GenomeNet

Database: UniProt
Entry: Q9IAL2
LinkDB: Q9IAL2
Original site: Q9IAL2 
ID   VSX1_CHICK              Reviewed;         350 AA.
AC   Q9IAL2;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 119.
DE   RecName: Full=Visual system homeobox 1;
DE   AltName: Full=Homeobox protein Chx10-1;
DE   AltName: Full=Transcription factor VSX1;
GN   Name=VSX1; Synonyms=CHX10-1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10640715; DOI=10.1016/s0925-4773(99)00251-8;
RA   Chen C.-M.A., Cepko C.L.;
RT   "Expression of Chx10 and Chx10-1 in the developing chicken retina.";
RL   Mech. Dev. 90:293-297(2000).
CC   -!- FUNCTION: Binds to the 37-bp core of the locus control region (LCR) of
CC       the red/green visual pigment gene cluster. May regulate the activity of
CC       the LCR and the cone opsin genes at earlier stages of development (By
CC       similarity). Dispensable in early retinal development (By similarity).
CC       {ECO:0000250|UniProtKB:Q91V10}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q91V10}.
CC   -!- TISSUE SPECIFICITY: Restricted to bipolar cells of the retina and
CC       spinal cord.
CC   -!- DEVELOPMENTAL STAGE: At stage 12, expressed throughout the invaginating
CC       optic vesicles and a subset of cells in the ventral spinal cord,
CC       presumably interneuron precursors. At stage 14, when the optic cup
CC       forms, expression is restricted to a subset of retinoblasts. At stage
CC       15, expression along the ventral spinal and hindbrain intensifies and
CC       persists beyond stage 20.
CC   -!- SIMILARITY: Belongs to the paired homeobox family. {ECO:0000305}.
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DR   EMBL; AF178670; AAF40312.1; -; mRNA.
DR   RefSeq; NP_990100.1; NM_204769.1.
DR   AlphaFoldDB; Q9IAL2; -.
DR   SMR; Q9IAL2; -.
DR   STRING; 9031.ENSGALP00000055813; -.
DR   PaxDb; 9031-ENSGALP00000043363; -.
DR   GeneID; 395537; -.
DR   KEGG; gga:395537; -.
DR   CTD; 30813; -.
DR   VEuPathDB; HostDB:geneid_395537; -.
DR   eggNOG; KOG0494; Eukaryota.
DR   InParanoid; Q9IAL2; -.
DR   PhylomeDB; Q9IAL2; -.
DR   PRO; PR:Q9IAL2; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR   GO; GO:0048666; P:neuron development; IBA:GO_Central.
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:0007601; P:visual perception; IEA:UniProtKB-KW.
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.
PE   2: Evidence at transcript level;
KW   Developmental protein; DNA-binding; Homeobox; Nucleus; Reference proteome;
KW   Sensory transduction; Transcription; Transcription regulation; Vision.
FT   CHAIN           1..350
FT                   /note="Visual system homeobox 1"
FT                   /id="PRO_0000049357"
FT   DOMAIN          217..270
FT                   /note="CVC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00829"
FT   DNA_BIND        157..216
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          27..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          112..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           52..59
FT                   /note="Octapeptide motif"
FT   COMPBIAS        112..126
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..287
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..307
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..330
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   350 AA;  37351 MW;  A60B738021703C33 CRC64;
     MPGRADPSGG RAAVPVPLPV AVAAAPSPAS VRSALPERSA RPGGAGLRAK GFAITDLLGL
     EAELQPPPGA APGPAGGYEG GGALGLGLGL LCGLAGPGAP CLLPAPLPLL PARGPRPGPP
     GPPPAARRHK ESASDEDSLS GDASELKMPA SQIKRKKRRH RTVFTAHQLE ELEKAFNEAH
     YPDVYAREML AVKTELPEDR IQVWFQNRRA KWRKREKCWG RSSVMAEYGL YGAMVRHSIP
     LPESIINSAK SGLVGSCAPW LLGMHKKSME VSRKAESQEK PADGWQAEQD GEELQGKQAS
     SQRSSEKLGP AKDPEDTAID LSRTAKQEKR SVLRQCVNGD PTTEQKDRDH
//
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