ID SIX1_GORGO Reviewed; 284 AA.
AC A1YER0;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=Homeobox protein SIX1;
DE AltName: Full=Sine oculis homeobox homolog 1;
GN Name=SIX1;
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Nickel G.C., Tefft D.L., Trevarthen K., Funt J., Adams M.D.;
RT "Positive selection in transcription factor genes on the human lineage.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription factor that is involved in the regulation of
CC cell proliferation, apoptosis and embryonic development (By
CC similarity). Plays an important role in the development of several
CC organs, including kidney, muscle and inner ear (By similarity).
CC Depending on context, functions as a transcriptional repressor or
CC activator (By similarity). Lacks an activation domain, and requires
CC interaction with EYA family members for transcription activation (By
CC similarity). Mediates nuclear translocation of EYA1 and EYA2 (By
CC similarity). Binds the 5'-TCA[AG][AG]TTNC-3' motif present in the MEF3
CC element in the MYOG promoter and CIDEA enhancer (By similarity).
CC Regulates the expression of numerous genes, including MYC, CCNA1, CCND1
CC and EZR (By similarity). Acts as an activator of the IGFBP5 promoter,
CC probably coactivated by EYA2 (By similarity). Repression of precursor
CC cell proliferation in myoblasts is switched to activation through
CC recruitment of EYA3 to the SIX1-DACH1 complex (By similarity). During
CC myogenesis, seems to act together with EYA2 and DACH2 (By similarity).
CC Regulates the expression of CCNA1 (By similarity). Promotes brown
CC adipocyte differentiation (By similarity).
CC {ECO:0000250|UniProtKB:Q15475, ECO:0000250|UniProtKB:Q62231}.
CC -!- SUBUNIT: Interacts with DACH1 (By similarity). Interacts with EYA1 (By
CC similarity). Interacts with EYA2 (By similarity). Interacts with CDH1
CC (By similarity). Interacts with TBX18 (By similarity). Interacts with
CC CEBPA (By similarity). Interacts with CEBPB (By similarity). Interacts
CC with EBF2 (By similarity). {ECO:0000250|UniProtKB:Q15475,
CC ECO:0000250|UniProtKB:Q62231}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
CC Cytoplasm {ECO:0000250}.
CC -!- PTM: Phosphorylated during interphase; becomes hyperphosphorylated
CC during mitosis. Hyperphosphorylation impairs binding to promoter
CC elements (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated by the anaphase promoting complex (APC), leading to
CC its proteasomal degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SIX/Sine oculis homeobox family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ976442; ABM46628.1; -; Genomic_DNA.
DR RefSeq; XP_004055308.1; XM_004055260.2.
DR AlphaFoldDB; A1YER0; -.
DR SMR; A1YER0; -.
DR STRING; 9593.ENSGGOP00000001372; -.
DR Ensembl; ENSGGOT00000001397.3; ENSGGOP00000001372.2; ENSGGOG00000001388.3.
DR GeneID; 101128790; -.
DR KEGG; ggo:101128790; -.
DR CTD; 6495; -.
DR eggNOG; KOG0775; Eukaryota.
DR GeneTree; ENSGT00940000156487; -.
DR HOGENOM; CLU_046914_2_0_1; -.
DR InParanoid; A1YER0; -.
DR OMA; YKAHYVE; -.
DR OrthoDB; 602349at2759; -.
DR Proteomes; UP000001519; Chromosome 14.
DR Bgee; ENSGGOG00000001388; Expressed in testis and 2 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISS:UniProtKB.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISS:UniProtKB.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; ISS:UniProtKB.
DR GO; GO:0030855; P:epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0048699; P:generation of neurons; ISS:UniProtKB.
DR GO; GO:0048839; P:inner ear development; ISS:UniProtKB.
DR GO; GO:0042472; P:inner ear morphogenesis; ISS:UniProtKB.
DR GO; GO:0001822; P:kidney development; ISS:UniProtKB.
DR GO; GO:0072172; P:mesonephric tubule formation; ISS:UniProtKB.
DR GO; GO:0072075; P:metanephric mesenchyme development; ISS:UniProtKB.
DR GO; GO:0051451; P:myoblast migration; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0001759; P:organ induction; ISS:UniProtKB.
DR GO; GO:0007389; P:pattern specification process; ISS:UniProtKB.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; ISS:UniProtKB.
DR GO; GO:0090336; P:positive regulation of brown fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0072107; P:positive regulation of ureteric bud formation; ISS:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0072095; P:regulation of branch elongation involved in ureteric bud branching; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISS:UniProtKB.
DR GO; GO:0045664; P:regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:0014857; P:regulation of skeletal muscle cell proliferation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0048741; P:skeletal muscle fiber development; IBA:GO_Central.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISS:UniProtKB.
DR GO; GO:0048538; P:thymus development; ISS:UniProtKB.
DR GO; GO:0030878; P:thyroid gland development; ISS:UniProtKB.
DR GO; GO:0001657; P:ureteric bud development; ISS:UniProtKB.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR008422; Homeobox_KN_domain.
DR InterPro; IPR031701; SIX1_SD.
DR PANTHER; PTHR10390; HOMEOBOX PROTEIN SIX; 1.
DR PANTHER; PTHR10390:SF13; HOMEOBOX PROTEIN SIX1; 1.
DR Pfam; PF05920; Homeobox_KN; 1.
DR Pfam; PF16878; SIX1_SD; 1.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 3: Inferred from homology;
KW Activator; Apoptosis; Cytoplasm; Developmental protein; DNA-binding;
KW Homeobox; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..284
FT /note="Homeobox protein SIX1"
FT /id="PRO_0000285458"
FT DNA_BIND 124..183
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 168..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 284 AA; 32210 MW; A4195376CFB9E3EA CRC64;
MSMLPSFGFT QEQVACVCEV LQQGGNLERL GRFLWSLPAC DHLHKNESVL KAKAVVAFHR
GNFRELYKIL ESHQFSPHNH PKLQQLWLKA HYVEAEKLRG RPLGAVGKYR VRRKFPLPRT
IWDGEETSYC FKEKSRGVLR EWYAHNPYPS PREKRELAEA TGLTTTQVSN WFKNRRQRDR
AAEAKERENT ENNNSSSNKQ NQLSPLEGGK PLMSSSEEEF SPPQSPDQNS VLLLQGNMGH
ARSSNYSLPG LTASQPSHGL QTHQHQLQDS LLGPLTSSLV DLGS
//
