ID   PROX1_HUMAN             Reviewed;         737 AA.
AC   Q92786; A6NK29; A8K2B1; Q5SW76; Q8TB91;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 2.
DT   24-JAN-2024, entry version 189.
DE   RecName: Full=Prospero homeobox protein 1;
DE   AltName: Full=Homeobox prospero-like protein PROX1;
DE            Short=PROX-1;
GN   Name=PROX1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Embryonic brain;
RX   PubMed=8812486; DOI=10.1006/geno.1996.0392;
RA   Zinovieva R.D., Duncan M.K., Johnson T.R., Torres R., Polymeropoulos M.H.,
RA   Tomarev S.I.;
RT   "Structure and chromosomal localization of the human homeobox gene Prox
RT   1.";
RL   Genomics 35:517-522(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Muscle;
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   [6]
RP   REVIEW.
RX   PubMed=22733308; DOI=10.1007/s10555-012-9390-8;
RA   Elsir T., Smits A., Lindstroem M.S., Nister M.;
RT   "Transcription factor PROX1: its role in development and cancer.";
RL   Cancer Metastasis Rev. 31:793-805(2012).
RN   [7]
RP   FUNCTION.
RX   PubMed=23723244; DOI=10.1093/nar/gkt447;
RA   Takeda Y., Jetten A.M.;
RT   "Prospero-related homeobox 1 (Prox1) functions as a novel modulator of
RT   retinoic acid-related orphan receptors alpha- and gamma-mediated
RT   transactivation.";
RL   Nucleic Acids Res. 41:6992-7008(2013).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-199; SER-295 AND
RP   SER-557, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [9]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-324, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "System-wide analysis of SUMOylation dynamics in response to replication
RT   stress reveals novel small ubiquitin-like modified target proteins and
RT   acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [10]
RP   STRUCTURE BY NMR OF 575-737.
RX   PubMed=22733734; DOI=10.1073/pnas.1203013109;
RA   Lange O.F., Rossi P., Sgourakis N.G., Song Y., Lee H.W., Aramini J.M.,
RA   Ertekin A., Xiao R., Acton T.B., Montelione G.T., Baker D.;
RT   "Determination of solution structures of proteins up to 40 kDa using CS-
RT   Rosetta with sparse NMR data from deuterated samples.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:10873-10878(2012).
CC   -!- FUNCTION: Transcription factor involved in developmental processes such
CC       as cell fate determination, gene transcriptional regulation and
CC       progenitor cell regulation in a number of organs. Plays a critical role
CC       in embryonic development and functions as a key regulatory protein in
CC       neurogenesis and the development of the heart, eye lens, liver,
CC       pancreas and the lymphatic system. Involved in the regulation of the
CC       circadian rhythm. Represses: transcription of the retinoid-related
CC       orphan receptor RORG, transcriptional activator activity of RORA and
CC       RORG and the expression of RORA/G-target genes including core clock
CC       components: BMAL1, NPAS2 and CRY1 and metabolic genes: AVPR1A and
CC       ELOVL3. {ECO:0000269|PubMed:23723244, ECO:0000303|PubMed:22733308}.
CC   -!- SUBUNIT: Interacts with RORA and RORG (via AF-2 motif).
CC       {ECO:0000250|UniProtKB:P48437}.
CC   -!- INTERACTION:
CC       Q92786; P56545: CTBP2; NbExp=2; IntAct=EBI-3912635, EBI-741533;
CC       Q92786; P20823: HNF1A; NbExp=3; IntAct=EBI-3912635, EBI-636034;
CC       Q92786; P41235: HNF4A; NbExp=3; IntAct=EBI-3912635, EBI-1049011;
CC       Q92786; O00482-2: NR5A2; NbExp=9; IntAct=EBI-3912635, EBI-9257474;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P48437}. Note=RORG
CC       promotes its nuclear localization. {ECO:0000250|UniProtKB:P48437}.
CC   -!- TISSUE SPECIFICITY: Most actively expressed in the developing lens.
CC       Detected also in embryonic brain, lung, liver and kidney. In adult, it
CC       is more abundant in heart and liver than in brain, skeletal muscle,
CC       kidney and pancreas. {ECO:0000269|PubMed:8812486}.
CC   -!- DOMAIN: The Prospero-type homeodomain and the adjacent Prospero domain
CC       act as a single structural unit, the Homeo-Prospero domain. The
CC       Prospero-type homeodomain is essential for repression of RORG
CC       transcriptional activator activity. {ECO:0000250|UniProtKB:P48437,
CC       ECO:0000255|PROSITE-ProRule:PRU01162}.
CC   -!- SIMILARITY: Belongs to the Prospero homeodomain family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01162}.
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DR   EMBL; U44060; AAC50656.1; -; mRNA.
DR   EMBL; AK290176; BAF82865.1; -; mRNA.
DR   EMBL; AC011700; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL606537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471100; EAW93360.1; -; Genomic_DNA.
DR   EMBL; BC024201; AAH24201.1; -; mRNA.
DR   CCDS; CCDS31021.1; -.
DR   RefSeq; NP_001257545.1; NM_001270616.1.
DR   RefSeq; NP_002754.2; NM_002763.4.
DR   RefSeq; XP_016857322.1; XM_017001833.1.
DR   PDB; 2LMD; NMR; -; A=575-737.
DR   PDBsum; 2LMD; -.
DR   AlphaFoldDB; Q92786; -.
DR   BMRB; Q92786; -.
DR   SMR; Q92786; -.
DR   BioGRID; 111613; 33.
DR   IntAct; Q92786; 15.
DR   MINT; Q92786; -.
DR   STRING; 9606.ENSP00000355925; -.
DR   iPTMnet; Q92786; -.
DR   PhosphoSitePlus; Q92786; -.
DR   BioMuta; PROX1; -.
DR   DMDM; 85702224; -.
DR   jPOST; Q92786; -.
DR   MassIVE; Q92786; -.
DR   MaxQB; Q92786; -.
DR   PaxDb; 9606-ENSP00000355925; -.
DR   PeptideAtlas; Q92786; -.
DR   ProteomicsDB; 75470; -.
DR   Pumba; Q92786; -.
DR   Antibodypedia; 34616; 717 antibodies from 44 providers.
DR   DNASU; 5629; -.
DR   Ensembl; ENST00000366958.9; ENSP00000355925.4; ENSG00000117707.17.
DR   Ensembl; ENST00000435016.2; ENSP00000400694.1; ENSG00000117707.17.
DR   GeneID; 5629; -.
DR   KEGG; hsa:5629; -.
DR   MANE-Select; ENST00000366958.9; ENSP00000355925.4; NM_001270616.2; NP_001257545.1.
DR   UCSC; uc001hkg.3; human.
DR   AGR; HGNC:9459; -.
DR   CTD; 5629; -.
DR   DisGeNET; 5629; -.
DR   GeneCards; PROX1; -.
DR   HGNC; HGNC:9459; PROX1.
DR   HPA; ENSG00000117707; Tissue enriched (liver).
DR   MIM; 601546; gene.
DR   neXtProt; NX_Q92786; -.
DR   OpenTargets; ENSG00000117707; -.
DR   PharmGKB; PA33812; -.
DR   VEuPathDB; HostDB:ENSG00000117707; -.
DR   eggNOG; KOG3779; Eukaryota.
DR   GeneTree; ENSGT00940000154790; -.
DR   HOGENOM; CLU_016051_0_0_1; -.
DR   InParanoid; Q92786; -.
DR   OMA; NGDNHNF; -.
DR   OrthoDB; 2877587at2759; -.
DR   PhylomeDB; Q92786; -.
DR   TreeFam; TF316638; -.
DR   PathwayCommons; Q92786; -.
DR   SignaLink; Q92786; -.
DR   SIGNOR; Q92786; -.
DR   BioGRID-ORCS; 5629; 23 hits in 1186 CRISPR screens.
DR   ChiTaRS; PROX1; human.
DR   GeneWiki; PROX1; -.
DR   GenomeRNAi; 5629; -.
DR   Pharos; Q92786; Tbio.
DR   PRO; PR:Q92786; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q92786; Protein.
DR   Bgee; ENSG00000117707; Expressed in sural nerve and 159 other cell types or tissues.
DR   ExpressionAtlas; Q92786; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0003677; F:DNA binding; IMP:BHF-UCL.
DR   GO; GO:0050692; F:DNA binding domain binding; IPI:BHF-UCL.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IC:BHF-UCL.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:BHF-UCL.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR   GO; GO:0050693; F:LBD domain binding; IPI:BHF-UCL.
DR   GO; GO:0016922; F:nuclear receptor binding; IPI:BHF-UCL.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR   GO; GO:0090425; P:acinar cell differentiation; IEA:Ensembl.
DR   GO; GO:0060414; P:aorta smooth muscle tissue morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0055009; P:atrial cardiac muscle tissue morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0060837; P:blood vessel endothelial cell differentiation; IEA:Ensembl.
DR   GO; GO:0007420; P:brain development; IEP:BHF-UCL.
DR   GO; GO:0061114; P:branching involved in pancreas morphogenesis; IEA:Ensembl.
DR   GO; GO:0021707; P:cerebellar granule cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR   GO; GO:0021542; P:dentate gyrus development; ISS:BHF-UCL.
DR   GO; GO:0021516; P:dorsal spinal cord development; ISS:BHF-UCL.
DR   GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IEP:BHF-UCL.
DR   GO; GO:0060214; P:endocardium formation; ISS:BHF-UCL.
DR   GO; GO:0010631; P:epithelial cell migration; IEA:Ensembl.
DR   GO; GO:0002194; P:hepatocyte cell migration; IEA:Ensembl.
DR   GO; GO:0070365; P:hepatocyte differentiation; IEP:BHF-UCL.
DR   GO; GO:0072574; P:hepatocyte proliferation; IEA:Ensembl.
DR   GO; GO:0001822; P:kidney development; IEP:BHF-UCL.
DR   GO; GO:0002088; P:lens development in camera-type eye; IEP:BHF-UCL.
DR   GO; GO:0070309; P:lens fiber cell morphogenesis; IEP:BHF-UCL.
DR   GO; GO:0046619; P:lens placode formation involved in camera-type eye formation; ISS:BHF-UCL.
DR   GO; GO:0001889; P:liver development; IEP:BHF-UCL.
DR   GO; GO:0030324; P:lung development; IEP:BHF-UCL.
DR   GO; GO:0001946; P:lymphangiogenesis; IDA:BHF-UCL.
DR   GO; GO:0060836; P:lymphatic endothelial cell differentiation; IDA:BHF-UCL.
DR   GO; GO:0060838; P:lymphatic endothelial cell fate commitment; IMP:BHF-UCL.
DR   GO; GO:0070858; P:negative regulation of bile acid biosynthetic process; IMP:BHF-UCL.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:BHF-UCL.
DR   GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:BHF-UCL.
DR   GO; GO:0007406; P:negative regulation of neuroblast proliferation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:0045071; P:negative regulation of viral genome replication; IDA:BHF-UCL.
DR   GO; GO:0021915; P:neural tube development; ISS:BHF-UCL.
DR   GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl.
DR   GO; GO:0048664; P:neuron fate determination; IEA:Ensembl.
DR   GO; GO:0097150; P:neuronal stem cell population maintenance; ISS:BHF-UCL.
DR   GO; GO:0030910; P:olfactory placode formation; ISS:BHF-UCL.
DR   GO; GO:0043049; P:otic placode formation; ISS:BHF-UCL.
DR   GO; GO:0031016; P:pancreas development; IEP:BHF-UCL.
DR   GO; GO:0045787; P:positive regulation of cell cycle; ISS:BHF-UCL.
DR   GO; GO:1901978; P:positive regulation of cell cycle checkpoint; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
DR   GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:BHF-UCL.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:BHF-UCL.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:BHF-UCL.
DR   GO; GO:2000979; P:positive regulation of forebrain neuron differentiation; ISS:BHF-UCL.
DR   GO; GO:0060421; P:positive regulation of heart growth; ISS:BHF-UCL.
DR   GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISS:BHF-UCL.
DR   GO; GO:0060298; P:positive regulation of sarcomere organization; ISS:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR   GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR   GO; GO:0010468; P:regulation of gene expression; IDA:BHF-UCL.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
DR   GO; GO:0060042; P:retina morphogenesis in camera-type eye; ISS:BHF-UCL.
DR   GO; GO:0030240; P:skeletal muscle thin filament assembly; ISS:BHF-UCL.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0048845; P:venous blood vessel morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0055005; P:ventricular cardiac myofibril assembly; ISS:BHF-UCL.
DR   GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL.
DR   Gene3D; 1.10.10.500; Homeo-prospero domain; 1.
DR   InterPro; IPR023082; Homeo_prospero_dom.
DR   InterPro; IPR037131; Homeo_prospero_dom_sf.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR039350; Prospero_homeodomain.
DR   PANTHER; PTHR12198; HOMEOBOX PROTEIN PROSPERO/PROX-1/CEH-26; 1.
DR   PANTHER; PTHR12198:SF6; PROSPERO HOMEOBOX PROTEIN 1; 1.
DR   Pfam; PF05044; HPD; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   PROSITE; PS51818; HOMEO_PROSPERO; 1.
DR   Genevisible; Q92786; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Biological rhythms; Developmental protein; DNA-binding;
KW   Homeobox; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW   Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..737
FT                   /note="Prospero homeobox protein 1"
FT                   /id="PRO_0000208880"
FT   DOMAIN          577..635
FT                   /note="Prospero-type homeo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01162"
FT   DOMAIN          636..735
FT                   /note="Prospero"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01162"
FT   REGION          1..28
FT                   /note="Interaction with RORG"
FT                   /evidence="ECO:0000250|UniProtKB:P48437"
FT   REGION          103..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          320..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          445..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..735
FT                   /note="Homeo-Prospero"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01162"
FT   REGION          723..729
FT                   /note="Essential for nuclear localization, interaction with
FT                   RORG, repression of RORG transcriptional activator
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:P48437"
FT   COMPBIAS        103..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..242
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..341
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         177
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         179
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48437"
FT   MOD_RES         199
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         291
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48437"
FT   MOD_RES         295
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         511
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48437"
FT   MOD_RES         514
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48437"
FT   MOD_RES         557
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   CROSSLNK        324
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25755297"
FT   VARIANT         584
FT                   /note="H -> R (in dbSNP:rs12121210)"
FT                   /id="VAR_049362"
FT   CONFLICT        251..253
FT                   /note="RQL -> LHV (in Ref. 1; AAC50656)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        455..457
FT                   /note="PAA -> LV (in Ref. 1; AAC50656)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        724
FT                   /note="I -> F (in Ref. 1; AAC50656)"
FT                   /evidence="ECO:0000305"
FT   HELIX           582..592
FT                   /evidence="ECO:0007829|PDB:2LMD"
FT   HELIX           599..606
FT                   /evidence="ECO:0007829|PDB:2LMD"
FT   HELIX           614..645
FT                   /evidence="ECO:0007829|PDB:2LMD"
FT   HELIX           650..652
FT                   /evidence="ECO:0007829|PDB:2LMD"
FT   STRAND          653..656
FT                   /evidence="ECO:0007829|PDB:2LMD"
FT   HELIX           660..669
FT                   /evidence="ECO:0007829|PDB:2LMD"
FT   HELIX           679..698
FT                   /evidence="ECO:0007829|PDB:2LMD"
FT   HELIX           705..715
FT                   /evidence="ECO:0007829|PDB:2LMD"
FT   HELIX           728..730
FT                   /evidence="ECO:0007829|PDB:2LMD"
FT   HELIX           732..734
FT                   /evidence="ECO:0007829|PDB:2LMD"
SQ   SEQUENCE   737 AA;  83203 MW;  D243CEB421B313CA CRC64;
     MPDHDSTALL SRQTKRRRVD IGVKRTVGTA SAFFAKARAT FFSAMNPQGS EQDVEYSVVQ
     HADGEKSNVL RKLLKRANSY EDAMMPFPGA TIISQLLKNN MNKNGGTEPS FQASGLSSTG
     SEVHQEDICS NSSRDSPPEC LSPFGRPTMS QFDMDRLCDE HLRAKRARVE NIIRGMSHSP
     SVALRGNENE REMAPQSVSP RESYRENKRK QKLPQQQQQS FQQLVSARKE QKREERRQLK
     QQLEDMQKQL RQLQEKFYQI YDSTDSENDE DGNLSEDSMR SEILDARAQD SVGRSDNEMC
     ELDPGQFIDR ARALIREQEM AENKPKREGN NKERDHGPNS LQPEGKHLAE TLKQELNTAM
     SQVVDTVVKV FSAKPSRQVP QVFPPLQIPQ ARFAVNGENH NFHTANQRLQ CFGDVIIPNP
     LDTFGNVQMA SSTDQTEALP LVVRKNSSDQ SASGPAAGGH HQPLHQSPLS ATTGFTTSTF
     RHPFPLPLMA YPFQSPLGAP SGSFSGKDRA SPESLDLTRD TTSLRTKMSS HHLSHHPCSP
     AHPPSTAEGL SLSLIKSECG DLQDMSEISP YSGSAMQEGL SPNHLKKAKL MFFYTRYPSS
     NMLKTYFSDV KFNRCITSQL IKWFSNFREF YYIQMEKYAR QAINDGVTST EELSITRDCE
     LYRALNMHYN KANDFEVPER FLEVAQITLR EFFNAIIAGK DVDPSWKKAI YKVICKLDSE
     VPEIFKSPNC LQELLHE
//