RPGR1_HUMAN
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 03-AUG-2022, entry version 178.
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 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; 65.
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; Q96KN7; -.
DR PeptideAtlas; Q96KN7; -.
DR PRIDE; 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; 101 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 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; 152378at2759; -.
DR PhylomeDB; Q96KN7; -.
DR TreeFam; TF328883; -.
DR PathwayCommons; Q96KN7; -.
DR SignaLink; Q96KN7; -.
DR SIGNOR; Q96KN7; -.
DR BioGRID-ORCS; 57096; 24 hits in 1067 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 113 other tissues.
DR ExpressionAtlas; Q96KN7; baseline and differential.
DR Genevisible; Q96KN7; HS.
DR GO; GO:0005930; C:axoneme; IEA:Ensembl.
DR GO; GO:0035869; C:ciliary transition zone; IBA:GO_Central.
DR GO; GO:0032391; C:photoreceptor connecting cilium; ISS:UniProtKB.
DR GO; GO:0120206; C:photoreceptor distal connecting cilium; IEA:Ensembl.
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 Gene3D; 2.60.40.150; -; 3.
DR InterPro; IPR021656; C2-C2_1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR031134; RPGRIP1.
DR InterPro; IPR041091; RPGRIP1_C.
DR InterPro; IPR031139; RPGRIP1_fam.
DR PANTHER; PTHR14240; PTHR14240; 1.
DR PANTHER; PTHR14240:SF3; PTHR14240:SF3; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF11618; C2-C2_1; 1.
DR Pfam; PF18111; RPGR1_C; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 1.
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
