FTM_HUMAN
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 03-AUG-2022, entry version 154.
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";
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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; 184.
DR CORUM; Q68CZ1; -.
DR IntAct; Q68CZ1; 158.
DR MINT; Q68CZ1; -.
DR STRING; 9606.ENSP00000369257; -.
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; Q68CZ1; -.
DR PeptideAtlas; Q68CZ1; -.
DR PRIDE; Q68CZ1; -.
DR ProteomicsDB; 66034; -. [Q68CZ1-1]
DR ProteomicsDB; 66035; -. [Q68CZ1-2]
DR Antibodypedia; 28413; 112 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 CTD; 23322; -.
DR DisGeNET; 23322; -.
DR GeneCards; RPGRIP1L; -.
DR GeneReviews; RPGRIP1L; -.
DR HGNC; HGNC:29168; RPGRIP1L.
DR HPA; ENSG00000103494; Low tissue specificity.
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; MKFFNQE; -.
DR OrthoDB; 152378at2759; -.
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 1074 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 131 other tissues.
DR ExpressionAtlas; Q68CZ1; baseline and differential.
DR Genevisible; Q68CZ1; HS.
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 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; IPR041091; RPGRIP1_C.
DR InterPro; IPR031139; RPGRIP1_fam.
DR InterPro; IPR031136; RPGRIP1L.
DR PANTHER; PTHR14240; PTHR14240; 1.
DR PANTHER; PTHR14240:SF4; PTHR14240:SF4; 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; SSF49562; 2.
DR PROSITE; PS50004; C2; 2.
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
