ID FTM_HUMAN Reviewed; 1315 AA. AC Q68CZ1; A0PJ88; Q9Y2K8; DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 27-MAR-2024, entry version 163. DE RecName: Full=Protein fantom; DE AltName: Full=Nephrocystin-8; DE AltName: Full=RPGR-interacting protein 1-like protein; DE Short=RPGRIP1-like protein; GN Name=RPGRIP1L; Synonyms=FTM, KIAA1005, NPHP8; 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 [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Endometrial adenocarcinoma; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-351 (ISOFORMS 1/2). RC TISSUE=Testis; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 181-1315 (ISOFORM 2). RC TISSUE=Brain; RX PubMed=10231032; DOI=10.1093/dnares/6.1.63; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:63-70(1999). RN [5] RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INVOLVEMENT IN MKS5, VARIANTS RP JBTS7 PRO-615; ILE-677 AND PRO-695, AND CHARACTERIZATION OF VARIANTS JBTS7 RP PRO-615; ILE-677 AND PRO-695. RX PubMed=17558409; DOI=10.1038/ng2039; RA Delous M., Baala L., Salomon R., Laclef C., Vierkotten J., Tory K., RA Golzio C., Lacoste T., Besse L., Ozilou C., Moutkine I., Hellman N.E., RA Anselme I., Silbermann F., Vesque C., Gerhardt C., Rattenberry E., RA Wolf M.T.F., Gubler M.C., Martinovic J., Encha-Razavi F., Boddaert N., RA Gonzales M., Macher M.A., Nivet H., Champion G., Bertheleme J.P., RA Niaudet P., McDonald F., Hildebrandt F., Johnson C.A., Vekemans M., RA Antignac C., Ruether U., Schneider-Maunoury S., Attie-Bitach T., RA Saunier S.; RT "The ciliary gene RPGRIP1L is mutated in cerebello-oculo-renal syndrome RT (Joubert syndrome type B) and Meckel syndrome."; RL Nat. Genet. 39:875-881(2007). RN [6] RP INTERACTION WITH NPHP4, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT RP JBTS7 PRO-615, AND CHARACTERIZATION OF VARIANT JBTS7 PRO-615. RX PubMed=17558407; DOI=10.1038/ng2069; RA Arts H.H., Doherty D., van Beersum S.E.C., Parisi M.A., Letteboer S.J.F., RA Gorden N.T., Peters T.A., Maerker T., Voesenek K., Kartono A., Ozyurek H., RA Farin F.M., Kroes H.Y., Wolfrum U., Brunner H.G., Cremers F.P.M., RA Glass I.A., Knoers N.V.A.M., Roepman R.; RT "Mutations in the gene encoding the basal body protein RPGRIP1L, a RT nephrocystin-4 interactor, cause Joubert syndrome."; RL Nat. Genet. 39:882-888(2007). RN [7] RP TISSUE SPECIFICITY. RX PubMed=17434869; DOI=10.1126/science.1141634; RA Frayling T.M., Timpson N.J., Weedon M.N., Zeggini E., Freathy R.M., RA Lindgren C.M., Perry J.R., Elliott K.S., Lango H., Rayner N.W., Shields B., RA Harries L.W., Barrett J.C., Ellard S., Groves C.J., Knight B., Patch A.M., RA Ness A.R., Ebrahim S., Lawlor D.A., Ring S.M., Ben-Shlomo Y., RA Jarvelin M.-R., Sovio U., Bennett A.J., Melzer D., Ferrucci L., Loos R.J., RA Barroso I., Wareham N.J., Karpe F., Owen K.R., Cardon L.R., Walker M., RA Hitman G.A., Palmer C.N., Doney A.S., Morris A.D., Davey-Smith G., RA Hattersley A.T., McCarthy M.I.; RT "A common variant in the FTO gene is associated with body mass index and RT predisposes to childhood and adult obesity."; RL Science 316:889-894(2007). RN [8] RP INTERACTION WITH RPGR, VARIANTS GLY-199; THR-229; SER-447; PHE-546; RP ILE-647; ILE-677; LEU-937; SER-1025; GLY-1183; ASN-1264 AND TYR-1264, RP VARIANT MKS5 CYS-1236, CHARACTERIZATION OF VARIANT THR-229, AND ASSOCIATION RP OF VARIANT THR-229 WITH RETINAL DEGENERATION IN CILIOPATHIES. 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 [9] RP FUNCTION, INTERACTION WITH TBXA2R, AND TISSUE SPECIFICITY. RX PubMed=19464661; DOI=10.1016/j.prostaglandins.2009.02.001; RA Tokue S., Sasaki M., Nakahata N.; RT "Thromboxane A2-induced signal transduction is negatively regulated by RT KIAA1005 that directly interacts with thromboxane A2 receptor."; RL Prostaglandins Other Lipid Mediat. 89:8-15(2009). RN [10] RP FUNCTION. RX PubMed=21565611; DOI=10.1016/j.cell.2011.04.019; RA Sang L., Miller J.J., Corbit K.C., Giles R.H., Brauer M.J., Otto E.A., RA Baye L.M., Wen X., Scales S.J., Kwong M., Huntzicker E.G., Sfakianos M.K., RA Sandoval W., Bazan J.F., Kulkarni P., Garcia-Gonzalo F.R., Seol A.D., RA O'Toole J.F., Held S., Reutter H.M., Lane W.S., Rafiq M.A., Noor A., RA Ansar M., Devi A.R., Sheffield V.C., Slusarski D.C., Vincent J.B., RA Doherty D.A., Hildebrandt F., Reiter J.F., Jackson P.K.; RT "Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy disease genes RT and pathways."; RL Cell 145:513-528(2011). RN [11] RP SUBCELLULAR LOCATION, AND INTERACTION WITH RPGR AND NEK4. 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 INVOLVEMENT IN CILIOPATHIES, AND VARIANT GLY-1183. RX PubMed=21258341; DOI=10.1038/ng.756; RA Davis E.E., Zhang Q., Liu Q., Diplas B.H., Davey L.M., Hartley J., RA Stoetzel C., Szymanska K., Ramaswami G., Logan C.V., Muzny D.M., RA Young A.C., Wheeler D.A., Cruz P., Morgan M., Lewis L.R., Cherukuri P., RA Maskeri B., Hansen N.F., Mullikin J.C., Blakesley R.W., Bouffard G.G., RA Gyapay G., Rieger S., Tonshoff B., Kern I., Soliman N.A., Neuhaus T.J., RA Swoboda K.J., Kayserili H., Gallagher T.E., Lewis R.A., Bergmann C., RA Otto E.A., Saunier S., Scambler P.J., Beales P.L., Gleeson J.G., RA Maher E.R., Attie-Bitach T., Dollfus H., Johnson C.A., Green E.D., RA Gibbs R.A., Hildebrandt F., Pierce E.A., Katsanis N.; RT "TTC21B contributes both causal and modifying alleles across the ciliopathy RT spectrum."; RL Nat. Genet. 43:189-196(2011). RN [13] RP INTERACTION WITH INVS; NPHP4 AND DVL2. RX PubMed=22927466; DOI=10.1083/jcb.201111009; RA Mahuzier A., Gaude H.M., Grampa V., Anselme I., Silbermann F., RA Leroux-Berger M., Delacour D., Ezan J., Montcouquiol M., Saunier S., RA Schneider-Maunoury S., Vesque C.; RT "Dishevelled stabilization by the ciliopathy protein Rpgrip1l is essential RT for planar cell polarity."; RL J. Cell Biol. 198:927-940(2012). RN [14] RP STRUCTURE BY NMR OF 595-737. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the first C2 domain from human KIAA1005 protein."; RL Submitted (OCT-2007) to the PDB data bank. RN [15] RP VARIANTS JBTS7 LYS-393; PRO-615 AND ARG-633. RX PubMed=17960139; DOI=10.1038/sj.ki.5002630; RA Wolf M.T., Saunier S., O'Toole J.F., Wanner N., Groshong T., Attanasio M., RA Salomon R., Stallmach T., Sayer J.A., Waldherr R., Griebel M., Oh J., RA Neuhaus T.J., Josefiak U., Antignac C., Otto E.A., Hildebrandt F.; RT "Mutational analysis of the RPGRIP1L gene in patients with Joubert syndrome RT and nephronophthisis."; RL Kidney Int. 72:1520-1526(2007). RN [16] RP VARIANT COACH3 PRO-659. RX PubMed=19574260; DOI=10.1136/jmg.2009.067249; RA Doherty D., Parisi M.A., Finn L.S., Gunay-Aygun M., Al-Mateen M., Bates D., RA Clericuzio C., Demir H., Dorschner M., van Essen A.J., Gahl W.A., RA Gentile M., Gorden N.T., Hikida A., Knutzen D., Ozyurek H., Phelps I., RA Rosenthal P., Verloes A., Weigand H., Chance P.F., Dobyns W.B., Glass I.A.; RT "Mutations in 3 genes (MKS3, CC2D2A and RPGRIP1L) cause COACH syndrome RT (Joubert syndrome with congenital hepatic fibrosis)."; RL J. Med. Genet. 47:8-21(2010). RN [17] RP VARIANT JBTS7 ARG-550. RX PubMed=22693042; DOI=10.1002/humu.22134; RA Alazami A.M., Alshammari M.J., Salih M.A., Alzahrani F., Hijazi H., RA Seidahmed M.Z., Abu Safieh L., Aldosary M., Khan A.O., Alkuraya F.S.; RT "Molecular characterization of Joubert syndrome in Saudi Arabia."; RL Hum. Mutat. 33:1423-1428(2012). CC -!- FUNCTION: Negatively regulates signaling through the G-protein coupled CC thromboxane A2 receptor (TBXA2R) (PubMed:19464661). May be involved in CC mechanisms like programmed cell death, craniofacial development, CC patterning of the limbs, and formation of the left-right axis (By CC similarity). Involved in the organization of apical junctions; the CC function is proposed to implicate a NPHP1-4-8 module. Does not seem to CC be strictly required for ciliogenesis (PubMed:19464661). Involved in CC establishment of planar cell polarity such as in cochlear sensory CC epithelium and is proposed to implicate stabilization of disheveled CC proteins (By similarity). Involved in regulation of proteasomal CC activity at the primary cilium probably implicating association with CC PSDM2 (By similarity). {ECO:0000250|UniProtKB:Q8CG73, CC ECO:0000269|PubMed:19464661}. CC -!- SUBUNIT: Interacts with NPHP4 and NPHP1; NPHP1, NPHP4 and RPGRIP1L are CC proposed to form a functional NPHP1-4-8 module localized to cell-cell CC contacts and the ciliary transition zone; NPHP4 mediates the CC interaction between NPHP1 and RPGRIP1L. Interacts with IQCB1; the CC interaction likely requires additional interactors (By similarity). CC Interacts with TBXA2R (via C-terminus). Interacts with RPGR. Interacts CC with NEK4. Interacts with NPHP4, INVS and DVL2; the complex is proposed CC to be involved in DVL2 stabilization. {ECO:0000250|UniProtKB:Q8CG73, CC ECO:0000269|PubMed:17558407, ECO:0000269|PubMed:19430481, CC ECO:0000269|PubMed:19464661, ECO:0000269|PubMed:22927466}. CC -!- INTERACTION: CC Q68CZ1; Q9R0X5: Rpgr; Xeno; NbExp=3; IntAct=EBI-5235485, EBI-6915619; CC Q68CZ1-2; O75161: NPHP4; NbExp=8; IntAct=EBI-9356215, EBI-4281852; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, cilium basal CC body {ECO:0000250|UniProtKB:Q8CG73, ECO:0000269|PubMed:21685204}. CC Cytoplasm, cytoskeleton, cilium axoneme. Cytoplasm, cytoskeleton, CC microtubule organizing center, centrosome CC {ECO:0000250|UniProtKB:Q8CG73}. Cell junction, tight junction CC {ECO:0000250|UniProtKB:Q8CG73}. Note=In cultured renal cells, it CC localizes diffusely in the cytoplasm but, as cells approach confluence, CC it accumulates to basolateral tight junctions. Localizes to the ciliary CC transition zone. {ECO:0000250|UniProtKB:Q8CG73}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q68CZ1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q68CZ1-2; Sequence=VSP_026161, VSP_026162; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with relatively high level CC of expression in hypothalamus and islet. During early development, CC expressed in multiple organs including brain, eye, forelimb and kidney. CC {ECO:0000269|PubMed:17434869, ECO:0000269|PubMed:17558407, CC ECO:0000269|PubMed:17558409, ECO:0000269|PubMed:19464661}. CC -!- DISEASE: Note=Ciliary dysfunction leads to a broad spectrum of CC disorders, collectively termed ciliopathies. Overlapping clinical CC features include retinal degeneration, renal cystic disease, skeletal CC abnormalities, fibrosis of various organ, and a complex range of CC anatomical and functional defects of the central and peripheral nervous CC system. The ciliopathy range of diseases includes Meckel-Gruber CC syndrome, Bardet-Biedl syndrome, Joubert syndrome, nephronophtisis, CC Senior-Loken syndrome, and Jeune asphyxiating thoracic dystrophy among CC others. Single-locus allelism is insufficient to explain the variable CC penetrance and expressivity of such disorders, leading to the CC suggestion that variations across multiple sites of the ciliary CC proteome, including RPGRIP1L, influence the clinical outcome. CC {ECO:0000269|PubMed:19430481, ECO:0000269|PubMed:21258341}. CC -!- DISEASE: Joubert syndrome 7 (JBTS7) [MIM:611560]: A disorder presenting CC with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal CC breathing abnormalities and psychomotor delay. Neuroradiologically, it CC is characterized by cerebellar vermian hypoplasia/aplasia, thickened CC and reoriented superior cerebellar peduncles, and an abnormally large CC interpeduncular fossa, giving the appearance of a molar tooth on CC transaxial slices (molar tooth sign). Additional variable features CC include retinal dystrophy and renal disease. CC {ECO:0000269|PubMed:17558407, ECO:0000269|PubMed:17558409, CC ECO:0000269|PubMed:17960139, ECO:0000269|PubMed:22693042}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Meckel syndrome 5 (MKS5) [MIM:611561]: A disorder CC characterized by a combination of renal cysts and variably associated CC features including developmental anomalies of the central nervous CC system (typically encephalocele), hepatic ductal dysplasia and cysts, CC and polydactyly. {ECO:0000269|PubMed:17558409, CC ECO:0000269|PubMed:19430481}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: COACH syndrome 3 (COACH3) [MIM:619113]: A form of COACH CC syndrome, a disorder characterized by cerebellar vermis hypoplasia, CC developmental delay, impaired intellectual development, ataxia, and CC hepatic fibrosis. Patients present the molar tooth sign, a midbrain- CC hindbrain malformation pathognomonic for Joubert syndrome and related CC disorders. Other features, such as coloboma and renal cysts, may be CC variable. COACH3 inheritance is autosomal recessive. CC {ECO:0000269|PubMed:19574260}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the RPGRIP1 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=RPGRIP1-like (RPGRIP1L); Note=Leiden Open Variation CC Database (LOVD); CC URL="https://databases.lovd.nl/shared/genes/RPGRIP1L"; 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; CR749645; CAH18439.1; -; mRNA. DR EMBL; AC007497; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC007909; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC084795; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC017977; AAH17977.1; ALT_TERM; mRNA. DR EMBL; AB023222; BAA76849.1; -; mRNA. DR CCDS; CCDS32447.1; -. [Q68CZ1-1] DR CCDS; CCDS45486.1; -. [Q68CZ1-2] DR RefSeq; NP_001121369.1; NM_001127897.3. [Q68CZ1-2] DR RefSeq; NP_056087.2; NM_015272.4. [Q68CZ1-1] DR PDB; 2YRB; NMR; -; A=595-737. DR PDBsum; 2YRB; -. DR AlphaFoldDB; Q68CZ1; -. DR SMR; Q68CZ1; -. DR BioGRID; 116911; 187. DR ComplexPortal; CPX-2806; NPHP transition zone complex. DR CORUM; Q68CZ1; -. DR IntAct; Q68CZ1; 158. DR MINT; Q68CZ1; -. DR STRING; 9606.ENSP00000493946; -. DR GlyGen; Q68CZ1; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q68CZ1; -. DR PhosphoSitePlus; Q68CZ1; -. DR BioMuta; RPGRIP1L; -. DR DMDM; 296434514; -. DR EPD; Q68CZ1; -. DR jPOST; Q68CZ1; -. DR MassIVE; Q68CZ1; -. DR MaxQB; Q68CZ1; -. DR PaxDb; 9606-ENSP00000369257; -. DR PeptideAtlas; Q68CZ1; -. DR ProteomicsDB; 66034; -. [Q68CZ1-1] DR ProteomicsDB; 66035; -. [Q68CZ1-2] DR Pumba; Q68CZ1; -. DR Antibodypedia; 28413; 132 antibodies from 28 providers. DR DNASU; 23322; -. DR Ensembl; ENST00000262135.9; ENSP00000262135.4; ENSG00000103494.16. [Q68CZ1-2] DR Ensembl; ENST00000647211.2; ENSP00000493946.1; ENSG00000103494.16. [Q68CZ1-1] DR GeneID; 23322; -. DR KEGG; hsa:23322; -. DR MANE-Select; ENST00000647211.2; ENSP00000493946.1; NM_015272.5; NP_056087.2. DR UCSC; uc002eho.5; human. [Q68CZ1-1] DR AGR; HGNC:29168; -. DR CTD; 23322; -. DR DisGeNET; 23322; -. DR GeneCards; RPGRIP1L; -. DR GeneReviews; RPGRIP1L; -. DR HGNC; HGNC:29168; RPGRIP1L. DR HPA; ENSG00000103494; Tissue enhanced (testis). DR MalaCards; RPGRIP1L; -. DR MIM; 610937; gene. DR MIM; 611560; phenotype. DR MIM; 611561; phenotype. DR MIM; 619113; phenotype. DR neXtProt; NX_Q68CZ1; -. DR OpenTargets; ENSG00000103494; -. DR Orphanet; 1454; Joubert syndrome with hepatic defect. DR Orphanet; 220497; Joubert syndrome with renal defect. DR Orphanet; 564; Meckel syndrome. DR PharmGKB; PA162401983; -. DR VEuPathDB; HostDB:ENSG00000103494; -. DR eggNOG; ENOG502QSQG; Eukaryota. DR GeneTree; ENSGT00520000055620; -. DR HOGENOM; CLU_002108_0_0_1; -. DR InParanoid; Q68CZ1; -. DR OMA; IEMYRPA; -. DR OrthoDB; 3435286at2759; -. DR PhylomeDB; Q68CZ1; -. DR TreeFam; TF328883; -. DR PathwayCommons; Q68CZ1; -. DR Reactome; R-HSA-5610787; Hedgehog 'off' state. DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane. DR SignaLink; Q68CZ1; -. DR SIGNOR; Q68CZ1; -. DR BioGRID-ORCS; 23322; 32 hits in 1149 CRISPR screens. DR ChiTaRS; RPGRIP1L; human. DR EvolutionaryTrace; Q68CZ1; -. DR GenomeRNAi; 23322; -. DR Pharos; Q68CZ1; Tbio. DR PRO; PR:Q68CZ1; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q68CZ1; Protein. DR Bgee; ENSG00000103494; Expressed in bronchial epithelial cell and 133 other cell types or tissues. DR ExpressionAtlas; Q68CZ1; baseline and differential. DR GO; GO:0005879; C:axonemal microtubule; IEA:Ensembl. DR GO; GO:0005930; C:axoneme; IDA:MGI. DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell. DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0036064; C:ciliary basal body; IDA:MGI. DR GO; GO:0035253; C:ciliary rootlet; IEA:Ensembl. DR GO; GO:0035869; C:ciliary transition zone; IDA:WormBase. DR GO; GO:0005929; C:cilium; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0032391; C:photoreceptor connecting cilium; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0031870; F:thromboxane A2 receptor binding; IPI:UniProtKB. DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl. DR GO; GO:0090102; P:cochlea development; IEA:Ensembl. DR GO; GO:0022038; P:corpus callosum development; IEA:Ensembl. DR GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl. DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl. DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl. DR GO; GO:0001736; P:establishment of planar polarity; IEA:Ensembl. DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:Ensembl. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0001822; P:kidney development; IEA:Ensembl. DR GO; GO:0021670; P:lateral ventricle development; IEA:Ensembl. DR GO; GO:0001889; P:liver development; IEA:Ensembl. DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0021532; P:neural tube patterning; IEA:Ensembl. DR GO; GO:1905515; P:non-motile cilium assembly; IBA:GO_Central. DR GO; GO:0043584; P:nose development; IEA:Ensembl. DR GO; GO:0021772; P:olfactory bulb development; IEA:Ensembl. DR GO; GO:0060039; P:pericardium development; IEA:Ensembl. DR GO; GO:0008589; P:regulation of smoothened signaling pathway; IEA:Ensembl. DR GO; GO:0046548; P:retinal rod cell development; IBA:GO_Central. 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:SF4; PROTEIN FANTOM; 1. DR PANTHER; PTHR14240; RETINITIS PIGMENTOSA GTPASE REGULATOR-INTERACTING PROTEIN; 1. DR Pfam; PF00168; C2; 1. DR Pfam; PF11618; C2-C2_1; 1. DR Pfam; PF18111; RPGR1_C; 1. DR SMART; SM00239; C2; 2. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2. DR PROSITE; PS50004; C2; 2. DR Genevisible; Q68CZ1; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell junction; Cell projection; KW Ciliopathy; Cilium; Coiled coil; Cytoplasm; Cytoskeleton; Disease variant; KW Joubert syndrome; Meckel syndrome; Reference proteome; Repeat; KW Tight junction. FT CHAIN 1..1315 FT /note="Protein fantom" FT /id="PRO_0000291267" FT DOMAIN 577..713 FT /note="C2 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT DOMAIN 773..897 FT /note="C2 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT REGION 1021..1083 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 64..144 FT /evidence="ECO:0000255" FT COILED 197..256 FT /evidence="ECO:0000255" FT COILED 326..555 FT /evidence="ECO:0000255" FT COMPBIAS 1024..1039 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1040..1060 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1061..1082 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 987..1020 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10231032" FT /id="VSP_026161" FT VAR_SEQ 1099..1144 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10231032" FT /id="VSP_026162" FT VARIANT 199 FT /note="S -> G (found in a patient with Leber congenital FT amaurosis)" FT /evidence="ECO:0000269|PubMed:19430481" FT /id="VAR_066476" FT VARIANT 229 FT /note="A -> T (associated with the development of retinal FT degeneration in individuals with ciliopathies caused by FT mutations in other genes; found in patients with Leber FT congenital amaurosis, Senior-Loken syndrome, Joubert FT syndrome and Bardet-Biedl syndrome; abrogates interaction FT with RPGR; dbSNP:rs61747071)" FT /evidence="ECO:0000269|PubMed:19430481" FT /id="VAR_066477" FT VARIANT 393 FT /note="E -> K (in JBTS7; dbSNP:rs375776718)" FT /evidence="ECO:0000269|PubMed:17960139" FT /id="VAR_076824" FT VARIANT 447 FT /note="L -> S (in dbSNP:rs138155747)" FT /evidence="ECO:0000269|PubMed:19430481" FT /id="VAR_066478" FT VARIANT 546 FT /note="L -> F (found in a patient with Leber congenital FT amaurosis; dbSNP:rs147331527)" FT /evidence="ECO:0000269|PubMed:19430481" FT /id="VAR_066479" FT VARIANT 550 FT /note="Q -> R (in JBTS7; dbSNP:rs772900011)" FT /evidence="ECO:0000269|PubMed:22693042" FT /id="VAR_069234" FT VARIANT 615 FT /note="T -> P (in JBTS7; affects interaction with NPHP4; FT dbSNP:rs121918198)" FT /evidence="ECO:0000269|PubMed:17558407, FT ECO:0000269|PubMed:17558409, ECO:0000269|PubMed:17960139" FT /id="VAR_039393" FT VARIANT 633 FT /note="C -> R (in JBTS7; dbSNP:rs898062661)" FT /evidence="ECO:0000269|PubMed:17960139" FT /id="VAR_076825" FT VARIANT 647 FT /note="V -> I (in dbSNP:rs145572901)" FT /evidence="ECO:0000269|PubMed:19430481" FT /id="VAR_066480" FT VARIANT 659 FT /note="S -> P (in COACH3; dbSNP:rs267607020)" FT /evidence="ECO:0000269|PubMed:19574260" FT /id="VAR_063805" FT VARIANT 677 FT /note="T -> I (in JBTS7; also in a patient with Leber FT congenital amaurosis; affects interaction with NPHP4; FT dbSNP:rs532768944)" FT /evidence="ECO:0000269|PubMed:17558409, FT ECO:0000269|PubMed:19430481" FT /id="VAR_039394" FT VARIANT 695 FT /note="A -> P (in JBTS7; seems not to affect interaction FT with NPHP4; dbSNP:rs121918200)" FT /evidence="ECO:0000269|PubMed:17558409" FT /id="VAR_039395" FT VARIANT 744 FT /note="R -> Q (in dbSNP:rs2302677)" FT /id="VAR_039396" FT VARIANT 937 FT /note="R -> L (in a patient with Leber congenital FT amaurosis; dbSNP:rs776795273)" FT /evidence="ECO:0000269|PubMed:19430481" FT /id="VAR_066481" FT VARIANT 1025 FT /note="G -> S (in dbSNP:rs2111119)" FT /evidence="ECO:0000269|PubMed:19430481" FT /id="VAR_039397" FT VARIANT 1183 FT /note="A -> G (in a patient with Meckel-Gruber like FT syndrome also carrying L-220 and V-280 in TTC21B; also FT found in patients with Leber congenital amaurosis and a FT patient with Bardet-Biedl syndrome; dbSNP:rs139974543)" FT /evidence="ECO:0000269|PubMed:19430481, FT ECO:0000269|PubMed:21258341" FT /id="VAR_065556" FT VARIANT 1236 FT /note="R -> C (in MKS5; dbSNP:rs151332923)" FT /evidence="ECO:0000269|PubMed:19430481" FT /id="VAR_066482" FT VARIANT 1264 FT /note="D -> N (in dbSNP:rs3213758)" FT /evidence="ECO:0000269|PubMed:19430481" FT /id="VAR_039398" FT VARIANT 1264 FT /note="D -> Y (in patients with Leber congenital FT amaurosis)" FT /evidence="ECO:0000269|PubMed:19430481" FT /id="VAR_066483" FT CONFLICT 300 FT /note="R -> K (in Ref. 4; BAA76849)" FT /evidence="ECO:0000305" FT CONFLICT 575 FT /note="G -> D (in Ref. 1; CAH18439)" FT /evidence="ECO:0000305" FT CONFLICT 595 FT /note="D -> G (in Ref. 1; CAH18439)" FT /evidence="ECO:0000305" FT CONFLICT 992 FT /note="P -> L (in Ref. 1; CAH18439)" FT /evidence="ECO:0000305" FT CONFLICT 1143 FT /note="T -> S (in Ref. 1; CAH18439)" FT /evidence="ECO:0000305" FT STRAND 605..614 FT /evidence="ECO:0007829|PDB:2YRB" FT HELIX 618..623 FT /evidence="ECO:0007829|PDB:2YRB" FT STRAND 630..635 FT /evidence="ECO:0007829|PDB:2YRB" FT STRAND 648..652 FT /evidence="ECO:0007829|PDB:2YRB" FT STRAND 657..663 FT /evidence="ECO:0007829|PDB:2YRB" FT HELIX 667..675 FT /evidence="ECO:0007829|PDB:2YRB" FT STRAND 678..685 FT /evidence="ECO:0007829|PDB:2YRB" FT STRAND 690..698 FT /evidence="ECO:0007829|PDB:2YRB" FT HELIX 702..705 FT /evidence="ECO:0007829|PDB:2YRB" FT STRAND 710..716 FT /evidence="ECO:0007829|PDB:2YRB" FT STRAND 718..721 FT /evidence="ECO:0007829|PDB:2YRB" FT STRAND 726..737 FT /evidence="ECO:0007829|PDB:2YRB" SQ SEQUENCE 1315 AA; 151201 MW; 694B83C6A109E50A CRC64; MSGPTDETAG DLPVKDTGLN LFGMGGLQET STTRTMKSRQ AVSRVSREEL EDRFLRLHDE NILLKQHARK QEDKIKRMAT KLIRLVNDKK RYERVGGGPK RLGRDVEMEE MIEQLQEKVH ELEKQNETLK NRLISAKQQL QTQGYRQTPY NNVQSRINTG RRKANENAGL QECPRKGIKF QDADVAETPH PMFTKYGNSL LEEARGEIRN LENVIQSQRG QIEELEHLAE ILKTQLRRKE NEIELSLLQL REQQATDQRS NIRDNVEMIK LHKQLVEKSN ALSAMEGKFI QLQEKQRTLR ISHDALMANG DELNMQLKEQ RLKCCSLEKQ LHSMKFSERR IEELQDRIND LEKERELLKE NYDKLYDSAF SAAHEEQWKL KEQQLKVQIA QLETALKSDL TDKTEILDRL KTERDQNEKL VQENRELQLQ YLEQKQQLDE LKKRIKLYNQ ENDINADELS EALLLIKAQK EQKNGDLSFL VKVDSEINKD LERSMRELQA THAETVQELE KTRNMLIMQH KINKDYQMEV EAVTRKMENL QQDYELKVEQ YVHLLDIRAA RIHKLEAQLK DIAYGTKQYK FKPEIMPDDS VDEFDETIHL ERGENLFEIH INKVTFSSEV LQASGDKEPV TFCTYAFYDF ELQTTPVVRG LHPEYNFTSQ YLVHVNDLFL QYIQKNTITL EVHQAYSTEY ETIAACQLKF HEILEKSGRI FCTASLIGTK GDIPNFGTVE YWFRLRVPMD QAIRLYRERA KALGYITSNF KGPEHMQSLS QQAPKTAQLS STDSTDGNLN ELHITIRCCN HLQSRASHLQ PHPYVVYKFF DFADHDTAII PSSNDPQFDD HMYFPVPMNM DLDRYLKSES LSFYVFDDSD TQENIYIGKV NVPLISLAHD RCISGIFELT DHQKHPAGTI HVILKWKFAY LPPSGSITTE DLGNFIRSEE PEVVQRLPPA SSVSTLVLAP RPKPRQRLTP VDKKVSFVDI MPHQSDETSP PPEDRKEISP EVEHIPEIEI NMLTVPHVPK VSQEGSVDEV KENTEKMQQG KDDVSLLSEG QLAEQSLASS EDETEITEDL EPEVEEDMSA SDSDDCIIPG PISKNIKQSL ALSPGLGCSS AISAHCNFRL PGSSDFPASA SQVDGITGAC HHTQPSEKIR IEIIALSLND SQVTMDDTIQ RLFVECRFYS LPAEETPVSL PKPKSGQWVY YNYSNVIYVD KENNKAKRDI LKAILQKQEM PNRSLRFTVV SDPPEDEQDL ECEDIGVAHV DLADMFQEGR DLIEQNIDVF DARADGEGIG KLRVTVEALH ALQSVYKQYR DDLEA //