ID F7IP03_CALJA Unreviewed; 1521 AA.
AC F7IP03;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 4.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Homeobox protein cut-like {ECO:0000256|RuleBase:RU361129};
GN Name=CUX1 {ECO:0000313|Ensembl:ENSCJAP00000029680.5};
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:ENSCJAP00000029680.5, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000029680.5}
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:ENSCJAP00000029680.5}
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.ENSCJAP00000029680; -.
DR Ensembl; ENSCJAT00000031364.5; ENSCJAP00000029680.5; ENSCJAG00000016076.5.
DR eggNOG; KOG0963; Eukaryota.
DR eggNOG; KOG2252; Eukaryota.
DR GeneTree; ENSGT00940000159751; -.
DR InParanoid; F7IP03; -.
DR OMA; LESKPYH; -.
DR TreeFam; TF318206; -.
DR Proteomes; UP000008225; Chromosome 2.
DR Bgee; ENSCJAG00000016076; Expressed in kidney and 6 other cell types or tissues.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; 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:SF4; HOMEOBOX PROTEIN CUT-LIKE 1; 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 553..640
FT /note="CUT"
FT /evidence="ECO:0000259|PROSITE:PS51042"
FT DOMAIN 948..1035
FT /note="CUT"
FT /evidence="ECO:0000259|PROSITE:PS51042"
FT DOMAIN 1131..1218
FT /note="CUT"
FT /evidence="ECO:0000259|PROSITE:PS51042"
FT DOMAIN 1256..1316
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DNA_BIND 1258..1317
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT REGION 407..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1225..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1326..1496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 112..355
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 448..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..943
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1087
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1116
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1369..1384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1456..1471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1521 AA; 166223 MW; C159EF3D516AB0AF CRC64;
MAANVGSMFQ YWKRFDLQQL QRELDATATV LANRQDESEQ SRKRLIEQSR EFKKNTPEDL
RKQVAPLLKS FQGEIDALSK RSKEAEAAFL NVYKRLIDVP DPVPALDLGQ QLQLKVQRLH
DIETENQKLR ETLEEYNKEF AEVKNQEVTI KALKEKIREY EQTLKNQAET IALEKEQKLQ
NDFAEKERKL QETQMSTTSK LEEAEHKVQS LQTALEKTRT ELFDLKTKYD EETTAKADEI
EMIMTDLERA NQRAEVAQRE AETLREQLSS ANHSLQLASQ IQKAPDVEQA IEVLTRSSLE
VELAAKEREI AQLVEDVQRL QAGLTKLREN SASQISQLEQ QLSAKNSTLK QLEEKLKGQA
DYEEVKKELN ILKSMEFAPS EGAGTQDAAK PLEVLLLEKN RSLQSENAAL RISNSDLSGS
ARRKGKDQPE SRRPGSLPAP PPSQLPRNPG EQASNTNGTH QFSPAGLSQD FFSSSLASPS
LPLASTGKFA LNSLLQRQLM QSFYSKAMQE AGSTSMIFST GPYSTNSISS QSPLQQSPDV
NGMAPSPSQS ESAGSVSEGE DMDTAEIARQ VKEQLIKHNI GQRIFGHYVL GLSQGSVSEI
LARPKPWNKL TVRGKEPFHK MKQFLSDEQN ILALRSIQGR QRENPGQSLN RLFQEVPKRR
NGSEGNITTR IRASETGSDE AIKSILEQAK RELQVQKTAE PAQPSSASGS GNSDDAIRSI
LQQARREMEA QQAALDPALK QASLSQSDIT ILTPKLLSTS PMPTVSTYPP LAISLKKPPA
APEAGASALP NPPALKKEAQ DTPGLDPQGV ADCAQGVLRQ VKNEVGRSGA WKDHWWSTVQ
VQPERRNATA SSEEAKAEEV GSGKDKGGGG SGGSSQPRAE RSQLQGPTSS EYWKEWPSAE
SPYSQSSELS LTGASRSETP QNSPLPSSPL VPMSKPTKPS VPPLTPEQYE VYMYQEVDTI
ELTRQVKEKL AKNGICQRIF GEKVLGLSQG SVSDMLSRPK PWSKLTQKGR EPFIRMQLWL
NGELGQGVLP VQGQQQGPVL HSVTSLQDPL QQGCVSSEST PKTSASCSPA PESPMSSSES
VKSLTELVQQ PCPPIEANKD GKPPEPSDPP ASDSQPATPL PLSGHSALSI QELVAMSPEL
DTYGITKRVK EVLTDNNLGQ RLFGETILGL TQGSVSDLLA RPKPWHKLSL KGREPFVRMQ
LWLNDPNNVE KLMDMKRMEK KAYMKRRHSS VSDTQPCEPP SVGTEYSQGA SPQPQHQLKK
PRVVLAPEEK EALKRAYQQK PYPSPKTIED LATQLNLKTS TVINWFHNYR SRIRRELFIE
EIQAGSQGQA GASDSPSARS GRAAPSSEGD SCDGVEAPEG PGSADTEEPK SQGEAEREEA
PRPAEQTEPL PSGTPGPDDA RDDDHEGGPA DGPEPLPSPA TATATATAAP AAPEDAATSA
AAPPGEGPAA PSSAPPPGSG SSSSAPRRPS SLQSLFGLPE AAGARDSRDN PLRKKKAANL
NSIIHRLEKA ASREEPIEWE F
//
