RPGR_HUMAN
ID RPGR_HUMAN Reviewed; 1020 AA.
AC Q92834; B1ARN3; E9PE28; O00702; O00737; Q3KN84; Q8N5T6; Q93039; Q9HD29;
AC Q9UMR1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=X-linked retinitis pigmentosa GTPase regulator;
DE Flags: Precursor;
GN Name=RPGR; Synonyms=RP3, XLRP3;
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] (ISOFORMS 2 AND 4), AND VARIANTS RP3 GLN-98;
RP VAL-215; ARG-250 AND 296-THR--ILE-300 DEL.
RX PubMed=8673101; DOI=10.1038/ng0596-35;
RA Meindl A., Dry K.L., Herrmann K., Manson F.D., Ciccodicola A., Edgar A.J.,
RA Carvalho M.R.S., Achatz H., Hellebrand H., Lennon A.A., Migliaccio C.,
RA Porter K., Zrenner E., Bird A.C., Jay M., Lorenz B., Wittwer B., D'Urso M.,
RA Meitinger T., Wright A.F.;
RT "A gene (RPGR) with homology to the RCC1 guanine nucleotide exchange factor
RT is mutated in X-linked retinitis pigmentosa (RP3).";
RL Nat. Genet. 13:35-42(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS RP3 CYS-130; SER-235
RP AND SER-275.
RC TISSUE=Retina;
RX PubMed=8817343; DOI=10.1093/hmg/5.7.1035;
RA Roepman R., van Duijnhoven G., Rosenberg T., Pinckers A.J.L.G.,
RA Bleeker-Wagemakers L.M., Bergen A.A.B., Post J., Beck A., Reinhardt R.,
RA Ropers H.-H., Cremers F., Berger W.;
RT "Positional cloning of the gene for X-linked retinitis pigmentosa 3:
RT homology with the guanine-nucleotide-exchange factor RCC1.";
RL Hum. Mol. Genet. 5:1035-1041(1996).
RN [3]
RP SEQUENCE REVISION.
RA Berger W.;
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Retina;
RX PubMed=10401007; DOI=10.1093/hmg/8.8.1571;
RA Kirschner R., Rosenberg T., Schultz-Heienbrok R., Lenzner S., Feil S.,
RA Roepman R., Cremers F.P.M., Ropers H.-H., Berger W.;
RT "RPGR transcription studies in mouse and human tissues reveal a retina-
RT specific isoform that is disrupted in a patient with X-linked retinitis
RT pigmentosa.";
RL Hum. Mol. Genet. 8:1571-1578(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RX PubMed=11702207; DOI=10.1007/s004390100572;
RA Kirschner R., Erturk D., Zeitz C., Sahin S., Ramser J., Cremers F.P.M.,
RA Ropers H.-H., Berger W.;
RT "DNA sequence comparison of human and mouse retinitis pigmentosa GTPase
RT regulator (RPGR) identifies tissue-specific exons and putative regulatory
RT elements.";
RL Hum. Genet. 109:271-278(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 525-840 (ISOFORM 1), AND VARIANTS RP3
RP GLN-98 AND ARG-250.
RX PubMed=10932196; DOI=10.1038/78182;
RA Vervoort R., Lennon A.A., Bird A.C., Tulloch B., Axton R., Miano M.G.,
RA Meindl A., Meitinger T., Ciccodicola A., Wright A.F.;
RT "Mutational hot spot within a new RPGR exon in X-linked retinitis
RT pigmentosa.";
RL Nat. Genet. 25:462-466(2000).
RN [10]
RP INTERACTION WITH PDE6D, CHARACTERIZATION OF RP3 VARIANTS GLN-98; CYS-130;
RP VAL-215; SER-235; ARG-250 AND SER-275, AND MUTAGENESIS OF VAL-36.
RX PubMed=9990021; DOI=10.1073/pnas.96.4.1315;
RA Linari M., Ueffing M., Manson F., Wright A., Meitinger T., Becker J.;
RT "The retinitis pigmentosa GTPase regulator, RPGR, interacts with the delta
RT subunit of rod cyclic GMP phosphodiesterase.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1315-1320(1999).
RN [11]
RP INVOLVEMENT IN RP3/RP15.
RX PubMed=10970770; DOI=10.1086/303091;
RA Mears A.J., Hiriyanna S., Vervoort R., Yashar B., Gieser L., Fahrner S.,
RA Daiger S.P., Heckenlively J.R., Sieving P.A., Wright A.F., Swaroop A.;
RT "Remapping of the RP15 locus for X-linked cone-rod degeneration to Xp11.4-
RT p21.1, and identification of a de novo insertion in the RPGR exon ORF15.";
RL Am. J. Hum. Genet. 67:1000-1003(2000).
RN [12]
RP INTERACTION WITH RPGRIP1.
RX PubMed=10958648; DOI=10.1093/hmg/9.14.2095;
RA Roepman R., Bernoud-Hubac N., Schick D.E., Maugeri A., Berger W.,
RA Ropers H.-H., Cremers F.P.M., Ferreira P.A.;
RT "The retinitis pigmentosa GTPase regulator (RPGR) interacts with novel
RT transport-like proteins in the outer segments of rod photoreceptors.";
RL Hum. Mol. Genet. 9:2095-2105(2000).
RN [13]
RP INVOLVEMENT IN CORDX1, AND VARIANT ASP-345.
RX PubMed=11857109; DOI=10.1086/339620;
RA Demirci F.Y.K., Rigatti B.W., Wen G., Radak A.L., Mah T.S., Baic C.L.,
RA Traboulsi E.I., Alitalo T., Ramser J., Gorin M.B.;
RT "X-linked cone-rod dystrophy (locus COD1): identification of mutations in
RT RPGR exon ORF15.";
RL Am. J. Hum. Genet. 70:1049-1053(2002).
RN [14]
RP INVOLVEMENT IN MDXLA.
RX PubMed=12160730; DOI=10.1006/geno.2002.6815;
RA Ayyagari R., Demirci F.Y., Liu J., Bingham E.L., Stringham H., Kakuk L.E.,
RA Boehnke M., Gorin M.B., Richards J.E., Sieving P.A.;
RT "X-linked recessive atrophic macular degeneration from RPGR mutation.";
RL Genomics 80:166-171(2002).
RN [15]
RP TISSUE SPECIFICITY.
RX PubMed=12140192; DOI=10.1093/hmg/11.16.1899;
RA Mavlyutov T.A., Zhao H., Ferreira P.A.;
RT "Species-specific subcellular localization of RPGR and RPGRIP isoforms:
RT implications for the phenotypic variability of congenital retinopathies
RT among species.";
RL Hum. Mol. Genet. 11:1899-1907(2002).
RN [16]
RP INVOLVEMENT IN RPDSI.
RX PubMed=12920075; DOI=10.1136/jmg.40.8.609;
RA Zito I., Downes S.M., Patel R.J., Cheetham M.E., Ebenezer N.D.,
RA Jenkins S.A., Bhattacharya S.S., Webster A.R., Holder G.E., Bird A.C.,
RA Bamiou D.E., Hardcastle A.J.;
RT "RPGR mutation associated with retinitis pigmentosa, impaired hearing, and
RT sinorespiratory infections.";
RL J. Med. Genet. 40:609-615(2003).
RN [17]
RP ALTERNATIVE SPLICING (ISOFORM 6), INTERACTION WITH NPM1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15772089; DOI=10.1093/hmg/ddi129;
RA Shu X., Fry A.M., Tulloch B., Manson F.D., Crabb J.W., Khanna H.,
RA Faragher A.J., Lennon A., He S., Trojan P., Giessl A., Wolfrum U.,
RA Vervoort R., Swaroop A., Wright A.F.;
RT "RPGR ORF15 isoform co-localizes with RPGRIP1 at centrioles and basal
RT bodies and interacts with nucleophosmin.";
RL Hum. Mol. Genet. 14:1183-1197(2005).
RN [18]
RP INTERACTION WITH SMCA1 AND SMC3.
RX PubMed=16043481; DOI=10.1074/jbc.m505827200;
RA Khanna H., Hurd T.W., Lillo C., Shu X., Parapuram S.K., He S., Akimoto M.,
RA Wright A.F., Margolis B., Williams D.S., Swaroop A.;
RT "RPGR-ORF15, which is mutated in retinitis pigmentosa, associates with
RT SMC1, SMC3, and microtubule transport proteins.";
RL J. Biol. Chem. 280:33580-33587(2005).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [20]
RP INTERACTION WITH RPGRIP1L.
RX PubMed=19430481; DOI=10.1038/ng.366;
RA Khanna H., Davis E.E., Murga-Zamalloa C.A., Estrada-Cuzcano A., Lopez I.,
RA den Hollander A.I., Zonneveld M.N., Othman M.I., Waseem N., Chakarova C.F.,
RA Maubaret C., Diaz-Font A., MacDonald I., Muzny D.M., Wheeler D.A.,
RA Morgan M., Lewis L.R., Logan C.V., Tan P.L., Beer M.A., Inglehearn C.F.,
RA Lewis R.A., Jacobson S.G., Bergmann C., Beales P.L., Attie-Bitach T.,
RA Johnson C.A., Otto E.A., Bhattacharya S.S., Hildebrandt F., Gibbs R.A.,
RA Koenekoop R.K., Swaroop A., Katsanis N.;
RT "A common allele in RPGRIP1L is a modifier of retinal degeneration in
RT ciliopathies.";
RL Nat. Genet. 41:739-745(2009).
RN [21]
RP FUNCTION.
RX PubMed=21933838; DOI=10.1093/hmg/ddr423;
RA Gakovic M., Shu X., Kasioulis I., Carpanini S., Moraga I., Wright A.F.;
RT "The role of RPGR in cilia formation and actin stability.";
RL Hum. Mol. Genet. 20:4840-4850(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-418 AND SER-518, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-392, AND INTERACTION WITH
RP PDE6D.
RX PubMed=23559067; DOI=10.1038/embor.2013.37;
RA Watzlich D., Vetter I., Gotthardt K., Miertzschke M., Chen Y.X.,
RA Wittinghofer A., Ismail S.;
RT "The interplay between RPGR, PDE? and Arl2/3 regulate the ciliary targeting
RT of farnesylated cargo.";
RL EMBO Rep. 14:465-472(2013).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 1-392 IN COMPLEX WITH RPGRIP1,
RP INTERACTION WITH RPGRIP1; RPGRIP1L AND PDE6D, DOMAIN, MUTAGENESIS OF
RP ARG-323, AND CHARACTERIZATION OF VARIANT RP3 ARG-320.
RX PubMed=24981858; DOI=10.1016/j.celrep.2014.05.049;
RA Remans K., Burger M., Vetter I.R., Wittinghofer A.;
RT "C2 domains as protein-protein interaction modules in the ciliary
RT transition zone.";
RL Cell Rep. 8:1-9(2014).
RN [25]
RP VARIANTS RP3 VAL-60; VAL-75 AND GLY-262, AND VARIANTS LYS-425; VAL-431 AND
RP GLU-566.
RX PubMed=9399904; DOI=10.1086/301646;
RA Buraczynska M., Wu W., Fujita R., Buraczynska K., Phelps E., Andreasson S.,
RA Bennett J., Birch D.G., Fishman G.A., Hoffman D.R., Inana G.,
RA Jacobson S.G., Musarella M.A., Sieving P.A., Swaroop A.;
RT "Spectrum of mutations in the RPGR gene that are identified in 20% of
RT families with X-linked retinitis pigmentosa.";
RL Am. J. Hum. Genet. 61:1287-1292(1997).
RN [26]
RP VARIANT RP3 VAL-60.
RX PubMed=9855162; DOI=10.1016/s0161-6420(98)91231-3;
RA Fishman G.A., Grover S., Jacobson S.G., Alexander K.R., Derlacki D.J.,
RA Wu W., Buraczynska M., Swaroop A.;
RT "X-linked retinitis pigmentosa in two families with a missense mutation in
RT the RPGR gene and putative change of glycine to valine at codon 60.";
RL Ophthalmology 105:2286-2296(1998).
RN [27]
RP VARIANTS RP3 ASN-99 AND VAL-289.
RX PubMed=10482958; DOI=10.1038/sj.ejhg.5200352;
RA Miano M.G., Testa F., Strazzullo M., Trujillo M., De Bernardo C.,
RA Grammatico B., Simonelli F., Mangino M., Torrente I., Ruberto G.,
RA Beneyto M., Antinolo G., Rinaldi E., Danesino C., Ventruto V., D'Urso M.,
RA Ayuso C., Baiget M., Ciccodicola A.;
RT "Mutation analysis of the RPGR gene reveals novel mutations in south
RT European patients with X-linked retinitis pigmentosa.";
RL Eur. J. Hum. Genet. 7:687-694(1999).
RN [28]
RP VARIANTS ILE-76; LYS-425 AND GLU-566.
RX PubMed=10480356; DOI=10.1007/s004399900110;
RA Zito I., Thiselton D.L., Gorin M.B., Stout J.T., Plant C., Bird A.C.,
RA Bhattacharya S.S., Hardcastle A.J.;
RT "Identification of novel RPGR (retinitis pigmentosa GTPase regulator)
RT mutations in a subset of X-linked retinitis pigmentosa families segregating
RT with the RP3 locus.";
RL Hum. Genet. 105:57-62(1999).
RN [29]
RP VARIANT RP3 ARG-302.
RX PubMed=10737996;
RX DOI=10.1002/(sici)1098-1004(200004)15:4<386::aid-humu23>3.0.co;2-4;
RA Zito I., Gorin M.B., Plant C., Bird A.C., Bhattacharya S.S.,
RA Hardcastle A.J.;
RT "Novel mutations of the RPGR gene in RP3 families.";
RL Hum. Mutat. 15:386-386(2000).
RN [30]
RP VARIANTS LYS-425; GLN-526 DEL; MET-533 AND GLU-566.
RX PubMed=10980543;
RX DOI=10.1002/1098-1004(200009)16:3<273::aid-humu19>3.0.co;2-w;
RA Zito I., Morris A., Tyson P., Winship I., Sharp D., Gilbert D.,
RA Thiselton D.L., Bhattacharya S.S., Hardcastle A.J.;
RT "Sequence variation within the RPGR gene: evidence for a founder complex
RT allele.";
RL Hum. Mutat. 16:273-274(2000).
RN [31]
RP VARIANTS RP3 ARG-43; GLU-43; VAL-60; GLY-127; TYR-302 AND ASP-436, AND
RP VARIANTS ASP-345; LYS-425; VAL-431 AND GLU-566.
RX PubMed=10937588;
RA Sharon D., Bruns G.A.P., McGee T.L., Sandberg M.A., Berson E.L.,
RA Dryja T.P.;
RT "X-linked retinitis pigmentosa: mutation spectrum of the RPGR and RP2 genes
RT and correlation with visual function.";
RL Invest. Ophthalmol. Vis. Sci. 41:2712-2721(2000).
RN [32]
RP VARIANT RP3 ASP-436.
RX PubMed=11180598;
RX DOI=10.1002/1098-1004(200102)17:2<151::aid-humu7>3.0.co;2-w;
RA Guevara-Fujita M., Fahrner S., Buraczynska K., Cook J., Wheaton D.,
RA Cortes F., Vicencio C., Pena M., Fishman G.A., Mintz-Hittner H.,
RA Birch D.G., Hoffman D.R., Mears A.J., Fujita R., Swaroop A.;
RT "Five novel RPGR mutations in families with X-linked retinitis
RT pigmentosa.";
RL Hum. Mutat. 17:151-151(2001).
RN [33]
RP VARIANTS RP3 GLY-127; ARG-173; TYR-250; LEU-258 DEL; ARG-267; GLY-285 AND
RP ASP-436.
RX PubMed=11992260; DOI=10.1086/340848;
RA Breuer D.K., Yashar B.M., Filippova E., Hiriyanna S., Lyons R.H.,
RA Mears A.J., Asaye B., Acar C., Vervoort R., Wright A.F., Musarella M.A.,
RA Wheeler P., MacDonald I., Iannaccone A., Birch D., Hoffman D.R.,
RA Fishman G.A., Heckenlively J.R., Jacobson S.G., Sieving P.A., Swaroop A.;
RT "A comprehensive mutation analysis of RP2 and RPGR in a North American
RT cohort of families with X-linked retinitis pigmentosa.";
RL Am. J. Hum. Genet. 70:1545-1554(2002).
RN [34]
RP VARIANTS RP3 ASN-312; TYR-312 AND ARG-320.
RX PubMed=14564670; DOI=10.1086/379379;
RA Sharon D., Sandberg M.A., Rabe V.W., Stillberger M., Dryja T.P.,
RA Berson E.L.;
RT "RP2 and RPGR mutations and clinical correlations in patients with X-linked
RT retinitis pigmentosa.";
RL Am. J. Hum. Genet. 73:1131-1146(2003).
RN [35]
RP VARIANTS RP3 LEU-152 AND VAL-215.
RX PubMed=12657579; DOI=10.1167/iovs.02-0605;
RA Bader I., Brandau O., Achatz H., Apfelstedt-Sylla E., Hergersberg M.,
RA Lorenz B., Wissinger B., Wittwer B., Rudolph G., Meindl A., Meitinger T.;
RT "X-linked retinitis pigmentosa: RPGR mutations in most families with
RT definite X linkage and clustering of mutations in a short sequence stretch
RT of exon ORF15.";
RL Invest. Ophthalmol. Vis. Sci. 44:1458-1463(2003).
RN [36]
RP VARIANT RPDSI ARG-173.
RX PubMed=14627685; DOI=10.1136/jmg.40.11.e118;
RA Iannaccone A., Breuer D.K., Wang X.F., Kuo S.F., Normando E.M.,
RA Filippova E., Baldi A., Hiriyanna S., MacDonald C.B., Baldi F.,
RA Cosgrove D., Morton C.C., Swaroop A., Jablonski M.M.;
RT "Clinical and immunohistochemical evidence for an X linked retinitis
RT pigmentosa syndrome with recurrent infections and hearing loss in
RT association with an RPGR mutation.";
RL J. Med. Genet. 40:E118-E118(2003).
CC -!- FUNCTION: Could be a guanine-nucleotide releasing factor. Plays a role
CC in ciliogenesis. Probably regulates cilia formation by regulating actin
CC stress filaments and cell contractility. Plays an important role in
CC photoreceptor integrity. May play a critical role in spermatogenesis
CC and in intraflagellar transport processes (By similarity). May be
CC involved in microtubule organization and regulation of transport in
CC primary cilia. {ECO:0000250, ECO:0000269|PubMed:21933838}.
CC -!- SUBUNIT: Interacts with SPATA7 (By similarity). Interacts with CEP290
CC (By similarity). Interacts with WHRN (By similarity). Interacts with
CC PDE6D (PubMed:9990021, PubMed:23559067, PubMed:24981858). Interacts
CC with RPGRIP1 (PubMed:10958648, PubMed:24981858). Interacts with
CC RPGRIP1L (PubMed:19430481, PubMed:24981858). PDE6D, RPGRIP1 and
CC RPGRIP1L may compete for the same binding sites (PubMed:24981858).
CC Isoform 6 interacts with NPM1 (via C-terminus) (PubMed:15772089).
CC Isoform 6 interacts with SMC1A and SMC3 (PubMed:16043481).
CC {ECO:0000250|UniProtKB:Q9R0X5, ECO:0000269|PubMed:10958648,
CC ECO:0000269|PubMed:15772089, ECO:0000269|PubMed:16043481,
CC ECO:0000269|PubMed:19430481, ECO:0000269|PubMed:23559067,
CC ECO:0000269|PubMed:24981858, ECO:0000269|PubMed:9990021}.
CC -!- INTERACTION:
CC Q92834; Q8IX15-3: HOMEZ; NbExp=3; IntAct=EBI-6558417, EBI-10172004;
CC Q92834; O43924: PDE6D; NbExp=10; IntAct=EBI-6558417, EBI-712685;
CC Q92834; Q96KN7: RPGRIP1; NbExp=10; IntAct=EBI-6558417, EBI-1050213;
CC Q92834; Q96KN7-4: RPGRIP1; NbExp=3; IntAct=EBI-6558417, EBI-11525164;
CC Q92834; O55057: Pde6d; Xeno; NbExp=3; IntAct=EBI-6558417, EBI-6558402;
CC Q92834-2; O43924: PDE6D; NbExp=3; IntAct=EBI-6558503, EBI-712685;
CC Q92834-2; O55057: Pde6d; Xeno; NbExp=3; IntAct=EBI-6558503, EBI-6558402;
CC Q92834-6; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-16431517, EBI-25840379;
CC Q92834-6; Q8IX15-3: HOMEZ; NbExp=3; IntAct=EBI-16431517, EBI-10172004;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme
CC {ECO:0000250|UniProtKB:Q9R0X5}. Golgi apparatus
CC {ECO:0000269|PubMed:15772089}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q9R0X5}. Note=In the retinal photoreceptor cell
CC layer, localizes at the connecting cilium (By similarity). Colocalizes
CC with WHRN in the photoreceptor connecting cilium (By similarity).
CC Colocalizes with CEP290 in the photoreceptor connecting cilium (By
CC similarity). Colocalizes with RPGRIP1 in the photoreceptor connecting
CC cilium (By similarity). {ECO:0000250|UniProtKB:Q9R0X5}.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Cytoplasm, cytoskeleton, cilium basal
CC body. Cytoplasm, cytoskeleton, cilium axoneme.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q92834-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92834-2; Sequence=VSP_005548;
CC Name=3;
CC IsoId=Q92834-3; Sequence=VSP_005548, VSP_005549, VSP_005550;
CC Name=4;
CC IsoId=Q92834-4; Sequence=VSP_005547, VSP_005548;
CC Name=5;
CC IsoId=Q92834-5; Sequence=VSP_009183, VSP_009184;
CC Name=6; Synonyms=ORF15;
CC IsoId=Q92834-6; Sequence=VSP_044559;
CC -!- TISSUE SPECIFICITY: Heart, brain, placenta, lung, liver, muscle,
CC kidney, retina, pancreas and fetal retinal pigment epithelium. Isoform
CC 3 is found only in the retina. Colocalizes with RPGRIP1 in the outer
CC segment of rod photoreceptors and cone outer segments.
CC {ECO:0000269|PubMed:12140192}.
CC -!- DOMAIN: The RCC1 repeat region mediates interactions with RPGRIP1.
CC {ECO:0000269|PubMed:24981858}.
CC -!- PTM: Prenylated. {ECO:0000250}.
CC -!- DISEASE: Retinitis pigmentosa 3 (RP3) [MIM:300029]: An X-linked retinal
CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis
CC pigmentosa is characterized by retinal pigment deposits visible on
CC fundus examination and primary loss of rod photoreceptor cells followed
CC by secondary loss of cone photoreceptors. Patients typically have night
CC vision blindness and loss of midperipheral visual field. As their
CC condition progresses, they lose their far peripheral visual field and
CC eventually central vision as well. In RP3, affected males have a severe
CC phenotype, and carrier females show a wide spectrum of clinical
CC features ranging from completely asymptomatic to severe retinitis
CC pigmentosa. Heterozygous women can manifest a form of choroidoretinal
CC degeneration which is distinguished from other types by the absence of
CC visual defects in the presence of a brilliant, scintillating, golden-
CC hued, patchy appearance most striking around the macula, called a
CC tapetal-like retinal reflex. {ECO:0000269|PubMed:10482958,
CC ECO:0000269|PubMed:10737996, ECO:0000269|PubMed:10932196,
CC ECO:0000269|PubMed:10937588, ECO:0000269|PubMed:10970770,
CC ECO:0000269|PubMed:11180598, ECO:0000269|PubMed:11992260,
CC ECO:0000269|PubMed:12657579, ECO:0000269|PubMed:14564670,
CC ECO:0000269|PubMed:24981858, ECO:0000269|PubMed:8673101,
CC ECO:0000269|PubMed:8817343, ECO:0000269|PubMed:9399904,
CC ECO:0000269|PubMed:9855162}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Retinitis pigmentosa and sinorespiratory infections with or
CC without deafness (RPDSI) [MIM:300455]: A disease characterized by the
CC association primary ciliary dyskinesia features with retinitis
CC pigmentosa. Some patients also manifest deafness.
CC {ECO:0000269|PubMed:12920075, ECO:0000269|PubMed:14627685}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Cone-rod dystrophy, X-linked 1 (CORDX1) [MIM:304020]: An
CC inherited retinal dystrophy characterized by retinal pigment deposits
CC visible on fundus examination, predominantly in the macular region, and
CC initial loss of cone photoreceptors followed by rod degeneration. This
CC leads to decreased visual acuity and sensitivity in the central visual
CC field, followed by loss of peripheral vision. Severe loss of vision
CC occurs earlier than in retinitis pigmentosa. In cone-rod dystrophy X-
CC linked type 1 the degree of rod-photoreceptor involvement can be
CC variable, with degeneration increasing as the disease progresses.
CC Affected individuals (essentially all of whom are males) present with
CC decreased visual acuity, myopia, photophobia, abnormal color vision,
CC full peripheral visual fields, decreased photopic electroretinographic
CC responses, and granularity of the macular retinal pigment epithelium.
CC Although penetrance appears to be nearly 100%, there is variable
CC expressivity with respect to age at onset and severity of symptoms.
CC {ECO:0000269|PubMed:11857109}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Macular degeneration, X-linked, atrophic (MDXLA) [MIM:300834]:
CC An ocular disorder characterized by macular atrophy causing progressive
CC loss of visual acuity with minimal peripheral visual impairment. Some
CC patients manifest extensive macular degeneration plus peripheral loss
CC of retinal pigment epithelium and choriocapillaries. Full-field
CC electroretinograms (ERGs) show normal cone and rod responses in some
CC affected males despite advanced macular degeneration.
CC {ECO:0000269|PubMed:12160730}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=Mutations of the RPGR gene; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/rpgrmut.htm";
CC ---------------------------------------------------------------------------
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DR EMBL; U57629; AAC50481.1; -; mRNA.
DR EMBL; X97668; CAA66258.1; -; mRNA.
DR EMBL; AJ238395; CAB54002.1; -; mRNA.
DR EMBL; AJ318463; CAC86116.1; -; Genomic_DNA.
DR EMBL; AL606748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471141; EAW59441.1; -; Genomic_DNA.
DR EMBL; BC031624; AAH31624.1; -; mRNA.
DR EMBL; AF286471; AAG00550.1; -; Genomic_DNA.
DR EMBL; BK005711; DAA05713.1; -; mRNA.
DR CCDS; CCDS14246.1; -. [Q92834-2]
DR CCDS; CCDS35229.1; -. [Q92834-6]
DR RefSeq; NP_000319.1; NM_000328.2. [Q92834-2]
DR RefSeq; NP_001030025.1; NM_001034853.1. [Q92834-6]
DR RefSeq; XP_016885199.1; XM_017029710.1.
DR PDB; 4JHN; X-ray; 1.70 A; A/B/C/D=1-392.
DR PDB; 4JHP; X-ray; 1.90 A; C=7-368.
DR PDB; 4QAM; X-ray; 1.83 A; A=1-392.
DR PDBsum; 4JHN; -.
DR PDBsum; 4JHP; -.
DR PDBsum; 4QAM; -.
DR AlphaFoldDB; Q92834; -.
DR SMR; Q92834; -.
DR BioGRID; 112030; 45.
DR CORUM; Q92834; -.
DR IntAct; Q92834; 44.
DR iPTMnet; Q92834; -.
DR PhosphoSitePlus; Q92834; -.
DR BioMuta; RPGR; -.
DR DMDM; 23503098; -.
DR EPD; Q92834; -.
DR jPOST; Q92834; -.
DR MassIVE; Q92834; -.
DR MaxQB; Q92834; -.
DR PaxDb; Q92834; -.
DR PeptideAtlas; Q92834; -.
DR PRIDE; Q92834; -.
DR ProteomicsDB; 19799; -.
DR ProteomicsDB; 75513; -. [Q92834-1]
DR ProteomicsDB; 75514; -. [Q92834-2]
DR ProteomicsDB; 75515; -. [Q92834-3]
DR ProteomicsDB; 75516; -. [Q92834-4]
DR ProteomicsDB; 75517; -. [Q92834-5]
DR Antibodypedia; 472; 190 antibodies from 30 providers.
DR DNASU; 6103; -.
DR Ensembl; ENST00000339363.7; ENSP00000343671.3; ENSG00000156313.15. [Q92834-1]
DR Ensembl; ENST00000474584.5; ENSP00000418926.1; ENSG00000156313.15. [Q92834-5]
DR Ensembl; ENST00000482855.5; ENSP00000419276.1; ENSG00000156313.15. [Q92834-3]
DR Ensembl; ENST00000642395.2; ENSP00000493468.2; ENSG00000156313.15. [Q92834-2]
DR Ensembl; ENST00000644337.1; ENSP00000494557.1; ENSG00000156313.15. [Q92834-4]
DR Ensembl; ENST00000645032.1; ENSP00000495537.1; ENSG00000156313.15. [Q92834-6]
DR GeneID; 6103; -.
DR KEGG; hsa:6103; -.
DR MANE-Select; ENST00000645032.1; ENSP00000495537.1; NM_001034853.2; NP_001030025.1. [Q92834-6]
DR UCSC; uc004deb.4; human. [Q92834-1]
DR CTD; 6103; -.
DR DisGeNET; 6103; -.
DR GeneCards; RPGR; -.
DR GeneReviews; RPGR; -.
DR HGNC; HGNC:10295; RPGR.
DR HPA; ENSG00000156313; Low tissue specificity.
DR MalaCards; RPGR; -.
DR MIM; 300029; phenotype.
DR MIM; 300455; phenotype.
DR MIM; 300834; phenotype.
DR MIM; 304020; phenotype.
DR MIM; 312610; gene.
DR neXtProt; NX_Q92834; -.
DR OpenTargets; ENSG00000156313; -.
DR Orphanet; 49382; Achromatopsia.
DR Orphanet; 1872; Cone rod dystrophy.
DR Orphanet; 244; Primary ciliary dyskinesia.
DR Orphanet; 247522; Primary ciliary dyskinesia-retinitis pigmentosa syndrome.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA34656; -.
DR VEuPathDB; HostDB:ENSG00000156313; -.
DR eggNOG; KOG1075; Eukaryota.
DR eggNOG; KOG1426; Eukaryota.
DR GeneTree; ENSGT00940000159616; -.
DR HOGENOM; CLU_005210_5_2_1; -.
DR InParanoid; Q92834; -.
DR OMA; WNNVLPH; -.
DR OrthoDB; 1062377at2759; -.
DR PhylomeDB; Q92834; -.
DR TreeFam; TF331400; -.
DR PathwayCommons; Q92834; -.
DR SignaLink; Q92834; -.
DR SIGNOR; Q92834; -.
DR BioGRID-ORCS; 6103; 12 hits in 705 CRISPR screens.
DR ChiTaRS; RPGR; human.
DR GeneWiki; Retinitis_pigmentosa_GTPase_regulator; -.
DR GenomeRNAi; 6103; -.
DR Pharos; Q92834; Tbio.
DR PRO; PR:Q92834; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q92834; protein.
DR Bgee; ENSG00000156313; Expressed in sperm and 195 other tissues.
DR ExpressionAtlas; Q92834; baseline and differential.
DR Genevisible; Q92834; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
DR GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc.
DR GO; GO:0042073; P:intraciliary transport; ISS:UniProtKB.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IMP:UniProtKB.
DR Gene3D; 2.130.10.30; -; 1.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR Pfam; PF00415; RCC1; 6.
DR PRINTS; PR00633; RCCNDNSATION.
DR SUPFAM; SSF50985; SSF50985; 1.
DR PROSITE; PS00626; RCC1_2; 4.
DR PROSITE; PS50012; RCC1_3; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Ciliopathy; Cilium;
KW Cilium biogenesis/degradation; Cone-rod dystrophy; Cytoplasm; Cytoskeleton;
KW Deafness; Disease variant; Flagellum; Golgi apparatus;
KW Guanine-nucleotide releasing factor; Lipoprotein; Methylation;
KW Phosphoprotein; Prenylation; Reference proteome; Repeat;
KW Retinitis pigmentosa; Sensory transduction; Vision.
FT CHAIN 1..1017
FT /note="X-linked retinitis pigmentosa GTPase regulator"
FT /id="PRO_0000206638"
FT PROPEP 1018..1020
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370844"
FT REPEAT 54..105
FT /note="RCC1 1"
FT REPEAT 106..158
FT /note="RCC1 2"
FT REPEAT 159..208
FT /note="RCC1 3"
FT REPEAT 209..261
FT /note="RCC1 4"
FT REPEAT 262..313
FT /note="RCC1 5"
FT REPEAT 314..367
FT /note="RCC1 6"
FT REGION 609..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..776
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..853
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..875
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..906
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1020
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1017
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 1017
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 354..415
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:8673101"
FT /id="VSP_005547"
FT VAR_SEQ 473..480
FT /note="YLLDEMTK -> THHEPEFQ (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009183"
FT VAR_SEQ 481..1020
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009184"
FT VAR_SEQ 585..1020
FT /note="GNDTGQVGPQADTDGEGLQKEVYRHENNNGVDQLDAKEIEKESDGGHSQKES
FT EAEEIDSEKETKLAEIAGMKDLREREKSTKKMSPFFGNLPDRGMNTESEENKDFVKKRE
FT SCKQDVIFDSERESVEKPDSYMEGASESQQGIADGFQQPEAIEFSSGEKEDDEVETDQN
FT IRYGRKLIEQGNEKETKPIISKSMAKYDFKCDRLSEIPEEKEGAEDSKGNGIEEQEVEA
FT NEENVKVHGGRKEKTEILSDDLTDKAEDHEFSKTEELKLEDVDEEINAENVESKKKTVG
FT DDESVPTGYHSKTEGAERTNDDSSAETIEKKEKANLEERAICEYNENPKGYMLDDADSS
FT SLEILENSETTPSKDMKKTKKIFLFKRVPSINQKIVKNNNEPLPEIKSIGDQIILKSDN
FT KDADQNHMSQNHQNIPPTNTERRSKSCTIL -> EIPEEKEGAEDSKGNGIEEQEVEAN
FT EENVKVHGGRKEKTEILSDDLTDKAEVSEGKAKSVGEAEDGPEGRGDGTCEEGSSGAEH
FT WQDEEREKGEKDKGRGEMERPGEGEKELAEKEEWKKRDGEEQEQKEREQGHQKERNQEM
FT EEGGEEEHGEGEEEEGDREEEEEKEGEGKEEGEGEEVEGEREKEEGERKKEERAGKEEK
FT GEEEGDQGEGEEEETEGRGEEKEEGGEVEGGEVEEGKGEREEEEEEGEGEEEEGEGEEE
FT EGEGEEEEGEGKGEEEGEEGEGEEEGEEGEGEGEEEEGEGEGEEEGEGEGEEEEGEGEG
FT EEEGEGEGEEEEGEGKGEEEGEEGEGEGEEEEGEGEGEDGEGEGEEEEGEWEGEEEEGE
FT GEGEEEGEGEGEEGEGEGEEEEGEGEGEEEEGEEEGEEEGEGEEEGEGEGEEEEEGEVE
FT GEVEGEEGEGEGEEEEGEEEGEEREKEGEGEENRRNREEEEEEEGKYQETGEEENERQD
FT GEEYKKVSKIKGSVKYGKHKTYQKKSVTNTQGNGKEQRSKMPVQSKRLLKNGPSGSKKF
FT WNNVLPHYLELK (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_044559"
FT VAR_SEQ 585..789
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10401007,
FT ECO:0000303|PubMed:8673101, ECO:0000303|PubMed:8817343"
FT /id="VSP_005548"
FT VAR_SEQ 841..851
FT /note="DHEFSKTEELK -> YSASHSQIVSV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10401007"
FT /id="VSP_005549"
FT VAR_SEQ 852..1020
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10401007"
FT /id="VSP_005550"
FT VARIANT 43
FT /note="G -> E (in RP3; dbSNP:rs62638630)"
FT /evidence="ECO:0000269|PubMed:10937588"
FT /id="VAR_018057"
FT VARIANT 43
FT /note="G -> R (in RP3; dbSNP:rs62638629)"
FT /evidence="ECO:0000269|PubMed:10937588"
FT /id="VAR_018058"
FT VARIANT 60
FT /note="G -> V (in RP3; dbSNP:rs62638634)"
FT /evidence="ECO:0000269|PubMed:10937588,
FT ECO:0000269|PubMed:9399904, ECO:0000269|PubMed:9855162"
FT /id="VAR_008501"
FT VARIANT 75
FT /note="I -> V (in RP3; benign variant; dbSNP:rs111631988)"
FT /evidence="ECO:0000269|PubMed:9399904"
FT /id="VAR_008503"
FT VARIANT 76
FT /note="S -> I (in dbSNP:rs1801685)"
FT /evidence="ECO:0000269|PubMed:10480356"
FT /id="VAR_013624"
FT VARIANT 98
FT /note="H -> Q (in RP3; reduces interaction with PDE6D;
FT dbSNP:rs62638636)"
FT /evidence="ECO:0000269|PubMed:10932196,
FT ECO:0000269|PubMed:8673101, ECO:0000269|PubMed:9990021"
FT /id="VAR_008504"
FT VARIANT 99
FT /note="T -> N (in RP3; dbSNP:rs62638637)"
FT /evidence="ECO:0000269|PubMed:10482958"
FT /id="VAR_013625"
FT VARIANT 127
FT /note="R -> G (in RP3; dbSNP:rs62638643)"
FT /evidence="ECO:0000269|PubMed:10937588,
FT ECO:0000269|PubMed:11992260"
FT /id="VAR_018059"
FT VARIANT 130
FT /note="F -> C (in RP3; reduces interaction with PDE6D;
FT dbSNP:rs62638644)"
FT /evidence="ECO:0000269|PubMed:8817343,
FT ECO:0000269|PubMed:9990021"
FT /id="VAR_006850"
FT VARIANT 152
FT /note="S -> L (in RP3)"
FT /evidence="ECO:0000269|PubMed:12657579"
FT /id="VAR_025949"
FT VARIANT 173
FT /note="G -> R (in RP3 and RPDSI; dbSNP:rs137852550)"
FT /evidence="ECO:0000269|PubMed:11992260,
FT ECO:0000269|PubMed:14627685"
FT /id="VAR_018060"
FT VARIANT 184
FT /note="Q -> H (in dbSNP:rs5963403)"
FT /id="VAR_033259"
FT VARIANT 215
FT /note="G -> V (in RP3; reduces interaction with PDE6D;
FT dbSNP:rs62650218)"
FT /evidence="ECO:0000269|PubMed:12657579,
FT ECO:0000269|PubMed:8673101, ECO:0000269|PubMed:9990021"
FT /id="VAR_008505"
FT VARIANT 235
FT /note="P -> S (in RP3; reduces interaction with PDE6D;
FT dbSNP:rs62638651)"
FT /evidence="ECO:0000269|PubMed:8817343,
FT ECO:0000269|PubMed:9990021"
FT /id="VAR_006851"
FT VARIANT 250
FT /note="C -> R (in RP3; reduces interaction with PDE6D;
FT dbSNP:rs62650220)"
FT /evidence="ECO:0000269|PubMed:10932196,
FT ECO:0000269|PubMed:8673101, ECO:0000269|PubMed:9990021"
FT /id="VAR_008506"
FT VARIANT 250
FT /note="C -> Y (in RP3; dbSNP:rs1601961064)"
FT /evidence="ECO:0000269|PubMed:11992260"
FT /id="VAR_018061"
FT VARIANT 258
FT /note="Missing (in RP3)"
FT /evidence="ECO:0000269|PubMed:11992260"
FT /id="VAR_018062"
FT VARIANT 262
FT /note="A -> G (in RP3; unknown pathological significance;
FT dbSNP:rs138018739)"
FT /evidence="ECO:0000269|PubMed:9399904"
FT /id="VAR_008507"
FT VARIANT 267
FT /note="G -> E (in RP3)"
FT /id="VAR_018063"
FT VARIANT 267
FT /note="G -> R (in RP3)"
FT /evidence="ECO:0000269|PubMed:11992260"
FT /id="VAR_026127"
FT VARIANT 275
FT /note="G -> S (in RP3; reduces interaction with PDE6D;
FT dbSNP:rs62642057)"
FT /evidence="ECO:0000269|PubMed:8817343,
FT ECO:0000269|PubMed:9990021"
FT /id="VAR_006852"
FT VARIANT 285
FT /note="E -> G (in RP3)"
FT /evidence="ECO:0000269|PubMed:11992260"
FT /id="VAR_026128"
FT VARIANT 289
FT /note="I -> V (in RP3; dbSNP:rs62640587)"
FT /evidence="ECO:0000269|PubMed:10482958"
FT /id="VAR_013626"
FT VARIANT 296..300
FT /note="Missing (in RP3)"
FT /evidence="ECO:0000269|PubMed:8673101"
FT /id="VAR_013627"
FT VARIANT 302
FT /note="C -> R (in RP3; dbSNP:rs62640589)"
FT /evidence="ECO:0000269|PubMed:10737996"
FT /id="VAR_011561"
FT VARIANT 302
FT /note="C -> Y (in RP3; dbSNP:rs62640590)"
FT /evidence="ECO:0000269|PubMed:10937588"
FT /id="VAR_018064"
FT VARIANT 312
FT /note="D -> N (in RP3)"
FT /evidence="ECO:0000269|PubMed:14564670"
FT /id="VAR_018065"
FT VARIANT 312
FT /note="D -> Y (in RP3)"
FT /evidence="ECO:0000269|PubMed:14564670"
FT /id="VAR_018066"
FT VARIANT 320
FT /note="G -> R (in RP3; impairs protein folding;
FT dbSNP:rs62640593)"
FT /evidence="ECO:0000269|PubMed:14564670,
FT ECO:0000269|PubMed:24981858"
FT /id="VAR_018067"
FT VARIANT 345
FT /note="N -> D (in dbSNP:rs41305223)"
FT /evidence="ECO:0000269|PubMed:10937588,
FT ECO:0000269|PubMed:11857109"
FT /id="VAR_018068"
FT VARIANT 425
FT /note="R -> K (in dbSNP:rs1801687)"
FT /evidence="ECO:0000269|PubMed:10480356,
FT ECO:0000269|PubMed:10937588, ECO:0000269|PubMed:10980543,
FT ECO:0000269|PubMed:9399904"
FT /id="VAR_008508"
FT VARIANT 431
FT /note="I -> V (in dbSNP:rs62635003)"
FT /evidence="ECO:0000269|PubMed:10937588,
FT ECO:0000269|PubMed:9399904"
FT /id="VAR_008509"
FT VARIANT 436
FT /note="G -> D (in RP3; dbSNP:rs62635004)"
FT /evidence="ECO:0000269|PubMed:10937588,
FT ECO:0000269|PubMed:11180598, ECO:0000269|PubMed:11992260"
FT /id="VAR_008510"
FT VARIANT 526
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:10980543"
FT /id="VAR_011562"
FT VARIANT 533
FT /note="T -> M (in dbSNP:rs41312104)"
FT /evidence="ECO:0000269|PubMed:10980543"
FT /id="VAR_011563"
FT VARIANT 566
FT /note="G -> E (in dbSNP:rs1801688)"
FT /evidence="ECO:0000269|PubMed:10480356,
FT ECO:0000269|PubMed:10937588, ECO:0000269|PubMed:10980543,
FT ECO:0000269|PubMed:9399904"
FT /id="VAR_008511"
FT MUTAGEN 36
FT /note="V->F: Does not reduce interaction with PDE6D."
FT /evidence="ECO:0000269|PubMed:9990021"
FT MUTAGEN 323
FT /note="R->E: Abolishes interaction with RPGRIP1."
FT /evidence="ECO:0000269|PubMed:24981858"
FT CONFLICT 1..3
FT /note="MRE -> MAKLRRSTTTAL (in Ref. 4; CAB54002)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="K -> N (in Ref. 4; CAC86116)"
FT /evidence="ECO:0000305"
FT STRAND 13..20
FT /evidence="ECO:0007829|PDB:4JHN"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:4QAM"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:4JHP"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:4JHN"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:4JHN"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:4JHN"
FT HELIX 226..231
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 252..261
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 282..288
FT /evidence="ECO:0007829|PDB:4JHN"
FT TURN 291..294
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 297..302
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:4JHN"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:4JHN"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 349..356
FT /evidence="ECO:0007829|PDB:4JHN"
FT STRAND 358..367
FT /evidence="ECO:0007829|PDB:4JHN"
FT CONFLICT Q92834-6:1144
FT /note="V -> I (in Ref. 17; DAA05713)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1020 AA; 113387 MW; EAB16275A9A436C3 CRC64;
MREPEELMPD SGAVFTFGKS KFAENNPGKF WFKNDVPVHL SCGDEHSAVV TGNNKLYMFG
SNNWGQLGLG SKSAISKPTC VKALKPEKVK LAACGRNHTL VSTEGGNVYA TGGNNEGQLG
LGDTEERNTF HVISFFTSEH KIKQLSAGSN TSAALTEDGR LFMWGDNSEG QIGLKNVSNV
CVPQQVTIGK PVSWISCGYY HSAFVTTDGE LYVFGEPENG KLGLPNQLLG NHRTPQLVSE
IPEKVIQVAC GGEHTVVLTE NAVYTFGLGQ FGQLGLGTFL FETSEPKVIE NIRDQTISYI
SCGENHTALI TDIGLMYTFG DGRHGKLGLG LENFTNHFIP TLCSNFLRFI VKLVACGGCH
MVVFAAPHRG VAKEIEFDEI NDTCLSVATF LPYSSLTSGN VLQRTLSARM RRRERERSPD
SFSMRRTLPP IEGTLGLSAC FLPNSVFPRC SERNLQESVL SEQDLMQPEE PDYLLDEMTK
EAEIDNSSTV ESLGETTDIL NMTHIMSLNS NEKSLKLSPV QKQKKQQTIG ELTQDTALTE
NDDSDEYEEM SEMKEGKACK QHVSQGIFMT QPATTIEAFS DEEVGNDTGQ VGPQADTDGE
GLQKEVYRHE NNNGVDQLDA KEIEKESDGG HSQKESEAEE IDSEKETKLA EIAGMKDLRE
REKSTKKMSP FFGNLPDRGM NTESEENKDF VKKRESCKQD VIFDSERESV EKPDSYMEGA
SESQQGIADG FQQPEAIEFS SGEKEDDEVE TDQNIRYGRK LIEQGNEKET KPIISKSMAK
YDFKCDRLSE IPEEKEGAED SKGNGIEEQE VEANEENVKV HGGRKEKTEI LSDDLTDKAE
DHEFSKTEEL KLEDVDEEIN AENVESKKKT VGDDESVPTG YHSKTEGAER TNDDSSAETI
EKKEKANLEE RAICEYNENP KGYMLDDADS SSLEILENSE TTPSKDMKKT KKIFLFKRVP
SINQKIVKNN NEPLPEIKSI GDQIILKSDN KDADQNHMSQ NHQNIPPTNT ERRSKSCTIL
