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Database: UniProt
Entry: F6PIG8_CALJA
LinkDB: F6PIG8_CALJA
Original site: F6PIG8_CALJA 
ID   F6PIG8_CALJA            Unreviewed;      1484 AA.
AC   F6PIG8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 4.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Homeobox protein cut-like {ECO:0000256|RuleBase:RU361129};
GN   Name=CUX2 {ECO:0000313|Ensembl:ENSCJAP00000021531.5};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000021531.5, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000021531.5}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000021531.5}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108,
CC       ECO:0000256|RuleBase:RU000682}.
CC   -!- SIMILARITY: Belongs to the CUT homeobox family.
CC       {ECO:0000256|ARBA:ARBA00008190, ECO:0000256|RuleBase:RU361129}.
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DR   STRING; 9483.ENSCJAP00000021531; -.
DR   Ensembl; ENSCJAT00000022758.5; ENSCJAP00000021531.5; ENSCJAG00000011694.5.
DR   eggNOG; KOG0963; Eukaryota.
DR   eggNOG; KOG2252; Eukaryota.
DR   GeneTree; ENSGT00940000160241; -.
DR   HOGENOM; CLU_005104_1_0_1; -.
DR   InParanoid; F6PIG8; -.
DR   OMA; FHNYSRM; -.
DR   OrthoDB; 74668at2759; -.
DR   TreeFam; TF318206; -.
DR   Proteomes; UP000008225; Chromosome 9.
DR   Bgee; ENSCJAG00000011694; Expressed in frontal cortex and 2 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0071310; P:cellular response to organic substance; IEA:Ensembl.
DR   GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IEA:Ensembl.
DR   GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
DR   GO; GO:0007614; P:short-term memory; IEA:Ensembl.
DR   CDD; cd00086; homeodomain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 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   PANTHER; PTHR14043; CCAAT DISPLACEMENT PROTEIN-RELATED; 1.
DR   PANTHER; PTHR14043:SF5; HOMEOBOX PROTEIN CUT-LIKE 2; 1.
DR   Pfam; PF02376; CUT; 3.
DR   Pfam; PF00046; Homeodomain; 1.
DR   SMART; SM01109; CUT; 3.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 3.
DR   PROSITE; PS51042; CUT; 3.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU00108};
KW   Homeobox {ECO:0000256|ARBA:ARBA00023155, ECO:0000256|PROSITE-
KW   ProRule:PRU00108};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00108}; Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW   Transcription {ECO:0000256|RuleBase:RU361129};
KW   Transcription regulation {ECO:0000256|RuleBase:RU361129}.
FT   DOMAIN          544..631
FT                   /note="CUT"
FT                   /evidence="ECO:0000259|PROSITE:PS51042"
FT   DOMAIN          886..973
FT                   /note="CUT"
FT                   /evidence="ECO:0000259|PROSITE:PS51042"
FT   DOMAIN          1037..1124
FT                   /note="CUT"
FT                   /evidence="ECO:0000259|PROSITE:PS51042"
FT   DOMAIN          1165..1225
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000259|PROSITE:PS50071"
FT   DNA_BIND        1167..1226
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT   REGION          115..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          416..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          516..549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          661..689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          716..736
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          800..850
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          963..1030
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1230..1454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          200..273
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          310..355
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        129..144
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..466
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..532
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        801..818
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        977..994
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        995..1027
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1259..1279
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1280..1295
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1321..1336
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1378..1414
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1415..1430
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1484 AA;  161586 MW;  CB912C68E441C522 CRC64;
     MAANVGSMFQ YWKRFDLRRL QKELNSVASE LSARQEESEH SHKHLIELRR EFKKNVPEEI
     REMVAPVLKS FQAEVVALSK RSQEAEAAFL SVYKQLIEAP DPVPVFEAAR SLDDRLQPPS
     FEPSGQHRQD LHTSWKRNPE LLSPKEQREG TSPTVPTLTE GSHLPGIPGK ALLTETLLQR
     NEAEKQKGLQ EVQITLAARL GEAEEKIKVL HSALKATQAE LLELRRKYDE EAASKADEVG
     LIMTNLEKAN QRAEAAQREV ESLREQLASV NSSIRLACCS PQGPSGDKVN FALCSGPRLE
     AALASKDREI LRLLKDVQHL QSSLQELEEA SANQIADLER QLTAKSEAIE KLEEKLQAQS
     DYEEIKTELS ILKAMKLASS TCSLPQGMAK PEDSLLIAKE AFFPAQKFLL EKPSLLASPE
     EDPSEDDSIK DSLGTEQSYP SPQQLPPPPG PEDPLSPSPG QPLLGPTLGP DGPRTFSLSP
     FPSLASGERL MMPPATFKGE AGGLLVFPPA FYGTKPPTAP ATPAPGPELP GGPEPTDGGG
     GGAAGPGAEE EQLDTAEIAF QVKEQLLKHN IGQRVFGHYV LGLSQGSVSE ILARPKPWRK
     LTVKGKEPFI KMKQFLSDEQ NVLALRTIQV RQRGSITPRI RTPETGSDDA IKSILEQAKK
     EIESQKGGEP KTSAAPLSIA NGAGPASTSE DAIKSILEQA RREMQAQQQA LLEMEAAPRG
     RSVPASPPER PSLATANQNG APALVKQEEG GGGPAQAPLP VLSPAAFVQS IIRKVKSEIG
     DAGYFDHHWA SDRGLLSRPY ASVSPSLSSS SSGYSGQPNG RAWPRGDEAP APPEDEATAG
     AEDEPSRAGE LKAEGMVAEA GARLPYYPAY VPRTLKPTVP PLTPEQYELY MYREVDTLEL
     TRQVKEKLAK NGICQRIFGE KVLGLSQGSV SDMLSRPKPW SKLTQKGREP FIRMQLWLSD
     QLGQAVGQQP GPSQASPTEP RSSPSPPPSP TEPEKSSQEP LSLSLESSKE NQQPEGRSSS
     SLSGKMYSGG QAPGGIQEIV AMSPELDTYS ITKRVKEVLT DNNLGQRLFG ESILGLTQGS
     VSDLLSRPKP WHKLSLKGRE PFVRMQLWLN DPHNVEKLRD MKKLEKKAYL KRRYGLISTG
     SDSESPATRS ECPSPCLQPQ DLSLLQIKKP RVVLAPEEKE ALRKAYQLEP YPSQQTIELL
     SFQLNLKTNT VINWFHNYRS RMRREMLVEG TQDEPDLDPS GGPGILPPGH SHPDPTPQSP
     DSETEDQKPT VKELELQEGP EENSTTLTTQ DKAQVRIKQE QTEDTEEEAG SQPQDLGEPD
     KGQGPPKEEH PDPLGNDRLQ KVAPGPLLPG GPIPDSPSLH PPQESEAGER LHPDPLSFKS
     ASESSRCSLE VSLNSPSAAS SPGLMMSVSP VPSSSAPISP SPPGAPPAKV PSASPTADMA
     GALHPNAKVN PNLQRRHEKM ANLNSIIYRL ERAANREEAL EWEF
//
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