MCIN_XENLA
ID MCIN_XENLA Reviewed; 374 AA.
AC Q08B36;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Multicilin {ECO:0000303|PubMed:22231168};
DE AltName: Full=Multiciliate differentiation and DNA synthesis-associated cell cycle protein {ECO:0000303|PubMed:22231168};
DE Short=McIdas protein;
DE AltName: Full=Protein Idas;
GN Name=mcidas;
GN Synonyms=idas, mci {ECO:0000303|PubMed:22231168},
GN mcin {ECO:0000303|PubMed:22231168};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22231168; DOI=10.1038/ncb2406;
RA Stubbs J.L., Vladar E.K., Axelrod J.D., Kintner C.;
RT "Multicilin promotes centriole assembly and ciliogenesis during
RT multiciliate cell differentiation.";
RL Nat. Cell Biol. 14:140-147(2012).
RN [3]
RP FUNCTION, IDENTIFICATION IN THE EDM COMPLEX, AND MUTAGENESIS OF GLY-355 AND
RP ARG-370.
RX PubMed=24934224; DOI=10.1101/gad.243832.114;
RA Ma L., Quigley I., Omran H., Kintner C.;
RT "Multicilin drives centriole biogenesis via E2f proteins.";
RL Genes Dev. 28:1461-1471(2014).
RN [4]
RP MUTAGENESIS OF GLY-355 AND ARG-370.
RX PubMed=25048963; DOI=10.1038/ncomms5418;
RA Boon M., Wallmeier J., Ma L., Loges N.T., Jaspers M., Olbrich H.,
RA Dougherty G.W., Raidt J., Werner C., Amirav I., Hevroni A., Abitbul R.,
RA Avital A., Soferman R., Wessels M., O'Callaghan C., Chung E.M., Rutman A.,
RA Hirst R.A., Moya E., Mitchison H.M., Van Daele S., De Boeck K.,
RA Jorissen M., Kintner C., Cuppens H., Omran H.;
RT "MCIDAS mutations result in a mucociliary clearance disorder with reduced
RT generation of multiple motile cilia.";
RL Nat. Commun. 5:4418-4418(2014).
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. Activates genes required for centriole assembly
CC (plk4, cep152) and genes specifically required for motile cilia
CC formation (foxj1). Also promotes the deuterosome pathway of centriole
CC biogenesis by activating expression of ccdc67/deup1, but not its
CC paralog cep63. {ECO:0000269|PubMed:22231168,
CC ECO:0000269|PubMed:24934224}.
CC -!- SUBUNIT: Component of the EDM complex, at least composed of e2f4, e2f5,
CC mcidas and tfdp1. {ECO:0000269|PubMed:24934224}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22231168}.
CC -!- TISSUE SPECIFICITY: Expressed in multiciliate differentiating cells.
CC Expression is lost by stage 26, when multiciliate cells in the skin are
CC fully differentiated, but is then detected in the developing
CC nephrostomes of the kidneys where multiciliate cells form at later
CC stages. {ECO:0000269|PubMed:22231168}.
CC -!- INDUCTION: Down-regulated by Notch signaling.
CC -!- DOMAIN: The TIRT domain mediates interaction with e2f4 and tfdp1.
CC {ECO:0000269|PubMed:24934224}.
CC -!- SIMILARITY: Belongs to the geminin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI24893.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC124892; AAI24893.1; ALT_INIT; mRNA.
DR RefSeq; NP_001121276.1; NM_001127804.1.
DR AlphaFoldDB; Q08B36; -.
DR MaxQB; Q08B36; -.
DR DNASU; 100158359; -.
DR GeneID; 100158359; -.
DR KEGG; xla:100158359; -.
DR CTD; 100158359; -.
DR Xenbase; XB-GENE-22041450; mcidas.S.
DR OrthoDB; 935155at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 100158359; Expressed in egg cell and 7 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0098534; P:centriole assembly; IDA:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0044458; P:motile cilium assembly; IDA:UniProtKB.
DR GO; GO:1903251; P:multi-ciliated epithelial cell differentiation; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:1902017; P:regulation of cilium assembly; ISS:UniProtKB.
DR GO; GO:0006275; P:regulation of DNA replication; IEA:InterPro.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:2001141; P:regulation of RNA biosynthetic process; TAS: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..374
FT /note="Multicilin"
FT /id="PRO_0000411079"
FT REGION 230..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..374
FT /note="TIRT domain"
FT /evidence="ECO:0000303|PubMed:24934224"
FT COILED 164..212
FT /evidence="ECO:0000250|UniProtKB:D6RGH6"
FT MUTAGEN 355
FT /note="G->D: Loss of function due to disruption of the EDM
FT complex."
FT /evidence="ECO:0000269|PubMed:25048963"
FT MUTAGEN 370
FT /note="R->H: Loss of function due to disruption of the EDM
FT complex."
FT /evidence="ECO:0000269|PubMed:25048963"
SQ SEQUENCE 374 AA; 41907 MW; 2013DD7202C27E6F CRC64;
MQNRRKAFYK LCPNAMPDLS NRLSKKQSKT EKKLHKNIFA HTGPVTIYVD PPSSAVDSAL
ATIDWQDLVD CNSVIQQDAA GGAITQQQDH CLSGEPDFDL QEFRDAVDQF IADQPSLMQP
SLGPPEFQLP ACNVPVFEPC MTNPLQAQPE HLLPINVQTI PSTEQYWRDV ADHNQKALGD
ALVENNQLQV SLTEKQEEIV SLKEKNIQLN ELANQAKHLS SVLDKLMKER TKQNSGATQG
RLPVKRSLED FYPQSNEPDS TQVDEILREI SKKCNIALMG SDLSERKRPR LEPMDSMDWQ
EEGVTEIKMC GAFHGLKTST GLNSVNLGDT DLEDVSFRTS IKEHSTIRTL AFPQGNAFTI
RTSGGGYKFR WVPN
