ID   VSX1_MOUSE              Reviewed;         363 AA.
AC   Q91V10;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 161.
DE   RecName: Full=Visual system homeobox 1;
DE   AltName: Full=Homeodomain protein RINX;
DE   AltName: Full=Retinal inner nuclear layer homeobox protein;
DE   AltName: Full=Transcription factor VSX1;
GN   Name=Vsx1; Synonyms=Rinx;
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].
RC   STRAIN=BALB/cJ; TISSUE=Retina;
RX   PubMed=11731243; DOI=10.1016/s0925-4773(01)00585-8;
RA   Chow R.L., Snow B., Novak J., Looser J., Freund C., Vidgen D., Ploder L.,
RA   McInnes R.R.;
RT   "Vsx1, a rapidly evolving paired-like homeobox gene expressed in cone
RT   bipolar cells.";
RL   Mech. Dev. 109:315-322(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=SWR/J;
RX   PubMed=11485319; DOI=10.1006/bbrc.2001.5372;
RA   Ohtoshi A., Justice M.J., Behringer R.R.;
RT   "Isolation and characterization of Vsx1, a novel mouse CVC paired-like
RT   homeobox gene expressed during embryogenesis and in the retina.";
RL   Biochem. Biophys. Res. Commun. 286:133-140(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE, AND TISSUE SPECIFICITY.
RC   STRAIN=129/SvJ;
RX   PubMed=15838724; DOI=10.1007/s10384-004-0162-z;
RA   Hayashi T., Huang J., Deeb S.S.;
RT   "Expression of rinx/vsx1 during postnatal eye development in cone-bipolar,
RT   differentiating ganglion, and lens fiber cells.";
RL   Jpn. J. Ophthalmol. 49:93-105(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
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   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=17919464; DOI=10.1016/j.brainres.2007.06.007;
RA   Clark A.M., Yun S., Veien E.S., Wu Y.Y., Chow R.L., Dorsky R.I.,
RA   Levine E.M.;
RT   "Negative regulation of Vsx1 by its paralog Chx10/Vsx2 is conserved in the
RT   vertebrate retina.";
RL   Brain Res. 1192:99-113(2008).
CC   -!- FUNCTION: Binds to the 37-bp core of the locus control region (LCR) of
CC       the red/green visual pigment gene cluster (By similarity). May regulate
CC       the activity of the LCR and the cone opsin genes at earlier stages of
CC       development (By similarity). Dispensable in early retinal development
CC       (PubMed:17919464). {ECO:0000250|UniProtKB:Q9NZR4,
CC       ECO:0000269|PubMed:17919464}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17919464}.
CC   -!- TISSUE SPECIFICITY: Expressed in the postnatal retina (at protein
CC       level) (PubMed:17919464). In the adult, expressed exclusively in the
CC       cells of the neural retina with expression restricted to postnatal cone
CC       bipolar interneurons (PubMed:15838724). {ECO:0000269|PubMed:15838724,
CC       ECO:0000269|PubMed:17919464}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at P5, solely within the inner nuclear
CC       layer (INL) of the central neuroretina. By days P6 and P7, expression
CC       expands peripherally during neurogenesis. By P12, expression is
CC       restricted to the outer margin of the INL and reaches the outer
CC       periphery of the neuroretina.
CC   -!- DISRUPTION PHENOTYPE: At embryonic day 14.5 ocular morphology is normal
CC       as is expression and localization of retinal transcription and cell
CC       cycle regulatory proteins. {ECO:0000269|PubMed:17919464}.
CC   -!- SIMILARITY: Belongs to the paired homeobox family. {ECO:0000305}.
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DR   EMBL; AY056825; AAL11431.1; -; mRNA.
DR   EMBL; AF395732; AAL08947.1; -; mRNA.
DR   EMBL; AF391757; AAL09584.1; -; Genomic_DNA.
DR   EMBL; AF391758; AAL09585.1; -; mRNA.
DR   EMBL; BC057647; AAH57647.1; -; mRNA.
DR   CCDS; CCDS16860.1; -.
DR   PIR; JC7750; JC7750.
DR   RefSeq; NP_473409.1; NM_054068.2.
DR   AlphaFoldDB; Q91V10; -.
DR   SMR; Q91V10; -.
DR   BioGRID; 227900; 1.
DR   IntAct; Q91V10; 1.
DR   STRING; 10090.ENSMUSP00000039088; -.
DR   PhosphoSitePlus; Q91V10; -.
DR   PaxDb; 10090-ENSMUSP00000039088; -.
DR   ProteomicsDB; 297826; -.
DR   Antibodypedia; 9932; 177 antibodies from 23 providers.
DR   DNASU; 114889; -.
DR   Ensembl; ENSMUST00000046095.10; ENSMUSP00000039088.9; ENSMUSG00000033080.10.
DR   GeneID; 114889; -.
DR   KEGG; mmu:114889; -.
DR   UCSC; uc008muh.2; mouse.
DR   AGR; MGI:1890816; -.
DR   CTD; 30813; -.
DR   MGI; MGI:1890816; Vsx1.
DR   VEuPathDB; HostDB:ENSMUSG00000033080; -.
DR   eggNOG; KOG0494; Eukaryota.
DR   GeneTree; ENSGT00940000160793; -.
DR   HOGENOM; CLU_049243_1_0_1; -.
DR   InParanoid; Q91V10; -.
DR   OMA; WGSDHLK; -.
DR   OrthoDB; 2881066at2759; -.
DR   PhylomeDB; Q91V10; -.
DR   TreeFam; TF350743; -.
DR   BioGRID-ORCS; 114889; 6 hits in 77 CRISPR screens.
DR   PRO; PR:Q91V10; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q91V10; Protein.
DR   Bgee; ENSMUSG00000033080; Expressed in retinal neural layer and 10 other cell types or tissues.
DR   ExpressionAtlas; Q91V10; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
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; ISO:MGI.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR   GO; GO:0048666; P:neuron development; IMP:MGI.
DR   GO; GO:0042551; P:neuron maturation; IGI:MGI.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0060040; P:retinal bipolar neuron differentiation; IMP:MGI.
DR   GO; GO:0007601; P:visual perception; IMP:MGI.
DR   CDD; cd00086; homeodomain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   InterPro; IPR023339; CVC.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   PANTHER; PTHR24323; CEH-10 HOMEODOMAIN-CONTAINING HOMOLOG; 1.
DR   PANTHER; PTHR24323:SF3; VISUAL SYSTEM HOMEOBOX 1; 1.
DR   Pfam; PF00046; Homeodomain; 1.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   PROSITE; PS51496; CVC; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   Genevisible; Q91V10; MM.
PE   1: Evidence at protein level;
KW   Developmental protein; DNA-binding; Homeobox; Nucleus; Reference proteome;
KW   Sensory transduction; Transcription; Transcription regulation; Vision.
FT   CHAIN           1..363
FT                   /note="Visual system homeobox 1"
FT                   /id="PRO_0000049356"
FT   DOMAIN          231..283
FT                   /note="CVC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00829"
FT   DNA_BIND        171..230
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          42..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           31..38
FT                   /note="Octapeptide motif"
FT   MOTIF           168..173
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        150..165
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..318
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   363 AA;  38755 MW;  E250D452C77228C2 CRC64;
     MTGRDGLSDA RSRSRALAPG CPPTGSRLRS FAINDLLGLE ADLPTPAEPG LRSNSGDPAE
     AIGSGPGPGP GLCGSCPARG ALPLGLGLLC GFGAQPPSAA AAARARCLLL ADLRLLPSAG
     PEPAVAQGPV HPPPALGSQQ RSESVSTSDG DSPSEEKNDP KMSLILGKRK KRRHRTVFTA
     HQLEELEKAF GEAHYPDVYA REMLAAKTEL PEDRIQVWFQ NRRAKWRKRE KRWGGSSVMA
     EYGLYGAMVR HCIPLPDSVL NSADSLQGSC APWLLGMHKK STGMRKPESE DKLAGLWEFD
     HLKKGANKDE DGPERGPDET TQNPENSLED VAIDLSSSSR QETKKMPPGS STQLPQPPQV
     GAS
//