VSX1_XENLA
ID VSX1_XENLA Reviewed; 344 AA.
AC Q0P031;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Visual system homeobox 1;
DE AltName: Full=Transcription factor vsx1;
DE AltName: Full=Xvsx1;
GN Name=vsx1 {ECO:0000303|PubMed:17103185};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABC54559.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo {ECO:0000269|PubMed:17103185};
RX PubMed=17103185; DOI=10.1007/s00427-006-0109-0;
RA D'Autilia S., Decembrini S., Casarosa S., He R.-Q., Barsacchi G.,
RA Cremisi F., Andreazzoli M.;
RT "Cloning and developmental expression of the Xenopus homeobox gene Xvsx1.";
RL Dev. Genes Evol. 216:829-834(2006).
RN [2] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16903786; DOI=10.1371/journal.pbio.0040272;
RA Decembrini S., Andreazzoli M., Vignali R., Barsacchi G., Cremisi F.;
RT "Timing the generation of distinct retinal cells by homeobox proteins.";
RL PLoS Biol. 4:1562-1571(2006).
CC -!- FUNCTION: Involved in the differentiation of bipolar cells, the last
CC neurons of the retina to form. Together with other retinal homeobox
CC proteins, acts as an effector of a cellular clock which, depending on
CC cell cycle progression, establishes the generation of distinct retinal
CC neuronal cell types. {ECO:0000269|PubMed:16903786}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O42250}.
CC -!- TISSUE SPECIFICITY: Initially transcribed but not translated in early
CC neural (stage 15) retinal progenitors. Translation occurs during late
CC retinogenesis and requires cell cycle progression with the timing of
CC translation paralleling that of the generation of bipolar cells. Also
CC expressed in the ciliary marginal zone (CMZ) with translation beginning
CC in early postmitotic cells. Also transcribed in early neurulae in the
CC presumptive spinal cord, with expression expanding anteriorly to the
CC midbrain-hindbrain boundary during the tail bud stage.
CC {ECO:0000269|PubMed:16903786, ECO:0000269|PubMed:17103185}.
CC -!- DEVELOPMENTAL STAGE: First transcribed in the neurula at stage 15 and
CC is maintained throughout later stages, reaching a peak around stage 42.
CC {ECO:0000269|PubMed:16903786, ECO:0000269|PubMed:17103185}.
CC -!- SIMILARITY: Belongs to the paired homeobox family. {ECO:0000255}.
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DR EMBL; DQ324366; ABC54559.1; -; mRNA.
DR RefSeq; NP_001090191.1; NM_001096722.1.
DR AlphaFoldDB; Q0P031; -.
DR SMR; Q0P031; -.
DR GeneID; 779073; -.
DR KEGG; xla:779073; -.
DR CTD; 779073; -.
DR Xenbase; XB-GENE-866467; vsx1.L.
DR OrthoDB; 1348807at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 779073; Expressed in camera-type eye and 4 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0060040; P:retinal bipolar neuron differentiation; IEP:UniProtKB.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR023339; CVC.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR Pfam; PF00046; Homeodomain; 1.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51496; CVC; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Differentiation; DNA-binding; Homeobox; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..344
FT /note="Visual system homeobox 1"
FT /id="PRO_0000283817"
FT DOMAIN 210..263
FT /note="CVC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00829"
FT DNA_BIND 150..209
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..46
FT /note="Octapeptide motif"
FT /evidence="ECO:0000255"
FT REGION 111..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 146..150
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 113..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 344 AA; 38213 MW; 3AA0CCBB4F048D5D CRC64;
MTGRDDISEA KSKGKILAPS VGNEKSGRLH GPAMRSKGFA ITDLLGLEAE LQPPSISLPN
CEGPGVSLGG VSLTNGSLPL GLGFLCGFAS QQPPGTTCLL PTHIPFLQPR PDHHYLHTSD
KHKENISDDD SILGDKNDLK ASSAQSKRKK RRHRTVFTAH QLDELEKSFN EAHYPDVYAR
EMLALKTELP EDRIQVWFQN RRAKWRKREK CWGRSSVMAE YGLYGAMVRH SIPLPESIIN
SAKNGLVGSC APWLLGMHKK SVDITSKVDA DDLVTERSRG ESQVRDFTNP HSESHRSPRH
HSHSMDISEE RAIDLSSTAK QENQSSGRHN SIRDSQSDFT DSDH
