PROX1_HUMAN
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 03-AUG-2022, entry version 181.
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: ARNTL/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; 31.
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; Q92786; -.
DR PeptideAtlas; Q92786; -.
DR PRIDE; Q92786; -.
DR ProteomicsDB; 75470; -.
DR Antibodypedia; 34616; 648 antibodies from 44 providers.
DR DNASU; 5629; -.
DR Ensembl; ENST00000261454.8; ENSP00000261454.4; ENSG00000117707.16.
DR Ensembl; ENST00000366958.9; ENSP00000355925.4; ENSG00000117707.16.
DR Ensembl; ENST00000435016.2; ENSP00000400694.1; ENSG00000117707.16.
DR Ensembl; ENST00000498508.6; ENSP00000420283.2; ENSG00000117707.16.
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 CTD; 5629; -.
DR DisGeNET; 5629; -.
DR GeneCards; PROX1; -.
DR HGNC; HGNC:9459; PROX1.
DR HPA; ENSG00000117707; Tissue enhanced (brain, 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; 373478at2759; -.
DR PhylomeDB; Q92786; -.
DR TreeFam; TF316638; -.
DR PathwayCommons; Q92786; -.
DR SignaLink; Q92786; -.
DR SIGNOR; Q92786; -.
DR BioGRID-ORCS; 5629; 17 hits in 1099 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 158 other tissues.
DR ExpressionAtlas; Q92786; baseline and differential.
DR Genevisible; Q92786; HS.
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: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:0045892; P:negative regulation of transcription, DNA-templated; 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; -; 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 InterPro; IPR007738; Prox1.
DR PANTHER; PTHR12198; PTHR12198; 1.
DR PANTHER; PTHR12198:SF6; PTHR12198:SF6; 1.
DR Pfam; PF05044; HPD; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51818; HOMEO_PROSPERO; 1.
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
