ID RPGR_MOUSE Reviewed; 1001 AA. AC Q9R0X5; A2ADP3; G9BBQ2; O88408; Q9CU92; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2013, sequence version 2. DT 27-MAR-2024, entry version 171. DE RecName: Full=X-linked retinitis pigmentosa GTPase regulator; DE Short=mRpgr; DE Flags: Precursor; GN Name=Rpgr; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND ISOPRENYLATION AT CYS-998. RC TISSUE=Brain; RX PubMed=9677393; DOI=10.1074/jbc.273.31.19656; RA Yan D., Swain P.K., Breuer D., Tucker R.M., Wu W., Fujita R., RA Rehemtulla A., Burke D., Swaroop A.; RT "Biochemical characterization and subcellular localization of the mouse RT retinitis pigmentosa GTPase regulator."; RL J. Biol. Chem. 273:19656-19663(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Testis; 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 [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 1). RC STRAIN=129/SvEvTacfBr; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-845 (ISOFORMS 2/3). RC STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 525-1001 (ISOFORM 5), INTERACTION WITH RP WHRN, AND TISSUE SPECIFICITY. RC STRAIN=129/Sv; RX PubMed=22323458; DOI=10.1167/iovs.11-8845; RA Wright R.N., Hong D.H., Perkins B.; RT "RpgrORF15 connects to the usher protein network through direct RT interactions with multiple whirlin isoforms."; RL Invest. Ophthalmol. Vis. Sci. 53:1519-1529(2012). RN [7] RP INTERACTION WITH PDE6D. 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 [8] 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 [9] RP SUBCELLULAR 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 [10] RP INTERACTION WITH SMC1A AND SMC3, AND SUBCELLULAR LOCATION. 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 [11] RP INTERACTS WITH CEP290, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=16632484; DOI=10.1093/hmg/ddl107; RA Chang B., Khanna H., Hawes N., Jimeno D., He S., Lillo C., Parapuram S.K., RA Cheng H., Scott A., Hurd R.E., Sayer J.A., Otto E.A., Attanasio M., RA O'Toole J.F., Jin G., Shou C., Hildebrandt F., Williams D.S., RA Heckenlively J.R., Swaroop A.; RT "In-frame deletion in a novel centrosomal/ciliary protein CEP290/NPHP6 RT perturbs its interaction with RPGR and results in early-onset retinal RT degeneration in the rd16 mouse."; RL Hum. Mol. Genet. 15:1847-1857(2006). RN [12] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=18579752; DOI=10.1095/biolreprod.107.067454; RA Brunner S., Colman D., Travis A.J., Luhmann U.F., Shi W., Feil S., RA Imsand C., Nelson J., Grimm C., Rulicke T., Fundele R., Neidhardt J., RA Berger W.; RT "Overexpression of RPGR leads to male infertility in mice due to defects in RT flagellar assembly."; RL Biol. Reprod. 79:608-617(2008). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [14] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=20007830; DOI=10.1167/iovs.08-2742; RA Brunner S., Skosyrski S., Kirschner-Schwabe R., Knobeloch K.P., RA Neidhardt J., Feil S., Glaus E., Luhmann U.F., Ruther K., Berger W.; RT "Cone versus rod disease in a mutant Rpgr mouse caused by different genetic RT backgrounds."; RL Invest. Ophthalmol. Vis. Sci. 51:1106-1115(2010). RN [15] RP TISSUE SPECIFICITY. RX PubMed=20805823; DOI=10.1038/ki.2010.252; RA Patil S.B., Verma R., Venkatareddy M., Khanna H.; RT "Expression and localization of the ciliary disease protein retinitis RT pigmentosa GTPase regulator in mammalian kidney."; RL Kidney Int. 78:622-623(2010). RN [16] RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=21546531; DOI=10.1167/iovs.11-7470; RA Wright R.N., Hong D.H., Perkins B.; RT "Misexpression of the constitutive Rpgr(ex1-19) variant leads to severe RT photoreceptor degeneration."; RL Invest. Ophthalmol. Vis. Sci. 52:5189-5201(2011). RN [17] RP FUNCTION, AND MOUSE MODEL OF X-LINKED RETINOSA PIGMENTOSA. RX PubMed=22563472; DOI=10.1371/journal.pone.0035865; RA Thompson D.A., Khan N.W., Othman M.I., Chang B., Jia L., Grahek G., Wu Z., RA Hiriyanna S., Nellissery J., Li T., Khanna H., Colosi P., Swaroop A., RA Heckenlively J.R.; RT "Rd9 is a naturally occurring mouse model of a common form of retinitis RT pigmentosa caused by mutations in RPGR-ORF15."; RL PLoS ONE 7:E35865-E35865(2012). RN [18] RP INTERACTION WITH SPATA7, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=29899041; DOI=10.1083/jcb.201712117; RA Dharmat R., Eblimit A., Robichaux M.A., Zhang Z., Nguyen T.T., Jung S.Y., RA He F., Jain A., Li Y., Qin J., Overbeek P., Roepman R., Mardon G., RA Wensel T.G., Chen R.; RT "SPATA7 maintains a novel photoreceptor-specific zone in the distal RT connecting cilium."; RL J. Cell Biol. 217:2851-2865(2018). CC -!- FUNCTION: Could be a guanine-nucleotide releasing factor (By CC similarity). Plays a role in ciliogenesis (By similarity). Probably CC regulates cilia formation by regulating actin stress filaments and cell CC contractility (By similarity). May be involved in microtubule CC organization and regulation of transport in primary cilia (By CC similarity). Plays an important role in photoreceptor integrity. CC Isoform 5 may play a critical role in spermatogenesis and in CC intraflagellar transport processes. {ECO:0000250, CC ECO:0000269|PubMed:18579752, ECO:0000269|PubMed:22563472}. CC -!- SUBUNIT: Interacts with SPATA7 (PubMed:29899041). Interacts with PDE6D CC (PubMed:9990021). Interacts with RPGRIP1 and RPGRIP1L; PDE6D, RPGRIP1 CC and RPGRIP1L may compete for the same binding sites (By similarity). CC Interacts with NPM1 (By similarity). Interacts with PDE6D. Isoform 5 CC interacts (via N-terminus) with SMC1A and SMC3 (PubMed:16043481). CC Isoform 5 interacts with CEP290 (PubMed:16632484). Interacts with WHRN CC (PubMed:22323458). {ECO:0000250|UniProtKB:Q92834, CC ECO:0000269|PubMed:16043481, ECO:0000269|PubMed:16632484, CC ECO:0000269|PubMed:22323458, ECO:0000269|PubMed:29899041, CC ECO:0000269|PubMed:9990021}. CC -!- INTERACTION: CC Q9R0X5; Q68CZ1: RPGRIP1L; Xeno; NbExp=3; IntAct=EBI-6915619, EBI-5235485; CC Q9R0X5-5; Q80VW5-12: Whrn; NbExp=2; IntAct=EBI-6915646, EBI-6915655; CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:15772089, CC ECO:0000269|PubMed:16043481, ECO:0000269|PubMed:20007830, CC ECO:0000269|PubMed:9677393}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000250|UniProtKB:Q92834}. Cell CC projection, cilium {ECO:0000269|PubMed:29899041}. Note=In the retinal CC photoreceptor cell layer, localizes at the connecting cilium CC (PubMed:29899041). Colocalizes with WHRN in the photoreceptor CC connecting cilium (PubMed:22323458). Colocalizes with CEP290 in the CC photoreceptor connecting cilium (PubMed:16632484). Colocalizes with CC RPGRIP1 in the photoreceptor connecting cilium (PubMed:15772089). CC {ECO:0000269|PubMed:15772089, ECO:0000269|PubMed:16632484, CC ECO:0000269|PubMed:22323458, ECO:0000269|PubMed:29899041}. CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm, cytoskeleton, cilium CC basal body. Cytoplasm, cytoskeleton, cilium axoneme. Cytoplasm, CC cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:20007830}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Comment=Additional isoforms seem to exist.; CC Name=1; Synonyms=ex1-19; CC IsoId=Q9R0X5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9R0X5-2; Sequence=VSP_005552; CC Name=3; CC IsoId=Q9R0X5-3; Sequence=VSP_005552, VSP_005553; CC Name=4; CC IsoId=Q9R0X5-4; Sequence=VSP_005551, VSP_005552, VSP_005554, CC VSP_005555; CC Name=5; Synonyms=ORF15; CC IsoId=Q9R0X5-5; Sequence=VSP_045292; CC -!- TISSUE SPECIFICITY: Expressed in the retina (at protein level) CC (PubMed:10401007, PubMed:22323458, PubMed:12140192, PubMed:16632484, CC PubMed:20007830, PubMed:21546531, PubMed:29899041). Isoforms 1: CC Expressed in the retina (at protein level) (PubMed:21546531). Isoform CC 5: Expressed in the retina (at protein level) (PubMed:20007830, CC PubMed:21546531). Expressed in the brain (PubMed:9677393, CC PubMed:10401007). Expressed in the testis (at protein level) CC (PubMed:10401007, PubMed:18579752). Expressed in kidney (at protein CC level) (PubMed:10401007, PubMed:20805823). CC {ECO:0000269|PubMed:10401007, ECO:0000269|PubMed:12140192, CC ECO:0000269|PubMed:16632484, ECO:0000269|PubMed:18579752, CC ECO:0000269|PubMed:20007830, ECO:0000269|PubMed:20805823, CC ECO:0000269|PubMed:21546531, ECO:0000269|PubMed:22323458, CC ECO:0000269|PubMed:29899041, ECO:0000269|PubMed:9677393}. CC -!- DEVELOPMENTAL STAGE: At postnatal day 3 isoform 1 is expressed in the CC retina in a narrow band at the developing photoreceptor layer; CC expression in this band persists through to postnatal day 14 but CC becomes severely diminished in the adult retina. Isoform 5 is first CC detected in the retina at postnatal day 14 and is expressed at CC increased levels in the adult retina (at protein level). Expressed CC throughout embryonic development from day 7 of gestation. Also CC expressed in adult. {ECO:0000269|PubMed:21546531, CC ECO:0000269|PubMed:9677393}. CC -!- DOMAIN: The RCC1 repeat region mediates interactions with RPGRIP1. CC {ECO:0000250|UniProtKB:Q92834}. CC -!- PTM: Prenylated. {ECO:0000269|PubMed:9677393}. CC -!- MISCELLANEOUS: Male transgenic mice carrying multiple copies of the CC Rpgr transgene are infertile showing normal mating but no progeny; CC these mice also exhibit reduced sperm numbers as well as morphological CC and functional defects in the sperm flagellum. CC {ECO:0000305|PubMed:18579752}. CC -!- MISCELLANEOUS: Male BL/6 and BALB/c transgenic mice with an in-frame CC deletion of exon 4 of Rpgr show retinal degeneration that is rod or CC cone dominated, respectively. {ECO:0000305|PubMed:20007830}. CC -!- MISCELLANEOUS: Overexpression of isoform 1 results in atypical CC accumulation of Rpgr in photoreceptor outer segments, abnormal CC photoreceptor morphology and severe retinal degeneration. CC {ECO:0000305|PubMed:21546531}. CC -!- MISCELLANEOUS: In a mouse model of X-linked retinosa pigmentosa, where CC a 32bp duplication leads to a frameshift in the reading frame and a CC premature stop codon in isoform 5 (ORF15), mice exhibited retinal CC pathology including pigment loss and a slow progressive decrease in CC outer nuclear layer thickness. {ECO:0000305|PubMed:22563472}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC40190.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB30628.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAM22657.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF044677; AAC40190.1; ALT_INIT; mRNA. DR EMBL; AJ238396; CAB54041.1; -; mRNA. DR EMBL; AJ318464; CAC86115.1; -; Genomic_DNA. DR EMBL; AL671042; CAM22657.1; ALT_INIT; Genomic_DNA. DR EMBL; AK017192; BAB30628.3; ALT_INIT; mRNA. DR EMBL; BX005236; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; HQ260316; AEO00588.1; -; Genomic_DNA. DR RefSeq; NP_035415.1; NM_011285.2. DR AlphaFoldDB; Q9R0X5; -. DR SMR; Q9R0X5; -. DR BioGRID; 202963; 1. DR DIP; DIP-46319N; -. DR IntAct; Q9R0X5; 5. DR STRING; 10090.ENSMUSP00000037358; -. DR GlyGen; Q9R0X5; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9R0X5; -. DR PhosphoSitePlus; Q9R0X5; -. DR EPD; Q9R0X5; -. DR MaxQB; Q9R0X5; -. DR PaxDb; 10090-ENSMUSP00000037358; -. DR ProteomicsDB; 300437; -. [Q9R0X5-1] DR ProteomicsDB; 300438; -. [Q9R0X5-2] DR ProteomicsDB; 300439; -. [Q9R0X5-3] DR ProteomicsDB; 300440; -. [Q9R0X5-4] DR ProteomicsDB; 300441; -. [Q9R0X5-5] DR DNASU; 19893; -. DR GeneID; 19893; -. DR KEGG; mmu:19893; -. DR UCSC; uc009sqj.2; mouse. [Q9R0X5-4] DR AGR; MGI:1344037; -. DR MGI; MGI:1344037; Rpgr. DR eggNOG; KOG1426; Eukaryota. DR InParanoid; Q9R0X5; -. DR OrthoDB; 5475808at2759; -. DR TreeFam; TF331400; -. DR BioGRID-ORCS; 19893; 4 hits in 76 CRISPR screens. DR ChiTaRS; Rpgr; mouse. DR PRO; PR:Q9R0X5; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q9R0X5; Protein. DR GO; GO:0042995; C:cell projection; ISO:MGI. DR GO; GO:0005813; C:centrosome; ISS:UniProtKB. DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB. DR GO; GO:0005929; C:cilium; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:MGI. DR GO; GO:0120206; C:photoreceptor distal connecting cilium; IDA:MGI. DR GO; GO:0001750; C:photoreceptor outer segment; ISO:MGI. DR GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central. DR GO; GO:0071482; P:cellular response to light stimulus; IMP:MGI. DR GO; GO:0060271; P:cilium assembly; ISO:MGI. DR GO; GO:0042462; P:eye photoreceptor cell development; IMP:MGI. DR GO; GO:0042073; P:intraciliary transport; IMP:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central. DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:MGI. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR GO; GO:0007601; P:visual perception; IMP:MGI. DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 1. DR InterPro; IPR009091; RCC1/BLIP-II. DR InterPro; IPR000408; Reg_chr_condens. DR PANTHER; PTHR45622; UBIQUITIN-PROTEIN LIGASE E3A-RELATED; 1. DR PANTHER; PTHR45622:SF69; X-LINKED RETINITIS PIGMENTOSA GTPASE REGULATOR; 1. DR Pfam; PF00415; RCC1; 6. DR PRINTS; PR00633; RCCNDNSATION. DR SUPFAM; SSF50985; RCC1/BLIP-II; 1. DR PROSITE; PS00626; RCC1_2; 3. DR PROSITE; PS50012; RCC1_3; 6. PE 1: Evidence at protein level; KW Alternative splicing; Cell projection; Cilium; KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Flagellum; KW Golgi apparatus; Guanine-nucleotide releasing factor; Lipoprotein; KW Methylation; Phosphoprotein; Prenylation; Reference proteome; Repeat; KW Sensory transduction; Vision. FT CHAIN 1..998 FT /note="X-linked retinitis pigmentosa GTPase regulator" FT /id="PRO_0000206639" FT PROPEP 999..1001 FT /note="Removed in mature form" FT /evidence="ECO:0000255" FT /id="PRO_0000370845" 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 404..428 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 631..738 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 794..869 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 902..925 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 962..1001 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 631..675 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 688..718 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 794..812 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 842..861 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 969..1001 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 518 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q92834" FT MOD_RES 998 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000305" FT LIPID 998 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000303|PubMed:9677393" FT VAR_SEQ 260..469 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:9677393" FT /id="VSP_005551" FT VAR_SEQ 525..817 FT /note="Missing (in isoform 2, isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:9677393" FT /id="VSP_005552" FT VAR_SEQ 818..1001 FT /note="APQLSETVKPEEGEMDEEISILNVEDTVEEERKEGEKEIVEEGSIPETEGSE FT TIDITDEKLDEVLKEEDSASLLQRALREYNENPKGHMYDRVKSSSSEILGGNDPTSKDI FT KKAKKISFFNRMSLTGQKLMQNTNDPLPEIKPIGDQIALQSDKKDANQNHMGQNLQDST FT TPNMEGKSKSCTIL -> VSESERESGGEREDRSEGDGDQICEKVSLETEHLQRAQGKQ FT ERKKGKDKRARCILDMKEREEDKGWEKGSEGGDKMKRDEGNQEKRKKEMEERDAGDERS FT EEEEGEEEEPEEGEKEEGGEEEEGTSEDQSREDEGDRQEKEGRREGKGRQEDGREGWKE FT GEEQEQEEEIEEGEEEEREGEEEGGEEEGEGEGEREEEGEGEEEGEGEEEGEGEEEGEG FT EEEGEGEEEGEGEEEGEGEEEGEGEEDGEGEEDGEGEEEGEGEEEGEREEDGEGEEDGE FT GEEEGEGEEEGEGEEEGEGEEEGEGEGEEEGEGEWEGEEEGEGEEEGEGEEEGEGEEEG FT EGEEEGEGEEEGGEDDEGEELEKKKGDITEEEEEEEEGQEGDEREREEHGSCEDDVEED FT KTYDREEGEYKKAIGKVADNESQEDRKQSPKVSKINGSMKYGRHGTYSEKPITNLGKTQ FT PSKMPMESRQLVENGLLGSERFWSDVLPLYLELK (in isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_045292" FT VAR_SEQ 904..943 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:9677393" FT /id="VSP_005553" FT VAR_SEQ 904..907 FT /note="GHMY -> DFLL (in isoform 4)" FT /evidence="ECO:0000303|PubMed:9677393" FT /id="VSP_005554" FT VAR_SEQ 908..1001 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:9677393" FT /id="VSP_005555" FT CONFLICT 226 FT /note="N -> S (in Ref. 3; CAC86115)" FT /evidence="ECO:0000305" FT CONFLICT 606 FT /note="K -> R (in Ref. 2; CAB54041 and 6; AEO00588)" FT /evidence="ECO:0000305" FT CONFLICT 697 FT /note="S -> N (in Ref. 2; CAB54041 and 6; AEO00588)" FT /evidence="ECO:0000305" SQ SEQUENCE 1001 AA; 111801 MW; 021997395B74E6CA CRC64; MAESESLVPD TGAVFTFGKT KFAENIPSKF WFKNDIPICL SCGDEHTAIV TGNNKLYMFG SNNWGQLGLG SKAAIIKPTC IKALKPEKVK LAACGRNHTL VSTDTGGVYA AGGNNEGQLG LGDTDDRDTF HQIVFFTPAD TIKQLSAGAN TSAALTEDGK LFMWGDNSEG QIGLEDKSNV CIPHEVTVGK PISWISCGYY HSAFVTMDGE LYTFGEPENG KLGLPNELLM NHRSPQRVLG IPERVIQVAC GGGHTVVLTE KVVYAFGLGQ FGQLGLGTFL FETSEPKIIE RIKDQKICHI SCGENHTALM TELGLLYTFG DGRHGKLGLG MENFTNQFFP TLCSNFLRFA VQLIACGGCH MLVFATPRLG TIDEPKFEDV YEPYISTGSF SINDLSPRSS LNRSLSARLR RRERERPPCS ASMVGTLPPL EGTSASTSAY FYPSSPPFHL SVNNYPEKSP SESMEPLDSD YFEDKMNKDT ETENSSAVDS ENFGETNDIL NMTHMMTTSS NEKLLDFSPI QKQQNQDTFE KVMESTPCTE NEDSYEYEEM SKIKEVTVYK QYLAKGIYMI RPAEILEAFS DEEVGNGLDQ VEEPRVFTDG KGLQSKQVGK ESDEEIVSEK KTEVMEVADV KKIRESEENS KSDSLFDDLP DKTMNSESED NKDIAEERRS SEQNMTFDSE TELVEEPDSY MECERHSEQD SAEELEQPKL VEYSSEEKDE KDEKDDDEVE TENLWYDRNC TEQETENVFR ATRFFPKFDL KHDHLSGIPE EQEGPEDSEG NVVVEQVVQA QKENLEFEGD RKEAKAEAPS DVITEKEAPQ LSETVKPEEG EMDEEISILN VEDTVEEERK EGEKEIVEEG SIPETEGSET IDITDEKLDE VLKEEDSASL LQRALREYNE NPKGHMYDRV KSSSSEILGG NDPTSKDIKK AKKISFFNRM SLTGQKLMQN TNDPLPEIKP IGDQIALQSD KKDANQNHMG QNLQDSTTPN MEGKSKSCTI L //