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Database: UniProt
Entry: PITX3_DANRE
LinkDB: PITX3_DANRE
Original site: PITX3_DANRE 
ID   PITX3_DANRE             Reviewed;         293 AA.
AC   Q6QU75; Q6DUF5;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=Pituitary homeobox 3 {ECO:0000250|UniProtKB:O35160};
DE   AltName: Full=Bicoid-like homeodomain transcription factor Pitx3 {ECO:0000312|EMBL:AAT72155.1};
DE   AltName: Full=Homeobox protein PITX3;
DE   AltName: Full=Paired-like homeodomain transcription factor 3 {ECO:0000312|EMBL:AAR98874.1};
GN   Name=pitx3 {ECO:0000312|ZFIN:ZDB-GENE-041229-4}; ORFNames=si:dkey-196H17.1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAR98874.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   TISSUE=Embryo {ECO:0000269|PubMed:15728669};
RX   PubMed=15728669; DOI=10.1242/dev.01723;
RA   Dutta S., Dietrich J.E., Aspock G., Burdine R.D., Schier A.,
RA   Westerfield M., Varga Z.M.;
RT   "pitx3 defines an equivalence domain for lens and anterior pituitary
RT   placode.";
RL   Development 132:1579-1590(2005).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAT72155.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Eye {ECO:0000269|PubMed:15804565};
RX   PubMed=15804565; DOI=10.1016/j.mod.2004.11.012;
RA   Shi X., Bosenko D.V., Zinkevich N.S., Foley S., Hyde D.R., Semina E.V.,
RA   Vihtelic T.S.;
RT   "Zebrafish pitx3 is necessary for normal lens and retinal development.";
RL   Mech. Dev. 122:513-527(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [4] {ECO:0000312|EMBL:CAX12174.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye {ECO:0000312|EMBL:AAH94961.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000305}
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo {ECO:0000269|PubMed:18053265};
RX   PubMed=18053265; DOI=10.1186/1471-213x-7-135;
RA   Filippi A., Durr K., Ryu S., Willaredt M., Holzschuh J., Driever W.;
RT   "Expression and function of nr4a2, lmx1b, and pitx3 in zebrafish
RT   dopaminergic and noradrenergic neuronal development.";
RL   BMC Dev. Biol. 7:135-135(2007).
CC   -!- FUNCTION: Transcriptional regulator which may play a role in the
CC       differentiation and maintenance of meso-diencephalic dopaminergic
CC       (mdDA) neurons (By similarity). Required for lens and retinal
CC       development and for pituitary pre-placode formation and cell
CC       specification. {ECO:0000250, ECO:0000269|PubMed:15728669,
CC       ECO:0000269|PubMed:15804565, ECO:0000269|PubMed:18053265}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O35160,
CC       ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-
CC       ProRule:PRU00138}.
CC   -!- TISSUE SPECIFICITY: In the adult, high levels detected in the eye and
CC       much lower levels in internal organs such as liver, gastrointestinal
CC       system, heart, genitourinary system and pancreas.
CC       {ECO:0000269|PubMed:15728669, ECO:0000269|PubMed:15804565,
CC       ECO:0000269|PubMed:18053265}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout development with low levels
CC       detected from 3-8 hpf and highest levels in developing brain and lens
CC       at 24 hpf. In the embryo, expressed in anterior neural plate and later
CC       in lens and pituitary cells. Detected in the forebrain, lens and
CC       pectoral fin buds at 24 hpf. Becomes restricted to the lens equatorial
CC       region by 48 hpf. Strongest expression detected in the diencephalon and
CC       pituitary at 48 hpf. Evident in the cartilage surrounding the mouth at
CC       72 hpf, appearing in the iris of the eye, developing lower jaw and the
CC       branchial arches at 96 hpf and extending to developing musculature
CC       along the trunk. During lens development, exhibits widespread
CC       expression during the primary differentiation phase of lens formation
CC       and then restricted to the region of secondary fiber cell
CC       differentiation during the phase of lens growth. Expressed in both
CC       proliferating and early differentiating progenitor cells of the
CC       posterior tuberculum. {ECO:0000269|PubMed:15728669,
CC       ECO:0000269|PubMed:15804565, ECO:0000269|PubMed:18053265}.
CC   -!- SIMILARITY: Belongs to the paired homeobox family. Bicoid subfamily.
CC       {ECO:0000255}.
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DR   EMBL; AY525643; AAR98874.1; -; mRNA.
DR   EMBL; AY639155; AAT72155.1; -; mRNA.
DR   EMBL; AY643793; AAT68296.1; -; Genomic_DNA.
DR   EMBL; CR626878; CAX12174.1; -; Genomic_DNA.
DR   EMBL; BC094961; AAH94961.1; -; mRNA.
DR   RefSeq; NP_991238.1; NM_205675.2.
DR   AlphaFoldDB; Q6QU75; -.
DR   SMR; Q6QU75; -.
DR   STRING; 7955.ENSDARP00000093314; -.
DR   PaxDb; 7955-ENSDARP00000093314; -.
DR   GeneID; 402974; -.
DR   KEGG; dre:402974; -.
DR   AGR; ZFIN:ZDB-GENE-041229-4; -.
DR   CTD; 5309; -.
DR   ZFIN; ZDB-GENE-041229-4; pitx3.
DR   eggNOG; KOG0486; Eukaryota.
DR   HOGENOM; CLU_030301_0_0_1; -.
DR   InParanoid; Q6QU75; -.
DR   OMA; HESGCKG; -.
DR   OrthoDB; 5395268at2759; -.
DR   PhylomeDB; Q6QU75; -.
DR   TreeFam; TF351940; -.
DR   PRO; PR:Q6QU75; -.
DR   Proteomes; UP000000437; Chromosome 13.
DR   Bgee; ENSDARG00000070069; Expressed in adenohypophyseal placode and 45 other cell types or tissues.
DR   ExpressionAtlas; Q6QU75; baseline.
DR   GO; GO:0005634; C:nucleus; 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; IBA:GO_Central.
DR   GO; GO:0021984; P:adenohypophysis development; IMP:ZFIN.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR   GO; GO:0043010; P:camera-type eye development; IMP:ZFIN.
DR   GO; GO:0035270; P:endocrine system development; IMP:ZFIN.
DR   GO; GO:0002088; P:lens development in camera-type eye; IMP:ZFIN.
DR   GO; GO:0070306; P:lens fiber cell differentiation; IMP:ZFIN.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:ZFIN.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; IPR016233; Homeobox_Pitx/unc30.
DR   InterPro; IPR003654; OAR_dom.
DR   PANTHER; PTHR45882:SF2; PITUITARY HOMEOBOX 3; 1.
DR   PANTHER; PTHR45882; PITUITARY HOMEOBOX HOMOLOG PTX1; 1.
DR   Pfam; PF00046; Homeodomain; 1.
DR   Pfam; PF03826; OAR; 1.
DR   PIRSF; PIRSF000563; Homeobox_protein_Pitx/Unc30; 1.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS50803; OAR; 1.
PE   2: Evidence at transcript level;
KW   Activator; Developmental protein; DNA-binding; Homeobox; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..293
FT                   /note="Pituitary homeobox 3"
FT                   /id="PRO_0000407846"
FT   DNA_BIND        60..119
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           255..268
FT                   /note="OAR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00138"
FT   MOTIF           260..264
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:O35160"
FT   COMPBIAS        10..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        108
FT                   /note="F -> V (in Ref. 2; AAT68296)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        118
FT                   /note="R -> L (in Ref. 2; AAT68296)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        169
FT                   /note="F -> Y (in Ref. 2; AAT68296)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        189
FT                   /note="P -> A (in Ref. 2; AAT68296)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        204
FT                   /note="S -> L (in Ref. 2; AAT68296)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        221
FT                   /note="N -> S (in Ref. 2; AAT68296)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        224
FT                   /note="N -> D (in Ref. 2; AAT68296)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   293 AA;  32438 MW;  18F022FB832FBA93 CRC64;
     MDFNLLTDSE ARSPALSLSD SGTPQHDPGC KGQDNSDTEK SHQNHTDESN PEDGSLKKKQ
     RRQRTHFTSQ QLQELEATFQ RNRYPDMSTR EEIAVWTNLT EARVRVWFKN RRAKWRKRER
     NQQAELCKNG FGAQFNGLMQ PYDDMYSGYS YNNWATKSLA SSPLSAKSFP FFNSMNVSPL
     SSQPMFSPPS SIPSMNMASS MVPSAVAGVP GSGLNNLGNL NNLNSPTLNS AAVSAAACPY
     ATTAGPYMYR DTCNSSLASL RLKAKQHANF AYPAVQNPVS NLSPCQYAVD RPV
//
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