SIX6_MOUSE
ID SIX6_MOUSE Reviewed; 246 AA.
AC Q9QZ28; O88423;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Homeobox protein SIX6;
DE AltName: Full=Optic homeobox 2;
DE AltName: Full=Sine oculis homeobox homolog 6;
DE AltName: Full=Six9 protein;
GN Name=Six6; Synonyms=Optx2, Six9;
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 {ECO:0000312|EMBL:CAA09775.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=9724757; DOI=10.1073/pnas.95.18.10643;
RA Toy J., Yang J.-M., Leppert G.S., Sundin O.H.;
RT "The optx2 homeobox gene is expressed in early precursors of the eye and
RT activates retina-specific genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10643-10648(1998).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Eye;
RX PubMed=10473118; DOI=10.1016/s0925-4773(99)00068-4;
RA Jean D., Bernier G., Gruss P.;
RT "Six6 (Optx2) is a novel murine Six3-related homeobox gene that demarcates
RT the presumptive pituitary/hypothalamic axis and the ventral optic stalk.";
RL Mech. Dev. 84:31-40(1999).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Embryonic head;
RX PubMed=10381575; DOI=10.1016/s0925-4773(99)00017-9;
RA Lopez-Rios J., Gallardo E., Rodriguez de Cordoba S., Bovolenta P.;
RT "Six9 (Optx2), a new member of the Six gene family of transcription
RT factors, is expressed at early stages of vertebrate ocular and pituitary
RT development.";
RL Mech. Dev. 83:155-159(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP INTERACTION WITH TLE5 AND TLE4.
RX PubMed=12050133; DOI=10.1242/dev.129.12.2835;
RA Zhu C.C., Dyer M.A., Uchikawa M., Kondoh H., Lagutin O.V., Oliver G.;
RT "Six3-mediated auto repression and eye development requires its interaction
RT with members of the Groucho-related family of co-repressors.";
RL Development 129:2835-2849(2002).
CC -!- FUNCTION: May be involved in eye development.
CC {ECO:0000303|PubMed:10381575, ECO:0000303|PubMed:10473118,
CC ECO:0000303|PubMed:9724757}.
CC -!- SUBUNIT: Interacts with TLE4 and TLE5. {ECO:0000269|PubMed:12050133}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
CC -!- TISSUE SPECIFICITY: In the developing embryo, expressed mainly in the
CC ventral optic stalk, optic chiasma, the neural retina and the
CC primordial tissues that give rise to the pituitary/hypothalamus axis.
CC Not expressed in the lens placode. {ECO:0000269|PubMed:10381575,
CC ECO:0000269|PubMed:10473118}.
CC -!- DEVELOPMENTAL STAGE: Expression is first detected in the embryo at 8
CC dpc. {ECO:0000269|PubMed:10381575}.
CC -!- SIMILARITY: Belongs to the SIX/Sine oculis homeobox family.
CC {ECO:0000305}.
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DR EMBL; AF050130; AAC33850.1; -; mRNA.
DR EMBL; AF135267; AAD48911.1; -; mRNA.
DR EMBL; AJ011787; CAA09775.1; -; mRNA.
DR EMBL; AK017544; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK029309; BAC26387.1; -; mRNA.
DR CCDS; CCDS25972.1; -.
DR RefSeq; NP_035514.1; NM_011384.5.
DR AlphaFoldDB; Q9QZ28; -.
DR SMR; Q9QZ28; -.
DR BioGRID; 203264; 5.
DR IntAct; Q9QZ28; 5.
DR STRING; 10090.ENSMUSP00000021519; -.
DR PhosphoSitePlus; Q9QZ28; -.
DR PaxDb; Q9QZ28; -.
DR PRIDE; Q9QZ28; -.
DR ProteomicsDB; 261050; -.
DR Antibodypedia; 40; 166 antibodies from 29 providers.
DR DNASU; 20476; -.
DR Ensembl; ENSMUST00000021519; ENSMUSP00000021519; ENSMUSG00000021099.
DR GeneID; 20476; -.
DR KEGG; mmu:20476; -.
DR UCSC; uc007nvy.1; mouse.
DR CTD; 4990; -.
DR MGI; MGI:1341840; Six6.
DR VEuPathDB; HostDB:ENSMUSG00000021099; -.
DR eggNOG; KOG0775; Eukaryota.
DR GeneTree; ENSGT00940000160091; -.
DR HOGENOM; CLU_046914_0_1_1; -.
DR InParanoid; Q9QZ28; -.
DR OMA; GTPEMLG; -.
DR OrthoDB; 1197104at2759; -.
DR PhylomeDB; Q9QZ28; -.
DR TreeFam; TF315545; -.
DR BioGRID-ORCS; 20476; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Six6; mouse.
DR PRO; PR:Q9QZ28; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9QZ28; protein.
DR Bgee; ENSMUSG00000021099; Expressed in optic fissure and 65 other tissues.
DR ExpressionAtlas; Q9QZ28; baseline and differential.
DR Genevisible; Q9QZ28; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
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; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0001654; P:eye development; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR031701; SIX1_SD.
DR InterPro; IPR032947; SIX6.
DR PANTHER; PTHR10390:SF12; PTHR10390:SF12; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF16878; SIX1_SD; 1.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 1: Evidence at protein level;
KW Developmental protein; DNA-binding; Homeobox; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..246
FT /note="Homeobox protein SIX6"
FT /id="PRO_0000049308"
FT DNA_BIND 126..186
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 190..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 212
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95475"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95475"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95475"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95475"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95475"
FT CONFLICT 141
FT /note="H -> N (in Ref. 3; CAA09775)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="S -> T (in Ref. 3; CAA09775)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 246 AA; 27741 MW; F1332D5E617B2CF1 CRC64;
MFQLPILNFS PQQVAGVCET LEESGDVERL GRFLWSLPVA PAACEALNKN ESVLRARAIV
AFHGGNYREL YHILENHKFT KESHAKLQAL WLEAHYQEAE KLRGRPLGPV DKYRVRKKFP
LPRTIWDGEQ KTHCFKERTR HLLREWYLQD PYPNPSKKRE LAQATGLTPT QVGNWFKNRR
QRDRAAAAKN RLQQQVLSQG PGRVLRSEGE GTPEVLGVAS SPAASLSSKA ATSAISITSS
DSECDI
