ID   MCIN_PIG                Reviewed;         388 AA.
AC   F1SLM8;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 48.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
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   EMBL; CU929626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F1SLM8; -.
DR   SMR; F1SLM8; -.
DR   PRIDE; F1SLM8; -.
DR   Ensembl; ENSSSCT00000052937; ENSSSCP00000033119; ENSSSCG00000036183.
DR   VGNC; VGNC:90071; MCIDAS.
DR   GeneTree; ENSGT00940000153270; -.
DR   InParanoid; F1SLM8; -.
DR   OMA; ITQSRDC; -.
DR   OrthoDB; 935155at2759; -.
DR   Proteomes; UP000008227; Chromosome 16.
DR   Proteomes; UP000314985; Unplaced.
DR   Bgee; ENSSSCG00000036183; Expressed in oocyte and 3 other tissues.
DR   GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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; IEA:Ensembl.
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   3: Inferred from homology;
KW   Activator; Cell cycle; Cilium biogenesis/degradation; Coiled coil; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..388
FT                   /note="Multicilin"
FT                   /id="PRO_0000411078"
FT   REGION          2..133
FT                   /note="Necessary and sufficient for its degradation during
FT                   the cell cycle"
FT                   /evidence="ECO:0000250"
FT   REGION          23..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          134..388
FT                   /note="Necessary and sufficient for proper nuclear
FT                   localization"
FT                   /evidence="ECO:0000250"
FT   REGION          176..248
FT                   /note="Necessary and sufficient for interaction with GMNN
FT                   and sufficient for homodimerization"
FT                   /evidence="ECO:0000250"
FT   REGION          298..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          182..230
FT                   /evidence="ECO:0000250|UniProtKB:D6RGH6"
FT   COMPBIAS        32..46
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   388 AA;  42231 MW;  DCD955193A054712 CRC64;
     MQAACGGAAA GRRVFDSLCP NRMLDPQGRP FGKPGKLDRK FAPPRKFFPD RSISSRVSVY
     EDPPDPEPAA LPALTTIDLQ DLRDLADCSS LLGSHAPPSG DSAASQNHSL QTAADFDLQD
     FRDTVDDLIA DSSSLMSPPL AGGNFPFSPS DVLPFGSCLS PPLDSPALQS PPLRPPEVPP
     PEQYWKELAN QNQRALGDAL VENNQLHVTL TQKQEEIASL KERNVQLKEL ASRTRHLASV
     LDKLMITRSQ DCGAAAEPFL LKATAKRSLE ELFSAAGQDC AEVDAILREI SERCDEALQS
     RDPKRLRLQP EPPSMDGRPG NLHGAFRGLR TDCSRSSLNL SHSELEEGGS FSTPIRSHST
     IRTLAFPQGN AFTIRTANGG YKFRWVPS