CUX2_MOUSE
ID CUX2_MOUSE Reviewed; 1426 AA.
AC P70298; Q6P1E6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Homeobox protein cut-like 2;
DE AltName: Full=Homeobox protein Cux-2;
GN Name=Cux2; Synonyms=Cutl2;
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 [MRNA].
RX PubMed=8798433; DOI=10.1074/jbc.271.37.22624;
RA Quaggin S.E., Vanden Heuvel G.B., Golden K., Bodmer R., Igarashi P.;
RT "Primary structure, neural-specific expression, and chromosomal
RT localization of Cux-2, a second murine homeobox gene related to Drosophila
RT cut.";
RL J. Biol. Chem. 271:22624-22634(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18033766; DOI=10.1093/cercor/bhm199;
RA Cubelos B., Sebastian-Serrano A., Kim S., Moreno-Ortiz C., Redondo J.M.,
RA Walsh C.A., Nieto M.;
RT "Cux-2 controls the proliferation of neuronal intermediate precursors of
RT the cortical subventricular zone.";
RL Cereb. Cortex 18:1758-1770(2008).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20510857; DOI=10.1016/j.neuron.2010.04.038;
RA Cubelos B., Sebastian-Serrano A., Beccari L., Calcagnotto M.E.,
RA Cisneros E., Kim S., Dopazo A., Alvarez-Dolado M., Redondo J.M.,
RA Bovolenta P., Walsh C.A., Nieto M.;
RT "Cux1 and Cux2 regulate dendritic branching, spine morphology, and synapses
RT of the upper layer neurons of the cortex.";
RL Neuron 66:523-535(2010).
CC -!- FUNCTION: Transcription factor involved in the control of neuronal
CC proliferation and differentiation in the brain (PubMed:18033766,
CC PubMed:20510857). Regulates dendrite development and branching,
CC dendritic spine formation, and synaptogenesis in cortical layers II-III
CC (PubMed:20510857). Binds to DNA in a sequence-specific manner.
CC {ECO:0000269|PubMed:18033766, ECO:0000269|PubMed:20510857}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Restricted to neural tissues. Expressed exclusively
CC in the central and peripheral nervous systems.
CC -!- DISRUPTION PHENOTYPE: Knockout mice show moderately but consistently
CC bigger brains than wild-type animals. Cell density and thickness of
CC upper cortical layers (II-IV) are increased, while there are no
CC differences in neuronal density in layers V and VI (PubMed:18033766).
CC Neurons in layer II-III show simpler morphologies, with a significant
CC decrease in the dendritic length and the number of branches, as well as
CC a severe reduction of dendritic spines density associated with synaptic
CC defects. The working memory is impaired (PubMed:20510857).
CC {ECO:0000269|PubMed:18033766, ECO:0000269|PubMed:20510857}.
CC -!- SIMILARITY: Belongs to the CUT homeobox family. {ECO:0000305}.
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DR EMBL; U45665; AAC52762.1; -; mRNA.
DR EMBL; BC065113; AAH65113.1; -; mRNA.
DR CCDS; CCDS39251.1; -.
DR PIR; T30817; T30817.
DR RefSeq; NP_001299837.1; NM_001312908.1.
DR RefSeq; NP_031830.2; NM_007804.2.
DR AlphaFoldDB; P70298; -.
DR SMR; P70298; -.
DR IntAct; P70298; 1.
DR STRING; 10090.ENSMUSP00000107381; -.
DR iPTMnet; P70298; -.
DR PhosphoSitePlus; P70298; -.
DR MaxQB; P70298; -.
DR PaxDb; P70298; -.
DR PeptideAtlas; P70298; -.
DR PRIDE; P70298; -.
DR ProteomicsDB; 284068; -.
DR Antibodypedia; 31073; 84 antibodies from 21 providers.
DR DNASU; 13048; -.
DR Ensembl; ENSMUST00000086317; ENSMUSP00000083497; ENSMUSG00000042589.
DR Ensembl; ENSMUST00000111752; ENSMUSP00000107381; ENSMUSG00000042589.
DR Ensembl; ENSMUST00000168288; ENSMUSP00000130302; ENSMUSG00000042589.
DR GeneID; 13048; -.
DR KEGG; mmu:13048; -.
DR UCSC; uc008zkm.1; mouse.
DR CTD; 23316; -.
DR MGI; MGI:107321; Cux2.
DR VEuPathDB; HostDB:ENSMUSG00000042589; -.
DR eggNOG; KOG0963; Eukaryota.
DR eggNOG; KOG2252; Eukaryota.
DR GeneTree; ENSGT00940000160241; -.
DR HOGENOM; CLU_005104_1_0_1; -.
DR InParanoid; P70298; -.
DR OMA; QVDTAEI; -.
DR OrthoDB; 181575at2759; -.
DR PhylomeDB; P70298; -.
DR TreeFam; TF318206; -.
DR BioGRID-ORCS; 13048; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Cux2; mouse.
DR PRO; PR:P70298; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P70298; protein.
DR Bgee; ENSMUSG00000042589; Expressed in layer of neocortex and 222 other tissues.
DR ExpressionAtlas; P70298; baseline and differential.
DR Genevisible; P70298; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IMP:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0071310; P:cellular response to organic substance; IDA:MGI.
DR GO; GO:0050890; P:cognition; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:UniProtKB.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IMP:UniProtKB.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007614; P:short-term memory; IMP:UniProtKB.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 1.10.260.40; -; 3.
DR InterPro; IPR003350; CUT_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR Pfam; PF02376; CUT; 3.
DR Pfam; PF00046; Homeodomain; 1.
DR SMART; SM01109; CUT; 3.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47413; SSF47413; 3.
DR PROSITE; PS51042; CUT; 3.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; DNA-binding; Homeobox; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..1426
FT /note="Homeobox protein cut-like 2"
FT /id="PRO_0000202397"
FT DNA_BIND 482..569
FT /note="CUT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374"
FT DNA_BIND 828..915
FT /note="CUT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374"
FT DNA_BIND 983..1070
FT /note="CUT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374"
FT DNA_BIND 1113..1172
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 77..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1177..1392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 131..311
FT /evidence="ECO:0000255"
FT COILED 587..655
FT /evidence="ECO:0000255"
FT COMPBIAS 374..401
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..940
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..977
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1296..1357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1372
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14529"
FT CONFLICT 199
FT /note="S -> G (in Ref. 1; AAC52762)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="S -> N (in Ref. 1; AAC52762)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="T -> M (in Ref. 1; AAC52762)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="T -> N (in Ref. 1; AAC52762)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1426 AA; 154664 MW; 485B87D1C88D2577 CRC64;
MVAPVLKSFQ AEVVALSKRS REAEAAFLSV YKQLIEAPDP VPSFEVARTL DDRLQRPSFD
PSGQRLQDVH IAWKRCPEPP SAREQNEGTC PTGHTPANGN HLPGPEDTLV TDTLLQKNEA
ERQKGLQEVH ITLAARLGEA EEKIKVLHSA LKATQTELLE LRRKYDEEAA SKADEVGLIM
TNLEKANQRA EAAQREVESL REQLASVNSS IRLACCSPQG PSGEKVSFAL CSGPRLEAAL
ASKDREILRL LKDAQQLRHS LQELEEVSAN QIADLERQLA AKSEAIEKLQ EKLEAQADYE
EIKTELSILR AMKLASSTCS LPQTLAKPDD PLLVAKDVFF PTQKFLLEKP ALLASPEEDP
SEDDSIKGSL GTEPPYPPQL PPPPGPEDPL SPSPAQPLLG PSLGPDGPRT FSLSPFPSLA
PGERLAGDSL LSKHMMGPAA FKGETGNLLA FPPTFYGGAK PPSAPAASVP CPEPTGAPEA
VDGAGPEEEQ LDTAEIAFQV KEQLLKHNIG QRVFGHYVLG LSQGSVSEIL ARPKPWRKLT
VKGKEPFIKM KQFLSDEQNV LALRTIQVRQ RGSITPRIRT PETGSDDAIK SILEQAKKEI
ESQKGGESKN SPASVSIPNG TASSSTSEDA IKNILEQARR EMQAQQQALL EMESGPRGRS
VPPSPPERPS PATASQNGAL TCVKQEDGGG GSGSSSTVQA PLAVLSPAAF VQRIIRKVKS
EIGDAGYFDH HWASDRGLLS RPYASVSPSL SSSSSYSGQP NGRAWPRGDE ATIAPEDEAA
MGEDEAPRVG ELKAEAGAPE VGGGRLPYYP AYVPRTLKPT VPPLTPEQYE LYMYREVDTL
ELTRQVKEKL AKNGICQRIF GEKVLGLSQG SVSDMLSRPK PWSKLTQKGR EPFIRMQLWL
SDQLGQGQGQ APTQQPSASQ ASPTEPTSSP SPPPSPTEPE KTSQEPLGLS LESSKENQQP
EGRASSSLGG KPFSSSQAAG GIQEMVAMSP ELDTYSITKR VKEVLTDNNL GQRLFGESIL
GLTQGSVSDL LSRPKPWHKL SLKGREPFVR MQLWLSDPHN VEKLRDMKKL EKKAYLKRRY
GLIGTGSDSE SPAAHSECPS PCLQPQELSL MQAKKPRVVL APAEKEALRK AYQLEPYPSQ
QTIELLSFQL NLKTNTVINW FHNYRSRMRR EMLVEGTQDD PDFDPSGGPN VLTPGHTHRE
PTPQSPDSET EDQKPPMKSL ELQEPEGPLQ RAAPDRALVK IKQEEGLEVD GDSQPQDVGD
PDRGQDGPKE EHTHPLGNSD LSELAPGPFL SGTPNPDCPS LHNPQEKGTG EQVHSEPLSF
KSTSESSCCS LEGPPNSPSV ISSPDLTTCV SPAPSSSAPI SPSLPGAPPA KVPSTSPTGD
TAAALHPSTK VNPNLQRRHE KMANLNSIIY RLERAANREE VLEWEF
