ID RPGR1_HUMAN Reviewed; 1286 AA. AC Q96KN7; Q7Z2W6; Q8IXV5; Q96QA8; Q9HB94; Q9HB95; Q9HBK6; Q9NR40; DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 24-JAN-2024, entry version 186. DE RecName: Full=X-linked retinitis pigmentosa GTPase regulator-interacting protein 1; DE Short=RPGR-interacting protein 1; GN Name=RPGRIP1; 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 3), NUCLEOTIDE SEQUENCE [MRNA] RP OF 525-1286 (ISOFORM 1), INTERACTION WITH RPGR, TISSUE SPECIFICITY, AND RP VARIANT CORD13 SER-547. RC TISSUE=Retina; 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6), INTERACTION WITH RPGR, RP TISSUE SPECIFICITY, AND VARIANT GLN-1033. RX PubMed=10958647; DOI=10.1093/hmg/9.14.2085; RA Boylan J.P., Wright A.F.; RT "Identification of a novel protein interacting with RPGR."; RL Hum. Mol. Genet. 9:2085-2093(2000). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANTS LCA6 GLU-746 RP AND GLY-1114, AND VARIANT GLN-1033. RX PubMed=11528500; DOI=10.1038/sj.ejhg.5200689; RA Gerber S., Perrault I., Hanein S., Barbet F., Ducroq D., Ghazi I., RA Martin-Coignard D., Leowski C., Homfray T., Dufier J.-L., Munnich A., RA Kaplan J., Rozet J.-M.; RT "Complete exon-intron structure of the RPGR-interacting protein (RPGRIP1) RT gene allows the identification of mutations underlying Leber congenital RT amaurosis."; RL Eur. J. Hum. Genet. 9:561-571(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT GLN-1033. RC TISSUE=Brain; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 588-1286 (ISOFORM 1). RC TISSUE=Retina; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] 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 [8] RP INTERACTION WITH NPHP4, VARIANT GLY-876, AND CHARACTERIZATION OF VARIANT RP GLY-876. RX PubMed=16339905; DOI=10.1073/pnas.0505774102; RA Roepman R., Letteboer S.J., Arts H.H., van Beersum S.E., Lu X., Krieger E., RA Ferreira P.A., Cremers F.P.; RT "Interaction of nephrocystin-4 and RPGRIP1 is disrupted by nephronophthisis RT or Leber congenital amaurosis-associated mutations."; RL Proc. Natl. Acad. Sci. U.S.A. 102:18520-18525(2005). RN [9] RP INTERACTION WITH CEP290. RX PubMed=20200501; DOI=10.1038/ki.2010.27; RA Gerner M., Haribaskar R., Puetz M., Czerwitzki J., Walz G., Schaefer T.; RT "The retinitis pigmentosa GTPase regulator interacting protein 1 (RPGRIP1) RT links RPGR to the nephronophthisis protein network."; RL Kidney Int. 77:891-896(2010). RN [10] RP INTERACTION WITH NPHP4, INVOLVEMENT IN GLAUCOMA, VARIANTS LEU-32; ARG-135; RP VAL-318; THR-363; SER-585; HIS-589; GLN-598; SER-603; GLY-635; ILE-638; RP VAL-764; ILE-806; HIS-812; LEU-814; GLY-837; VAL-838; THR-841; GLN-852 AND RP ASP-883, AND CHARACTERIZATION OF VARIANTS HIS-589; GLN-598; GLY-635; RP VAL-764; ILE-806; HIS-812; GLY-837 AND VAL-838. RX PubMed=21224891; DOI=10.1038/ejhg.2010.217; RA Fernandez-Martinez L., Letteboer S., Mardin C.Y., Weisschuh N., Gramer E., RA Weber B.H., Rautenstrauss B., Ferreira P.A., Kruse F.E., Reis A., RA Roepman R., Pasutto F.; RT "Evidence for RPGRIP1 gene as risk factor for primary open angle RT glaucoma."; RL Eur. J. Hum. Genet. 19:445-451(2011). RN [11] RP INTERACTION WITH RPGR AND NEK4, AND SUBCELLULAR LOCATION. RX PubMed=21685204; DOI=10.1093/hmg/ddr280; RA Coene K.L., Mans D.A., Boldt K., Gloeckner C.J., van Reeuwijk J., Bolat E., RA Roosing S., Letteboer S.J., Peters T.A., Cremers F.P., Ueffing M., RA Roepman R.; RT "The ciliopathy-associated protein homologs RPGRIP1 and RPGRIP1L are linked RT to cilium integrity through interaction with Nek4 serine/threonine RT kinase."; RL Hum. Mol. Genet. 20:3592-3605(2011). RN [12] RP INTERACTION WITH SPATA7. RX PubMed=25398945; DOI=10.1093/hmg/ddu573; RA Eblimit A., Nguyen T.M., Chen Y., Esteve-Rudd J., Zhong H., Letteboer S., RA van Reeuwijk J., Simons D.L., Ding Q., Wu K.M., Li Y., van Beersum S., RA Moayedi Y., Xu H., Pickard P., Wang K., Gan L., Wu S.M., Williams D.S., RA Mardon G., Roepman R., Chen R.; RT "Spata7 is a retinal ciliopathy gene critical for correct RPGRIP1 RT localization and protein trafficking in the retina."; RL Hum. Mol. Genet. 24:1584-1601(2015). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 1091-1286 IN COMPLEX WITH RPGR, RP INTERACTION WITH RPGR, DOMAIN, REGION, CHARACTERIZATION OF VARIANT LCA6 RP GLY-1114, AND MUTAGENESIS OF GLU-1121; HIS-1174 AND GLU-1245. 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 [14] RP VARIANTS CORD13 SER-547 AND LEU-827. RX PubMed=12920076; DOI=10.1136/jmg.40.8.616; RA Hameed A., Abid A., Aziz A., Ismail M., Mehdi S.Q., Khaliq S.; RT "Evidence of RPGRIP1 gene mutations associated with recessive cone-rod RT dystrophy."; RL J. Med. Genet. 40:616-619(2003). RN [15] RP VARIANT LCA6 GLU-1211. RX PubMed=17554762; DOI=10.1002/humu.20565; RA Cideciyan A.V., Aleman T.S., Jacobson S.G., Khanna H., Sumaroka A., RA Aguirre G.K., Schwartz S.B., Windsor E.A., He S., Chang B., Stone E.M., RA Swaroop A.; RT "Centrosomal-ciliary gene CEP290/NPHP6 mutations result in blindness with RT unexpected sparing of photoreceptors and visual brain: implications for RT therapy of Leber congenital amaurosis."; RL Hum. Mutat. 28:1074-1083(2007). RN [16] RP VARIANT LCA6 GLU-1211. RX PubMed=17306875; DOI=10.1016/j.ophtha.2006.10.028; RA Jacobson S.G., Cideciyan A.V., Aleman T.S., Sumaroka A., Schwartz S.B., RA Roman A.J., Stone E.M.; RT "Leber congenital amaurosis caused by an RPGRIP1 mutation shows treatment RT potential."; RL Ophthalmology 114:895-898(2007). RN [17] RP VARIANT LCA6 PRO-631, AND VARIANTS GLN-96; GLU-192; PHE-432; TRP-601; RP GLN-1033 AND LEU-1057. RX PubMed=18682808; RA Seong M.W., Kim S.Y., Yu Y.S., Hwang J.M., Kim J.Y., Park S.S.; RT "Molecular characterization of Leber congenital amaurosis in Koreans."; RL Mol. Vis. 14:1429-1436(2008). RN [18] RP VARIANT GLN-1130. RX PubMed=21602930; DOI=10.1371/journal.pone.0019458; RA Li L., Xiao X., Li S., Jia X., Wang P., Guo X., Jiao X., Zhang Q., RA Hejtmancik J.F.; RT "Detection of variants in 15 genes in 87 unrelated Chinese patients with RT Leber congenital amaurosis."; RL PLoS ONE 6:E19458-E19458(2011). CC -!- FUNCTION: May function as scaffolding protein. Required for normal CC location of RPGR at the connecting cilium of photoreceptor cells. CC Required for normal disk morphogenesis and disk organization in the CC outer segment of photoreceptor cells and for survival of photoreceptor CC cells. {ECO:0000250|UniProtKB:Q9EPQ2, ECO:0000305|PubMed:10958648}. CC -!- SUBUNIT: Forms homodimers and elongated homopolymers (By similarity). CC Interacts with RPGR (PubMed:10958648, PubMed:10958647, CC PubMed:24981858). Interacts with NPHP4 (PubMed:16339905, CC PubMed:21224891). Interacts with NEK4 (PubMed:21685204). Interacts with CC SPATA7 (PubMed:25398945). Interacts with CEP290/NPHP6; mediating the CC association between RPGR and CEP290/NPHP6 (PubMed:20200501). CC {ECO:0000250|UniProtKB:Q9EPQ2, ECO:0000269|PubMed:10958647, CC ECO:0000269|PubMed:10958648, ECO:0000269|PubMed:16339905, CC ECO:0000269|PubMed:20200501, ECO:0000269|PubMed:21224891, CC ECO:0000269|PubMed:21685204, ECO:0000269|PubMed:24981858, CC ECO:0000269|PubMed:25398945}. CC -!- INTERACTION: CC Q96KN7; Q8WTP8: AEN; NbExp=3; IntAct=EBI-1050213, EBI-8637627; CC Q96KN7; Q9HC52: CBX8; NbExp=3; IntAct=EBI-1050213, EBI-712912; CC Q96KN7; Q8IYE0-2: CCDC146; NbExp=3; IntAct=EBI-1050213, EBI-10247802; CC Q96KN7; Q9NX63: CHCHD3; NbExp=3; IntAct=EBI-1050213, EBI-743375; CC Q96KN7; Q1MSJ5-2: CSPP1; NbExp=3; IntAct=EBI-1050213, EBI-10239155; CC Q96KN7; Q7L190: DPPA4; NbExp=3; IntAct=EBI-1050213, EBI-710457; CC Q96KN7; Q5TZK3: FAM74A6; NbExp=3; IntAct=EBI-1050213, EBI-10247271; CC Q96KN7; Q96JP0: FEM1C; NbExp=3; IntAct=EBI-1050213, EBI-2515330; CC Q96KN7; Q8WXI9: GATAD2B; NbExp=3; IntAct=EBI-1050213, EBI-923440; CC Q96KN7; Q9NQ87: HEYL; NbExp=3; IntAct=EBI-1050213, EBI-751092; CC Q96KN7; O15479: MAGEB2; NbExp=3; IntAct=EBI-1050213, EBI-1057615; CC Q96KN7; O75161: NPHP4; NbExp=3; IntAct=EBI-1050213, EBI-4281852; CC Q96KN7; Q92834: RPGR; NbExp=10; IntAct=EBI-1050213, EBI-6558417; CC Q96KN7; Q8N5L8: RPP25L; NbExp=3; IntAct=EBI-1050213, EBI-10189722; CC Q96KN7; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-1050213, EBI-748391; CC Q96KN7; Q9P0N9: TBC1D7; NbExp=3; IntAct=EBI-1050213, EBI-3258000; CC Q96KN7; P0C1Z6-2: TFPT; NbExp=3; IntAct=EBI-1050213, EBI-10178002; CC Q96KN7; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-1050213, EBI-492476; CC Q96KN7; Q9Y3M9: ZNF337; NbExp=3; IntAct=EBI-1050213, EBI-714987; CC Q96KN7; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-1050213, EBI-740727; CC Q96KN7; Q8TBZ8: ZNF564; NbExp=3; IntAct=EBI-1050213, EBI-10273713; CC Q96KN7-1; O75161-1: NPHP4; NbExp=9; IntAct=EBI-12499377, EBI-12499345; CC Q96KN7-4; A0A0S2Z4G9: RNF6; NbExp=3; IntAct=EBI-11525164, EBI-16428950; CC Q96KN7-4; Q92834: RPGR; NbExp=3; IntAct=EBI-11525164, EBI-6558417; CC Q96KN7-4; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-11525164, EBI-492476; CC Q96KN7-4; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-11525164, EBI-16429014; CC -!- SUBCELLULAR LOCATION: Cell projection, cilium CC {ECO:0000269|PubMed:21685204}. Note=Situated between the axonemal CC microtubules and the plasma membrane (By similarity). In the retinal CC photoreceptor cell layer, localizes at the connecting cilium, a thin CC bridge linking the cell body and the light-sensing outer segment (By CC similarity). Colocalizes with RGPR in the photoreceptor connecting CC cilium (By similarity). {ECO:0000250|UniProtKB:Q9EPQ2}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=Q96KN7-1; Sequence=Displayed; CC Name=2; Synonyms=a; CC IsoId=Q96KN7-2; Sequence=VSP_009521, VSP_009525; CC Name=3; Synonyms=b; CC IsoId=Q96KN7-3; Sequence=VSP_009522, VSP_009526; CC Name=4; CC IsoId=Q96KN7-4; Sequence=VSP_009519, VSP_009523, VSP_009524; CC Name=5; CC IsoId=Q96KN7-5; Sequence=VSP_009520; CC Name=6; CC IsoId=Q96KN7-6; Sequence=VSP_009520, VSP_009527; CC -!- TISSUE SPECIFICITY: Strong expression in retina, with weaker expression CC in testis. Expressed in other neurons such as amacrine cells. CC Colocalizes with RGPR in the outer segment of rod photoreceptors and CC cone outer segments. {ECO:0000269|PubMed:10958647, CC ECO:0000269|PubMed:10958648, ECO:0000269|PubMed:12140192}. CC -!- DOMAIN: The C2 domain does not bind calcium ions, and does not bind CC phosphoinositides. {ECO:0000269|PubMed:24981858}. CC -!- DISEASE: Leber congenital amaurosis 6 (LCA6) [MIM:613826]: A severe CC dystrophy of the retina, typically becoming evident in the first years CC of life. Visual function is usually poor and often accompanied by CC nystagmus, sluggish or near-absent pupillary responses, photophobia, CC high hyperopia and keratoconus. {ECO:0000269|PubMed:11528500, CC ECO:0000269|PubMed:17306875, ECO:0000269|PubMed:17554762, CC ECO:0000269|PubMed:18682808, ECO:0000269|PubMed:24981858}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Cone-rod dystrophy 13 (CORD13) [MIM:608194]: An inherited CC retinal dystrophy characterized by retinal pigment deposits visible on CC fundus examination, predominantly in the macular region, and initial CC loss of cone photoreceptors followed by rod degeneration. This leads to CC decreased visual acuity and sensitivity in the central visual field, CC followed by loss of peripheral vision. Severe loss of vision occurs CC earlier than in retinitis pigmentosa, due to cone photoreceptors CC degenerating at a higher rate than rod photoreceptors. CC {ECO:0000269|PubMed:10958648, ECO:0000269|PubMed:12920076}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Note=Heterozygous non-synonymous variants of RPGRIP1 may cause CC or increase the susceptibility to various forms of glaucoma, a CC genetically heterogeneous disorder. It is the second cause of blindness CC worldwide owing to the progressive degeneration of retinal ganglion CC neurons (PubMed:21224891). {ECO:0000269|PubMed:21224891}. CC -!- SIMILARITY: Belongs to the RPGRIP1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAE11866.1; Type=Erroneous initiation; Note=Truncated 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; AF227257; AAG10246.1; -; mRNA. DR EMBL; AF265666; AAG10000.1; -; mRNA. DR EMBL; AF265667; AAG10001.1; -; mRNA. DR EMBL; AF260257; AAF91371.1; -; mRNA. DR EMBL; AJ417048; CAD01136.1; -; Genomic_DNA. DR EMBL; AJ417049; CAD01136.1; JOINED; Genomic_DNA. DR EMBL; AJ417050; CAD01136.1; JOINED; Genomic_DNA. DR EMBL; AJ417051; CAD01136.1; JOINED; Genomic_DNA. DR EMBL; AJ417052; CAD01136.1; JOINED; Genomic_DNA. DR EMBL; AJ417053; CAD01136.1; JOINED; Genomic_DNA. DR EMBL; AJ417054; CAD01136.1; JOINED; Genomic_DNA. DR EMBL; AJ417055; CAD01136.1; JOINED; Genomic_DNA. DR EMBL; AJ417056; CAD01136.1; JOINED; Genomic_DNA. DR EMBL; AJ417057; CAD01136.1; JOINED; Genomic_DNA. DR EMBL; AJ417058; CAD01136.1; JOINED; Genomic_DNA. DR EMBL; AJ417059; CAD01136.1; JOINED; Genomic_DNA. DR EMBL; AJ417060; CAD01136.1; JOINED; Genomic_DNA. DR EMBL; AJ417061; CAD01136.1; JOINED; Genomic_DNA. DR EMBL; AJ417062; CAD01136.1; JOINED; Genomic_DNA. DR EMBL; AJ417063; CAD01136.1; JOINED; Genomic_DNA. DR EMBL; AJ417064; CAD01136.1; JOINED; Genomic_DNA. DR EMBL; AJ417065; CAD01136.1; JOINED; Genomic_DNA. DR EMBL; AJ417066; CAD01136.1; JOINED; Genomic_DNA. DR EMBL; AJ417067; CAD01135.1; -; mRNA. DR EMBL; AL135744; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC039089; AAH39089.1; -; mRNA. DR EMBL; BX571740; CAE11866.1; ALT_INIT; mRNA. DR CCDS; CCDS45080.1; -. [Q96KN7-1] DR CCDS; CCDS91848.1; -. [Q96KN7-4] DR RefSeq; NP_065099.3; NM_020366.3. [Q96KN7-1] DR PDB; 4QAM; X-ray; 1.83 A; B=1091-1286. DR PDBsum; 4QAM; -. DR AlphaFoldDB; Q96KN7; -. DR SMR; Q96KN7; -. DR BioGRID; 121364; 67. DR CORUM; Q96KN7; -. DR IntAct; Q96KN7; 64. DR STRING; 9606.ENSP00000382895; -. DR iPTMnet; Q96KN7; -. DR PhosphoSitePlus; Q96KN7; -. DR BioMuta; RPGRIP1; -. DR DMDM; 296452882; -. DR jPOST; Q96KN7; -. DR MassIVE; Q96KN7; -. DR MaxQB; Q96KN7; -. DR PaxDb; 9606-ENSP00000382895; -. DR PeptideAtlas; Q96KN7; -. DR ProteomicsDB; 77089; -. [Q96KN7-1] DR ProteomicsDB; 77090; -. [Q96KN7-2] DR ProteomicsDB; 77091; -. [Q96KN7-3] DR ProteomicsDB; 77092; -. [Q96KN7-4] DR ProteomicsDB; 77093; -. [Q96KN7-5] DR ProteomicsDB; 77094; -. [Q96KN7-6] DR Antibodypedia; 47230; 112 antibodies from 24 providers. DR DNASU; 57096; -. DR Ensembl; ENST00000382933.8; ENSP00000372391.4; ENSG00000092200.13. [Q96KN7-4] DR Ensembl; ENST00000400017.7; ENSP00000382895.2; ENSG00000092200.13. [Q96KN7-1] DR GeneID; 57096; -. DR KEGG; hsa:57096; -. DR MANE-Select; ENST00000400017.7; ENSP00000382895.2; NM_020366.4; NP_065099.3. DR UCSC; uc001wag.4; human. [Q96KN7-1] DR AGR; HGNC:13436; -. DR CTD; 57096; -. DR DisGeNET; 57096; -. DR GeneCards; RPGRIP1; -. DR HGNC; HGNC:13436; RPGRIP1. DR HPA; ENSG00000092200; Group enriched (retina, testis). DR MalaCards; RPGRIP1; -. DR MIM; 605446; gene. DR MIM; 608194; phenotype. DR MIM; 613826; phenotype. DR neXtProt; NX_Q96KN7; -. DR OpenTargets; ENSG00000092200; -. DR Orphanet; 1872; Cone rod dystrophy. DR Orphanet; 65; Leber congenital amaurosis. DR Orphanet; 564; Meckel syndrome. DR PharmGKB; PA34657; -. DR VEuPathDB; HostDB:ENSG00000092200; -. DR eggNOG; ENOG502R3GU; Eukaryota. DR GeneTree; ENSGT00520000055620; -. DR HOGENOM; CLU_468463_0_0_1; -. DR InParanoid; Q96KN7; -. DR OMA; NTLAAGW; -. DR OrthoDB; 3435286at2759; -. DR PhylomeDB; Q96KN7; -. DR TreeFam; TF328883; -. DR PathwayCommons; Q96KN7; -. DR SignaLink; Q96KN7; -. DR SIGNOR; Q96KN7; -. DR BioGRID-ORCS; 57096; 25 hits in 1146 CRISPR screens. DR ChiTaRS; RPGRIP1; human. DR GeneWiki; RPGRIP1; -. DR GenomeRNAi; 57096; -. DR Pharos; Q96KN7; Tbio. DR PRO; PR:Q96KN7; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q96KN7; Protein. DR Bgee; ENSG00000092200; Expressed in left testis and 115 other cell types or tissues. DR ExpressionAtlas; Q96KN7; baseline and differential. DR GO; GO:0005930; C:axoneme; IEA:Ensembl. DR GO; GO:0035253; C:ciliary rootlet; IEA:Ensembl. DR GO; GO:0032391; C:photoreceptor connecting cilium; ISS:UniProtKB. DR GO; GO:0120206; C:photoreceptor distal connecting cilium; IEA:Ensembl. DR GO; GO:0031870; F:thromboxane A2 receptor binding; IBA:GO_Central. DR GO; GO:0061351; P:neural precursor cell proliferation; IEA:Ensembl. DR GO; GO:1905515; P:non-motile cilium assembly; IBA:GO_Central. DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW. DR GO; GO:0046548; P:retinal rod cell development; IBA:GO_Central. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR CDD; cd00030; C2; 1. DR Gene3D; 2.60.40.150; C2 domain; 3. DR InterPro; IPR021656; C2-C2_1. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR041091; RPGRIP1_C. DR InterPro; IPR031139; RPGRIP1_fam. DR PANTHER; PTHR14240; RETINITIS PIGMENTOSA GTPASE REGULATOR-INTERACTING PROTEIN; 1. DR PANTHER; PTHR14240:SF3; X-LINKED RETINITIS PIGMENTOSA GTPASE REGULATOR-INTERACTING PROTEIN 1; 1. DR Pfam; PF00168; C2; 1. DR Pfam; PF11618; C2-C2_1; 1. DR Pfam; PF18111; RPGR1_C; 1. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2. DR PROSITE; PS50004; C2; 1. DR Genevisible; Q96KN7; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell projection; Ciliopathy; Cilium; KW Coiled coil; Cone-rod dystrophy; Disease variant; Glaucoma; KW Leber congenital amaurosis; Reference proteome; Sensory transduction; KW Vision. FT CHAIN 1..1286 FT /note="X-linked retinitis pigmentosa GTPase regulator- FT interacting protein 1" FT /id="PRO_0000097432" FT DOMAIN 781..906 FT /note="C2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT REGION 144..193 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 934..1008 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1058..1108 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1091..1281 FT /note="Interaction with RPGR" FT /evidence="ECO:0000269|PubMed:24981858" FT COILED 294..584 FT /evidence="ECO:0000255" FT COMPBIAS 939..956 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 978..1001 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1058..1087 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1088..1102 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 1..641 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:10958648" FT /id="VSP_009522" FT VAR_SEQ 1..617 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10958648" FT /id="VSP_009521" FT VAR_SEQ 1..384 FT /note="Missing (in isoform 5 and isoform 6)" FT /evidence="ECO:0000303|PubMed:10958647" FT /id="VSP_009520" FT VAR_SEQ 1..358 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_009519" FT VAR_SEQ 359..383 FT /note="EFQERVEDLEKERKLLNDNYDKLLE -> MLKLDNKDVISHPLGYPSESLLS FT IA (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_009523" FT VAR_SEQ 588..903 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_009524" FT VAR_SEQ 618..623 FT /note="ISLLHQ -> MTFQHL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10958648" FT /id="VSP_009525" FT VAR_SEQ 642..673 FT /note="LAQAGDTQPTTFCTYSFYDFETHCTPLSVGPQ -> MLLMAPDRCRYVWKHC FT QPMEMRIKWIFLCCIR (in isoform 3)" FT /evidence="ECO:0000303|PubMed:10958648" FT /id="VSP_009526" FT VAR_SEQ 966..1286 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:10958647" FT /id="VSP_009527" FT VARIANT 32 FT /note="M -> L" FT /evidence="ECO:0000269|PubMed:21224891" FT /id="VAR_065720" FT VARIANT 96 FT /note="P -> Q (in dbSNP:rs1040904)" FT /evidence="ECO:0000269|PubMed:18682808" FT /id="VAR_057772" FT VARIANT 135 FT /note="S -> R" FT /evidence="ECO:0000269|PubMed:21224891" FT /id="VAR_065721" FT VARIANT 192 FT /note="K -> E (in dbSNP:rs6571751)" FT /evidence="ECO:0000269|PubMed:18682808" FT /id="VAR_017830" FT VARIANT 318 FT /note="A -> V (in a patient with primary open angle FT glaucoma; dbSNP:rs1325466987)" FT /evidence="ECO:0000269|PubMed:21224891" FT /id="VAR_065722" FT VARIANT 363 FT /note="R -> T (in a patient with normal tension glaucoma)" FT /evidence="ECO:0000269|PubMed:21224891" FT /id="VAR_065723" FT VARIANT 432 FT /note="S -> F (found in a patient with LCA6; FT dbSNP:rs190985984)" FT /evidence="ECO:0000269|PubMed:18682808" FT /id="VAR_067184" FT VARIANT 547 FT /note="A -> S (in CORD13; dbSNP:rs10151259)" FT /evidence="ECO:0000269|PubMed:10958648, FT ECO:0000269|PubMed:12920076" FT /id="VAR_017831" FT VARIANT 585 FT /note="P -> S (in dbSNP:rs147586703)" FT /evidence="ECO:0000269|PubMed:21224891" FT /id="VAR_065724" FT VARIANT 589 FT /note="Q -> H (does not affect the interaction with NPHP4; FT dbSNP:rs34067949)" FT /evidence="ECO:0000269|PubMed:21224891" FT /id="VAR_065725" FT VARIANT 598 FT /note="R -> Q (found in patients with primary open angle FT glaucoma and juvenile open angle glaucoma; affects the FT interaction with NPHP4; dbSNP:rs74034910)" FT /evidence="ECO:0000269|PubMed:21224891" FT /id="VAR_065726" FT VARIANT 601 FT /note="S -> L (in dbSNP:rs3748360)" FT /id="VAR_017832" FT VARIANT 601 FT /note="S -> W (found in a patient with LCA6; FT dbSNP:rs3748360)" FT /evidence="ECO:0000269|PubMed:18682808" FT /id="VAR_067185" FT VARIANT 603 FT /note="C -> S" FT /evidence="ECO:0000269|PubMed:21224891" FT /id="VAR_065727" FT VARIANT 631 FT /note="H -> P (in LCA6)" FT /evidence="ECO:0000269|PubMed:18682808" FT /id="VAR_067186" FT VARIANT 635 FT /note="A -> G (in a patient with normal tension glaucoma FT and a patient with primary open angle glaucoma; affects the FT interaction with NPHP4; dbSNP:rs200325360)" FT /evidence="ECO:0000269|PubMed:21224891" FT /id="VAR_065728" FT VARIANT 638 FT /note="T -> I (in dbSNP:rs1010290273)" FT /evidence="ECO:0000269|PubMed:21224891" FT /id="VAR_065729" FT VARIANT 746 FT /note="G -> E (in LCA6; dbSNP:rs61751268)" FT /evidence="ECO:0000269|PubMed:11528500" FT /id="VAR_017833" FT VARIANT 764 FT /note="A -> V (does not affect the interaction with NPHP4; FT dbSNP:rs758652031)" FT /evidence="ECO:0000269|PubMed:21224891" FT /id="VAR_065730" FT VARIANT 806 FT /note="T -> I (in a patient with primary open angle FT glaucoma who also carries variant K-352 in MYOC; affects FT the interaction with NPHP4; dbSNP:rs142796310)" FT /evidence="ECO:0000269|PubMed:21224891" FT /id="VAR_065731" FT VARIANT 812 FT /note="R -> H (does not affect the interaction with NPHP4)" FT /evidence="ECO:0000269|PubMed:21224891" FT /id="VAR_065732" FT VARIANT 814 FT /note="R -> L (in dbSNP:rs372647080)" FT /evidence="ECO:0000269|PubMed:21224891" FT /id="VAR_065733" FT VARIANT 827 FT /note="R -> L (in CORD13; dbSNP:rs28937883)" FT /evidence="ECO:0000269|PubMed:12920076" FT /id="VAR_017834" FT VARIANT 837 FT /note="A -> G (in a patient with primary open angle FT glaucoma and a patient with juvenile open angle glaucoma; FT affects the interaction with NPHP4; dbSNP:rs373515194)" FT /evidence="ECO:0000269|PubMed:21224891" FT /id="VAR_065734" FT VARIANT 838 FT /note="I -> V (in a patient with normal tension glaucoma FT and a patient with primary open angle glaucoma; affects the FT interaction with NPHP4; dbSNP:rs772480252)" FT /evidence="ECO:0000269|PubMed:21224891" FT /id="VAR_065735" FT VARIANT 841 FT /note="A -> T" FT /evidence="ECO:0000269|PubMed:21224891" FT /id="VAR_065736" FT VARIANT 852 FT /note="R -> Q (in dbSNP:rs181758389)" FT /evidence="ECO:0000269|PubMed:21224891" FT /id="VAR_065737" FT VARIANT 876 FT /note="D -> G (impairs interaction with NPHP4; FT dbSNP:rs61751274)" FT /evidence="ECO:0000269|PubMed:16339905" FT /id="VAR_076792" FT VARIANT 883 FT /note="G -> D" FT /evidence="ECO:0000269|PubMed:21224891" FT /id="VAR_065738" FT VARIANT 960 FT /note="A -> P (in dbSNP:rs35810926)" FT /id="VAR_057773" FT VARIANT 1033 FT /note="E -> Q (in dbSNP:rs3748361)" FT /evidence="ECO:0000269|PubMed:10958647, FT ECO:0000269|PubMed:11528500, ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:18682808" FT /id="VAR_017835" FT VARIANT 1057 FT /note="H -> L (found in a patient associated with LCA6; FT dbSNP:rs201521970)" FT /evidence="ECO:0000269|PubMed:18682808" FT /id="VAR_067187" FT VARIANT 1114 FT /note="D -> G (in LCA6; no effect on interaction with RPGR; FT dbSNP:rs17103671)" FT /evidence="ECO:0000269|PubMed:11528500, FT ECO:0000269|PubMed:24981858" FT /id="VAR_017836" FT VARIANT 1130 FT /note="E -> Q (found in a patient with LCA6)" FT /evidence="ECO:0000269|PubMed:21602930" FT /id="VAR_067188" FT VARIANT 1211 FT /note="V -> E (in LCA6)" FT /evidence="ECO:0000269|PubMed:17306875, FT ECO:0000269|PubMed:17554762" FT /id="VAR_076823" FT VARIANT 1240 FT /note="G -> E (in dbSNP:rs34725281)" FT /id="VAR_057774" FT MUTAGEN 1121 FT /note="E->A: Nearly abolishes interaction with RPGR; when FT associated with A-1174 and A-1245." FT /evidence="ECO:0000269|PubMed:24981858" FT MUTAGEN 1121 FT /note="E->K: Decreases interaction with RPGR." FT /evidence="ECO:0000269|PubMed:24981858" FT MUTAGEN 1174 FT /note="H->A: Nearly abolishes interaction with RPGR; when FT associated with A-1121 and A-1245." FT /evidence="ECO:0000269|PubMed:24981858" FT MUTAGEN 1174 FT /note="H->D: Abolishes interaction with RPGR." FT /evidence="ECO:0000269|PubMed:24981858" FT MUTAGEN 1245 FT /note="E->A: Nearly abolishes interaction with RPGR; when FT associated with A-1121 and A-1174." FT /evidence="ECO:0000269|PubMed:24981858" FT MUTAGEN 1245 FT /note="E->K: No effect on interaction with RPGR." FT /evidence="ECO:0000269|PubMed:24981858" FT CONFLICT 539 FT /note="Missing (in Ref. 1; AAG10246)" FT /evidence="ECO:0000305" FT CONFLICT 554..555 FT /note="HK -> SQR (in Ref. 1; AAG10246)" FT /evidence="ECO:0000305" FT CONFLICT 611 FT /note="G -> R (in Ref. 6; CAE11866)" FT /evidence="ECO:0000305" FT CONFLICT 1159 FT /note="P -> L (in Ref. 6; CAE11866)" FT /evidence="ECO:0000305" FT STRAND 1117..1127 FT /evidence="ECO:0007829|PDB:4QAM" FT HELIX 1132..1135 FT /evidence="ECO:0007829|PDB:4QAM" FT STRAND 1141..1145 FT /evidence="ECO:0007829|PDB:4QAM" FT HELIX 1153..1156 FT /evidence="ECO:0007829|PDB:4QAM" FT STRAND 1171..1180 FT /evidence="ECO:0007829|PDB:4QAM" FT TURN 1183..1185 FT /evidence="ECO:0007829|PDB:4QAM" FT HELIX 1187..1197 FT /evidence="ECO:0007829|PDB:4QAM" FT STRAND 1204..1213 FT /evidence="ECO:0007829|PDB:4QAM" FT HELIX 1220..1222 FT /evidence="ECO:0007829|PDB:4QAM" FT STRAND 1224..1232 FT /evidence="ECO:0007829|PDB:4QAM" FT HELIX 1233..1239 FT /evidence="ECO:0007829|PDB:4QAM" FT STRAND 1246..1251 FT /evidence="ECO:0007829|PDB:4QAM" FT TURN 1253..1255 FT /evidence="ECO:0007829|PDB:4QAM" FT STRAND 1258..1268 FT /evidence="ECO:0007829|PDB:4QAM" FT HELIX 1270..1282 FT /evidence="ECO:0007829|PDB:4QAM" SQ SEQUENCE 1286 AA; 146682 MW; 00AC1C2A0AC82253 CRC64; MSHLVDPTSG DLPVRDIDAI PLVLPASKGK NMKTQPPLSR MNREELEDSF FRLREDHMLV KELSWKQQDE IKRLRTTLLR LTAAGRDLRV AEEAAPLSET ARRGQKAGWR QRLSMHQRPQ MHRLQGHFHC VGPASPRRAQ PRVQVGHRQL HTAGAPVPEK PKRGPRDRLS YTAPPSFKEH ATNENRGEVA SKPSELVSGS NSIISFSSVI SMAKPIGLCM PNSAHIMASN TMQVEEPPKS PEKMWPKDEN FEQRSSLECA QKAAELRASI KEKVELIRLK KLLHERNASL VMTKAQLTEV QEAYETLLQK NQGILSAAHE ALLKQVNELR AELKEESKKA VSLKSQLEDV SILQMTLKEF QERVEDLEKE RKLLNDNYDK LLESMLDSSD SSSQPHWSNE LIAEQLQQQV SQLQDQLDAE LEDKRKVLLE LSREKAQNED LKLEVTNILQ KHKQEVELLQ NAATISQPPD RQSEPATHPA VLQENTQIEP SEPKNQEEKK LSQVLNELQV SHAETTLELE KTRDMLILQR KINVCYQEEL EAMMTKADND NRDHKEKLER LTRLLDLKNN RIKQLEGILR SHDLPTSEQL KDVAYGTRPL SLCLETLPAH GDEDKVDISL LHQGENLFEL HIHQAFLTSA ALAQAGDTQP TTFCTYSFYD FETHCTPLSV GPQPLYDFTS QYVMETDSLF LHYLQEASAR LDIHQAMASE HSTLAAGWIC FDRVLETVEK VHGLATLIGA GGEEFGVLEY WMRLRFPIKP SLQACNKRKK AQVYLSTDVL GGRKAQEEEF RSESWEPQNE LWIEITKCCG LRSRWLGTQP SPYAVYRFFT FSDHDTAIIP ASNNPYFRDQ ARFPVLVTSD LDHYLRREAL SIHVFDDEDL EPGSYLGRAR VPLLPLAKNE SIKGDFNLTD PAEKPNGSIQ VQLDWKFPYI PPESFLKPEA QTKGKDTKDS SKISSEEEKA SFPSQDQMAS PEVPIEAGQY RSKRKPPHGG ERKEKEHQVV SYSRRKHGKR IGVQGKNRME YLSLNILNGN TPEQVNYTEW KFSETNSFIG DGFKNQHEEE EMTLSHSALK QKEPLHPVND KESSEQGSEV SEAQTTDSDD VIVPPMSQKY PKADSEKMCI EIVSLAFYPE AEVMSDENIK QVYVEYKFYD LPLSETETPV SLRKPRAGEE IHFHFSKVID LDPQEQQGRR RFLFDMLNGQ DPDQGHLKFT VVSDPLDEEK KECEEVGYAY LQLWQILESG RDILEQELDI VSPEDLATPI GRLKVSLQAA AVLHAIYKEM TEDLFS //