesis-associated cell cycle protein;
DE Short=McIdas protein;
DE AltName: Full=Protein Idas;
GN Name=Mcidas; Synonyms=Idas, Mci, Mcin;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
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).
CC -!- FUNCTION: Transcription regulator specifically required for
CC multiciliate cell differentiation. Acts in a multiprotein complex
CC containing E2F4 and E2F5 that binds and activates genes required for
CC centriole biogenesis. Required for the deuterosome-mediated acentriolar
CC pathway. Plays a role in mitotic cell cycle progression by promoting
CC cell cycle exit. Modulates GMNN activity by reducing its affinity for
CC CDT1. {ECO:0000250|UniProtKB:D6RGH6, ECO:0000250|UniProtKB:Q08B36}.
CC -!- SUBUNIT: Heterodimer (via coiled-coil domain) with GMNN (via coiled-
CC coil domain); targets GMNN to the nucleus. Can form homodimers (in
CC vitro, via coiled-coil domain), but these are much less stable than the
CC heterodimer formed with GMNN. {ECO:0000250|UniProtKB:D6RGH6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:D6RGH6}.
CC Note=Excluded from the nucleolus. {ECO:0000250|UniProtKB:D6RGH6}.
CC -!- SIMILARITY: Belongs to the geminin family. {ECO:0000305}.
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DR AlphaFoldDB; D3ZDX9; -.
DR SMR; D3ZDX9; -.
DR STRING; 10116.ENSRNOP00000067993; -.
DR PhosphoSitePlus; D3ZDX9; -.
DR PaxDb; D3ZDX9; -.
DR RGD; 1584164; Mcidas.
DR eggNOG; ENOG502R4B5; Eukaryota.
DR InParanoid; D3ZDX9; -.
DR PRO; PR:D3ZDX9; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0098534; P:centriole assembly; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0044458; P:motile cilium assembly; ISS:UniProtKB.
DR GO; GO:1903251; P:multi-ciliated epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0045786; P:negative regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0008156; P:negative regulation of DNA replication; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:1902017; P:regulation of cilium assembly; ISS:UniProtKB.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; ISO:RGD.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISO:RGD.
DR InterPro; IPR022786; Geminin/Multicilin.
DR InterPro; IPR029699; Multicilin/Idas.
DR PANTHER; PTHR13372:SF3; PTHR13372:SF3; 1.
DR Pfam; PF07412; Geminin; 1.
PE 3: Inferred from homology;
KW Activator; Cell cycle; Cilium biogenesis/degradation; Coiled coil; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..379
FT /note="Multicilin"
FT /id="PRO_0000416280"
FT REGION 26..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 175..223
FT /evidence="ECO:0000250|UniProtKB:D6RGH6"
FT COMPBIAS 91..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 379 AA; 41162 MW; F20070693013FB12 CRC64;
MHACEGSAAG RRAFDSICPN RMLDLSRRSL GKPGKPERKF VPPWKSFPGC GGGSPVSVYE
DPLDAEPAPL PALTTIDLQD LADCTSLLGT EAPPSGDSPA SQNPSLQTEA DFNLQNFRDA
VDDLIADSSS LTSPPLTDGD FPFSPCDVPS FGSCLSPSLD PPALGSPHLP PPPTEQYWKE
VADQNQRALG TALIENNQLH VTLTQKQEEI ASLRERNVQL KELACRTRHL ASVLDKLMIT
QSPAEPFQLK ATTKRSLEEL FSATGQAGQG CAEVDAILRD ISQRCEEALQ NRDPKRPRLQ
QEPDSKDCST RNLHGVFRGL RTDCGASSVN LSHSELEEGG SFSTPIRSHS TIRTLAFPQG
KAFTIRTVTG GYKFRWVPS
