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MCIN_MOUSE
ID   MCIN_MOUSE              Reviewed;         379 AA.
AC   Q3UZ45;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=Gm6320, Idas, Mci, Mcin;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
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   [2]
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   [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [5]
RP   DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX   PubMed=21543332; DOI=10.1074/jbc.m110.207688;
RA   Pefani D.E., Dimaki M., Spella M., Karantzelis N., Mitsiki E., Kyrousi C.,
RA   Symeonidou I.E., Perrakis A., Taraviras S., Lygerou Z.;
RT   "Idas, a novel phylogenetically conserved geminin-related protein, binds to
RT   geminin and is required for cell cycle progression.";
RL   J. Biol. Chem. 286:23234-23246(2011).
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:0000269|PubMed:21543332}.
CC       Note=Excluded from the nucleolus. {ECO:0000250|UniProtKB:D6RGH6}.
CC   -!- DEVELOPMENTAL STAGE: At 12.5 dpc expression is restricted to the
CC       developing mouse brain. High levels are detected in the cortical hem
CC       and the choroid plexus epithelium in the telencephalic midline by cells
CC       starting to differentiate (at protein level).
CC       {ECO:0000269|PubMed:21543332}.
CC   -!- SIMILARITY: Belongs to the geminin family. {ECO:0000305}.
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DR   EMBL; AK134107; BAE22015.1; -; mRNA.
DR   EMBL; AC165265; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466568; EDL18399.1; -; Genomic_DNA.
DR   EMBL; BC150962; AAI50963.1; -; mRNA.
DR   CCDS; CCDS36783.1; -.
DR   RefSeq; NP_001033003.1; NM_001037914.3.
DR   AlphaFoldDB; Q3UZ45; -.
DR   SMR; Q3UZ45; -.
DR   STRING; 10090.ENSMUSP00000089721; -.
DR   PhosphoSitePlus; Q3UZ45; -.
DR   PaxDb; Q3UZ45; -.
DR   PRIDE; Q3UZ45; -.
DR   Antibodypedia; 62363; 107 antibodies from 17 providers.
DR   Ensembl; ENSMUST00000092089; ENSMUSP00000089721; ENSMUSG00000074651.
DR   GeneID; 622408; -.
DR   KEGG; mmu:622408; -.
DR   UCSC; uc007rxa.1; mouse.
DR   CTD; 345643; -.
DR   MGI; MGI:3648807; Mcidas.
DR   VEuPathDB; HostDB:ENSMUSG00000074651; -.
DR   eggNOG; ENOG502R4B5; Eukaryota.
DR   GeneTree; ENSGT00940000153270; -.
DR   HOGENOM; CLU_063884_0_0_1; -.
DR   InParanoid; Q3UZ45; -.
DR   OMA; ITQSRDC; -.
DR   OrthoDB; 935155at2759; -.
DR   PhylomeDB; Q3UZ45; -.
DR   TreeFam; TF101171; -.
DR   BioGRID-ORCS; 622408; 4 hits in 71 CRISPR screens.
DR   PRO; PR:Q3UZ45; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q3UZ45; protein.
DR   Bgee; ENSMUSG00000074651; Expressed in vascular system and 17 other tissues.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
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:MGI.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; ISS:UniProtKB.
DR   InterPro; IPR022786; Geminin/Multicilin.
DR   InterPro; IPR029699; Multicilin/Idas.
DR   PANTHER; PTHR13372:SF3; PTHR13372:SF3; 1.
DR   Pfam; PF07412; Geminin; 1.
PE   1: Evidence at protein level;
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_0000411077"
FT   REGION          1..129
FT                   /note="Necessary and sufficient for its degradation during
FT                   the cell cycle"
FT                   /evidence="ECO:0000250"
FT   REGION          26..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          130..379
FT                   /note="Necessary and sufficient for proper nuclear
FT                   localization"
FT                   /evidence="ECO:0000250"
FT   REGION          171..241
FT                   /note="Necessary and sufficient for interaction with GMNN
FT                   and sufficient for homodimerization"
FT                   /evidence="ECO:0000250"
FT   REGION          291..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          175..223
FT                   /evidence="ECO:0000250|UniProtKB:D6RGH6"
FT   COMPBIAS        291..311
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   379 AA;  41148 MW;  1750B792D6EBFF43 CRC64;
     MQACEGSAAG RRAFDSICPN RMLDLSRRTL GKPGKPERKF VPSWKSFSGC GGGSPVAVYE
     DPPDAEPAPL PALTTIDLQD LADCTSLLGT EASPSGDSSA SQNPSLQTEE DFNLQNFRDA
     MDDLIADSSS LMSPPLTNSD FPFSPCDVSS FGSCLSPSLD PPALGSPDLP PPPTEQYWKE
     VADQNQRALG TALIENNQLH VTLTQKQEEI ASLRERNVQL KELASRTRHL ASVLDKLMIT
     QSPAEPFQIK ATTKRSLEEL FCAAGQAGQG CAEVDAILRD ISQRCEEALH NRDPKRPRLQ
     PEPDSKDCSS RNLHGAFRGL RTDCSASSVN LSHSELEEGG SFSTPIRSHS TIRTLAFPQG
     KAFTIRTVTG GYKFRWVPS
 
 
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