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RPGR_MOUSE
ID   RPGR_MOUSE              Reviewed;        1001 AA.
AC   Q9R0X5; A2ADP3; G9BBQ2; O88408; Q9CU92;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2013, sequence version 2.
DT   25-MAY-2022, entry version 163.
DE   RecName: Full=X-linked retinitis pigmentosa GTPase regulator;
DE            Short=mRpgr;
DE   Flags: Precursor;
GN   Name=Rpgr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND ISOPRENYLATION AT CYS-998.
RC   TISSUE=Brain;
RX   PubMed=9677393; DOI=10.1074/jbc.273.31.19656;
RA   Yan D., Swain P.K., Breuer D., Tucker R.M., Wu W., Fujita R.,
RA   Rehemtulla A., Burke D., Swaroop A.;
RT   "Biochemical characterization and subcellular localization of the mouse
RT   retinitis pigmentosa GTPase regulator.";
RL   J. Biol. Chem. 273:19656-19663(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=10401007; DOI=10.1093/hmg/8.8.1571;
RA   Kirschner R., Rosenberg T., Schultz-Heienbrok R., Lenzner S., Feil S.,
RA   Roepman R., Cremers F.P.M., Ropers H.-H., Berger W.;
RT   "RPGR transcription studies in mouse and human tissues reveal a retina-
RT   specific isoform that is disrupted in a patient with X-linked retinitis
RT   pigmentosa.";
RL   Hum. Mol. Genet. 8:1571-1578(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 1).
RC   STRAIN=129/SvEvTacfBr;
RX   PubMed=11702207; DOI=10.1007/s004390100572;
RA   Kirschner R., Erturk D., Zeitz C., Sahin S., Ramser J., Cremers F.P.M.,
RA   Ropers H.-H., Berger W.;
RT   "DNA sequence comparison of human and mouse retinitis pigmentosa GTPase
RT   regulator (RPGR) identifies tissue-specific exons and putative regulatory
RT   elements.";
RL   Hum. Genet. 109:271-278(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-845 (ISOFORMS 2/3).
RC   STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 525-1001 (ISOFORM 5), INTERACTION WITH
RP   WHRN, AND TISSUE SPECIFICITY.
RC   STRAIN=129/Sv;
RX   PubMed=22323458; DOI=10.1167/iovs.11-8845;
RA   Wright R.N., Hong D.H., Perkins B.;
RT   "RpgrORF15 connects to the usher protein network through direct
RT   interactions with multiple whirlin isoforms.";
RL   Invest. Ophthalmol. Vis. Sci. 53:1519-1529(2012).
RN   [7]
RP   INTERACTION WITH PDE6D.
RX   PubMed=9990021; DOI=10.1073/pnas.96.4.1315;
RA   Linari M., Ueffing M., Manson F., Wright A., Meitinger T., Becker J.;
RT   "The retinitis pigmentosa GTPase regulator, RPGR, interacts with the delta
RT   subunit of rod cyclic GMP phosphodiesterase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:1315-1320(1999).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=12140192; DOI=10.1093/hmg/11.16.1899;
RA   Mavlyutov T.A., Zhao H., Ferreira P.A.;
RT   "Species-specific subcellular localization of RPGR and RPGRIP isoforms:
RT   implications for the phenotypic variability of congenital retinopathies
RT   among species.";
RL   Hum. Mol. Genet. 11:1899-1907(2002).
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15772089; DOI=10.1093/hmg/ddi129;
RA   Shu X., Fry A.M., Tulloch B., Manson F.D., Crabb J.W., Khanna H.,
RA   Faragher A.J., Lennon A., He S., Trojan P., Giessl A., Wolfrum U.,
RA   Vervoort R., Swaroop A., Wright A.F.;
RT   "RPGR ORF15 isoform co-localizes with RPGRIP1 at centrioles and basal
RT   bodies and interacts with nucleophosmin.";
RL   Hum. Mol. Genet. 14:1183-1197(2005).
RN   [10]
RP   INTERACTION WITH SMC1A AND SMC3, AND SUBCELLULAR LOCATION.
RX   PubMed=16043481; DOI=10.1074/jbc.m505827200;
RA   Khanna H., Hurd T.W., Lillo C., Shu X., Parapuram S.K., He S., Akimoto M.,
RA   Wright A.F., Margolis B., Williams D.S., Swaroop A.;
RT   "RPGR-ORF15, which is mutated in retinitis pigmentosa, associates with
RT   SMC1, SMC3, and microtubule transport proteins.";
RL   J. Biol. Chem. 280:33580-33587(2005).
RN   [11]
RP   INTERACTS WITH CEP290, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16632484; DOI=10.1093/hmg/ddl107;
RA   Chang B., Khanna H., Hawes N., Jimeno D., He S., Lillo C., Parapuram S.K.,
RA   Cheng H., Scott A., Hurd R.E., Sayer J.A., Otto E.A., Attanasio M.,
RA   O'Toole J.F., Jin G., Shou C., Hildebrandt F., Williams D.S.,
RA   Heckenlively J.R., Swaroop A.;
RT   "In-frame deletion in a novel centrosomal/ciliary protein CEP290/NPHP6
RT   perturbs its interaction with RPGR and results in early-onset retinal
RT   degeneration in the rd16 mouse.";
RL   Hum. Mol. Genet. 15:1847-1857(2006).
RN   [12]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=18579752; DOI=10.1095/biolreprod.107.067454;
RA   Brunner S., Colman D., Travis A.J., Luhmann U.F., Shi W., Feil S.,
RA   Imsand C., Nelson J., Grimm C., Rulicke T., Fundele R., Neidhardt J.,
RA   Berger W.;
RT   "Overexpression of RPGR leads to male infertility in mice due to defects in
RT   flagellar assembly.";
RL   Biol. Reprod. 79:608-617(2008).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [14]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=20007830; DOI=10.1167/iovs.08-2742;
RA   Brunner S., Skosyrski S., Kirschner-Schwabe R., Knobeloch K.P.,
RA   Neidhardt J., Feil S., Glaus E., Luhmann U.F., Ruther K., Berger W.;
RT   "Cone versus rod disease in a mutant Rpgr mouse caused by different genetic
RT   backgrounds.";
RL   Invest. Ophthalmol. Vis. Sci. 51:1106-1115(2010).
RN   [15]
RP   TISSUE SPECIFICITY.
RX   PubMed=20805823; DOI=10.1038/ki.2010.252;
RA   Patil S.B., Verma R., Venkatareddy M., Khanna H.;
RT   "Expression and localization of the ciliary disease protein retinitis
RT   pigmentosa GTPase regulator in mammalian kidney.";
RL   Kidney Int. 78:622-623(2010).
RN   [16]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=21546531; DOI=10.1167/iovs.11-7470;
RA   Wright R.N., Hong D.H., Perkins B.;
RT   "Misexpression of the constitutive Rpgr(ex1-19) variant leads to severe
RT   photoreceptor degeneration.";
RL   Invest. Ophthalmol. Vis. Sci. 52:5189-5201(2011).
RN   [17]
RP   FUNCTION, AND MOUSE MODEL OF X-LINKED RETINOSA PIGMENTOSA.
RX   PubMed=22563472; DOI=10.1371/journal.pone.0035865;
RA   Thompson D.A., Khan N.W., Othman M.I., Chang B., Jia L., Grahek G., Wu Z.,
RA   Hiriyanna S., Nellissery J., Li T., Khanna H., Colosi P., Swaroop A.,
RA   Heckenlively J.R.;
RT   "Rd9 is a naturally occurring mouse model of a common form of retinitis
RT   pigmentosa caused by mutations in RPGR-ORF15.";
RL   PLoS ONE 7:E35865-E35865(2012).
RN   [18]
RP   INTERACTION WITH SPATA7, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=29899041; DOI=10.1083/jcb.201712117;
RA   Dharmat R., Eblimit A., Robichaux M.A., Zhang Z., Nguyen T.T., Jung S.Y.,
RA   He F., Jain A., Li Y., Qin J., Overbeek P., Roepman R., Mardon G.,
RA   Wensel T.G., Chen R.;
RT   "SPATA7 maintains a novel photoreceptor-specific zone in the distal
RT   connecting cilium.";
RL   J. Cell Biol. 217:2851-2865(2018).
CC   -!- FUNCTION: Could be a guanine-nucleotide releasing factor (By
CC       similarity). Plays a role in ciliogenesis (By similarity). Probably
CC       regulates cilia formation by regulating actin stress filaments and cell
CC       contractility (By similarity). May be involved in microtubule
CC       organization and regulation of transport in primary cilia (By
CC       similarity). Plays an important role in photoreceptor integrity.
CC       Isoform 5 may play a critical role in spermatogenesis and in
CC       intraflagellar transport processes. {ECO:0000250,
CC       ECO:0000269|PubMed:18579752, ECO:0000269|PubMed:22563472}.
CC   -!- SUBUNIT: Interacts with SPATA7 (PubMed:29899041). Interacts with PDE6D
CC       (PubMed:9990021). Interacts with RPGRIP1 and RPGRIP1L; PDE6D, RPGRIP1
CC       and RPGRIP1L may compete for the same binding sites (By similarity).
CC       Interacts with NPM1 (By similarity). Interacts with PDE6D. Isoform 5
CC       interacts (via N-terminus) with SMC1A and SMC3 (PubMed:16043481).
CC       Isoform 5 interacts with CEP290 (PubMed:16632484). Interacts with WHRN
CC       (PubMed:22323458). {ECO:0000250|UniProtKB:Q92834,
CC       ECO:0000269|PubMed:16043481, ECO:0000269|PubMed:16632484,
CC       ECO:0000269|PubMed:22323458, ECO:0000269|PubMed:29899041,
CC       ECO:0000269|PubMed:9990021}.
CC   -!- INTERACTION:
CC       Q9R0X5; Q68CZ1: RPGRIP1L; Xeno; NbExp=3; IntAct=EBI-6915619, EBI-5235485;
CC       Q9R0X5-5; Q80VW5-12: Whrn; NbExp=2; IntAct=EBI-6915646, EBI-6915655;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:15772089,
CC       ECO:0000269|PubMed:16043481, ECO:0000269|PubMed:20007830,
CC       ECO:0000269|PubMed:9677393}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:Q92834}. Cell
CC       projection, cilium {ECO:0000269|PubMed:29899041}. Note=In the retinal
CC       photoreceptor cell layer, localizes at the connecting cilium
CC       (PubMed:29899041). Colocalizes with WHRN in the photoreceptor
CC       connecting cilium (PubMed:22323458). Colocalizes with CEP290 in the
CC       photoreceptor connecting cilium (PubMed:16632484). Colocalizes with
CC       RPGRIP1 in the photoreceptor connecting cilium (PubMed:15772089).
CC       {ECO:0000269|PubMed:15772089, ECO:0000269|PubMed:16632484,
CC       ECO:0000269|PubMed:22323458, ECO:0000269|PubMed:29899041}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm, cytoskeleton, cilium
CC       basal body. Cytoplasm, cytoskeleton, cilium axoneme. Cytoplasm,
CC       cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:20007830}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1; Synonyms=ex1-19;
CC         IsoId=Q9R0X5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9R0X5-2; Sequence=VSP_005552;
CC       Name=3;
CC         IsoId=Q9R0X5-3; Sequence=VSP_005552, VSP_005553;
CC       Name=4;
CC         IsoId=Q9R0X5-4; Sequence=VSP_005551, VSP_005552, VSP_005554,
CC                                  VSP_005555;
CC       Name=5; Synonyms=ORF15;
CC         IsoId=Q9R0X5-5; Sequence=VSP_045292;
CC   -!- TISSUE SPECIFICITY: Expressed in the retina (at protein level)
CC       (PubMed:10401007, PubMed:22323458, PubMed:12140192, PubMed:16632484,
CC       PubMed:20007830, PubMed:21546531, PubMed:29899041). Isoforms 1:
CC       Expressed in the retina (at protein level) (PubMed:21546531). Isoform
CC       5: Expressed in the retina (at protein level) (PubMed:20007830,
CC       PubMed:21546531). Expressed in the brain (PubMed:9677393,
CC       PubMed:10401007). Expressed in the testis (at protein level)
CC       (PubMed:10401007, PubMed:18579752). Expressed in kidney (at protein
CC       level) (PubMed:10401007, PubMed:20805823).
CC       {ECO:0000269|PubMed:10401007, ECO:0000269|PubMed:12140192,
CC       ECO:0000269|PubMed:16632484, ECO:0000269|PubMed:18579752,
CC       ECO:0000269|PubMed:20007830, ECO:0000269|PubMed:20805823,
CC       ECO:0000269|PubMed:21546531, ECO:0000269|PubMed:22323458,
CC       ECO:0000269|PubMed:29899041, ECO:0000269|PubMed:9677393}.
CC   -!- DEVELOPMENTAL STAGE: At postnatal day 3 isoform 1 is expressed in the
CC       retina in a narrow band at the developing photoreceptor layer;
CC       expression in this band persists through to postnatal day 14 but
CC       becomes severely diminished in the adult retina. Isoform 5 is first
CC       detected in the retina at postnatal day 14 and is expressed at
CC       increased levels in the adult retina (at protein level). Expressed
CC       throughout embryonic development from day 7 of gestation. Also
CC       expressed in adult. {ECO:0000269|PubMed:21546531,
CC       ECO:0000269|PubMed:9677393}.
CC   -!- DOMAIN: The RCC1 repeat region mediates interactions with RPGRIP1.
CC       {ECO:0000250|UniProtKB:Q92834}.
CC   -!- PTM: Prenylated. {ECO:0000269|PubMed:9677393}.
CC   -!- MISCELLANEOUS: Male transgenic mice carrying multiple copies of the
CC       Rpgr transgene are infertile showing normal mating but no progeny;
CC       these mice also exhibit reduced sperm numbers as well as morphological
CC       and functional defects in the sperm flagellum.
CC       {ECO:0000305|PubMed:18579752}.
CC   -!- MISCELLANEOUS: Male BL/6 and BALB/c transgenic mice with an in-frame
CC       deletion of exon 4 of Rpgr show retinal degeneration that is rod or
CC       cone dominated, respectively. {ECO:0000305|PubMed:20007830}.
CC   -!- MISCELLANEOUS: Overexpression of isoform 1 results in atypical
CC       accumulation of Rpgr in photoreceptor outer segments, abnormal
CC       photoreceptor morphology and severe retinal degeneration.
CC       {ECO:0000305|PubMed:21546531}.
CC   -!- MISCELLANEOUS: In a mouse model of X-linked retinosa pigmentosa, where
CC       a 32bp duplication leads to a frameshift in the reading frame and a
CC       premature stop codon in isoform 5 (ORF15), mice exhibited retinal
CC       pathology including pigment loss and a slow progressive decrease in
CC       outer nuclear layer thickness. {ECO:0000305|PubMed:22563472}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC40190.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB30628.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAM22657.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF044677; AAC40190.1; ALT_INIT; mRNA.
DR   EMBL; AJ238396; CAB54041.1; -; mRNA.
DR   EMBL; AJ318464; CAC86115.1; -; Genomic_DNA.
DR   EMBL; AL671042; CAM22657.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AK017192; BAB30628.3; ALT_INIT; mRNA.
DR   EMBL; BX005236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; HQ260316; AEO00588.1; -; Genomic_DNA.
DR   RefSeq; NP_035415.1; NM_011285.2.
DR   AlphaFoldDB; Q9R0X5; -.
DR   SMR; Q9R0X5; -.
DR   BioGRID; 202963; 1.
DR   DIP; DIP-46319N; -.
DR   IntAct; Q9R0X5; 5.
DR   STRING; 10090.ENSMUSP00000037358; -.
DR   iPTMnet; Q9R0X5; -.
DR   PhosphoSitePlus; Q9R0X5; -.
DR   EPD; Q9R0X5; -.
DR   MaxQB; Q9R0X5; -.
DR   PaxDb; Q9R0X5; -.
DR   PRIDE; Q9R0X5; -.
DR   ProteomicsDB; 300437; -. [Q9R0X5-1]
DR   ProteomicsDB; 300438; -. [Q9R0X5-2]
DR   ProteomicsDB; 300439; -. [Q9R0X5-3]
DR   ProteomicsDB; 300440; -. [Q9R0X5-4]
DR   ProteomicsDB; 300441; -. [Q9R0X5-5]
DR   DNASU; 19893; -.
DR   GeneID; 19893; -.
DR   KEGG; mmu:19893; -.
DR   UCSC; uc009sqj.2; mouse. [Q9R0X5-4]
DR   CTD; 6103; -.
DR   MGI; MGI:1344037; Rpgr.
DR   eggNOG; KOG1426; Eukaryota.
DR   InParanoid; Q9R0X5; -.
DR   TreeFam; TF331400; -.
DR   BioGRID-ORCS; 19893; 4 hits in 71 CRISPR screens.
DR   ChiTaRS; Rpgr; mouse.
DR   PRO; PR:Q9R0X5; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q9R0X5; protein.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR   GO; GO:0005929; C:cilium; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0032391; C:photoreceptor connecting cilium; IDA:MGI.
DR   GO; GO:0120206; C:photoreceptor distal connecting cilium; IDA:MGI.
DR   GO; GO:0001750; C:photoreceptor outer segment; ISO:MGI.
DR   GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0071482; P:cellular response to light stimulus; IMP:MGI.
DR   GO; GO:0060271; P:cilium assembly; ISO:MGI.
DR   GO; GO:0042462; P:eye photoreceptor cell development; IMP:MGI.
DR   GO; GO:0042073; P:intraciliary transport; IMP:UniProtKB.
DR   GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:MGI.
DR   GO; GO:0007601; P:visual perception; IMP:MGI.
DR   Gene3D; 2.130.10.30; -; 1.
DR   InterPro; IPR009091; RCC1/BLIP-II.
DR   InterPro; IPR000408; Reg_chr_condens.
DR   Pfam; PF00415; RCC1; 6.
DR   PRINTS; PR00633; RCCNDNSATION.
DR   SUPFAM; SSF50985; SSF50985; 1.
DR   PROSITE; PS00626; RCC1_2; 3.
DR   PROSITE; PS50012; RCC1_3; 6.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell projection; Cilium;
KW   Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Flagellum;
KW   Golgi apparatus; Guanine-nucleotide releasing factor; Lipoprotein;
KW   Methylation; Phosphoprotein; Prenylation; Reference proteome; Repeat;
KW   Sensory transduction; Vision.
FT   CHAIN           1..998
FT                   /note="X-linked retinitis pigmentosa GTPase regulator"
FT                   /id="PRO_0000206639"
FT   PROPEP          999..1001
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000370845"
FT   REPEAT          54..105
FT                   /note="RCC1 1"
FT   REPEAT          106..158
FT                   /note="RCC1 2"
FT   REPEAT          159..208
FT                   /note="RCC1 3"
FT   REPEAT          209..261
FT                   /note="RCC1 4"
FT   REPEAT          262..313
FT                   /note="RCC1 5"
FT   REPEAT          314..367
FT                   /note="RCC1 6"
FT   REGION          404..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          631..738
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          794..869
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          902..925
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          962..1001
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        631..675
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        688..718
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        794..812
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        842..861
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        969..1001
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         518
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92834"
FT   MOD_RES         998
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000305"
FT   LIPID           998
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000303|PubMed:9677393"
FT   VAR_SEQ         260..469
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:9677393"
FT                   /id="VSP_005551"
FT   VAR_SEQ         525..817
FT                   /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:9677393"
FT                   /id="VSP_005552"
FT   VAR_SEQ         818..1001
FT                   /note="APQLSETVKPEEGEMDEEISILNVEDTVEEERKEGEKEIVEEGSIPETEGSE
FT                   TIDITDEKLDEVLKEEDSASLLQRALREYNENPKGHMYDRVKSSSSEILGGNDPTSKDI
FT                   KKAKKISFFNRMSLTGQKLMQNTNDPLPEIKPIGDQIALQSDKKDANQNHMGQNLQDST
FT                   TPNMEGKSKSCTIL -> VSESERESGGEREDRSEGDGDQICEKVSLETEHLQRAQGKQ
FT                   ERKKGKDKRARCILDMKEREEDKGWEKGSEGGDKMKRDEGNQEKRKKEMEERDAGDERS
FT                   EEEEGEEEEPEEGEKEEGGEEEEGTSEDQSREDEGDRQEKEGRREGKGRQEDGREGWKE
FT                   GEEQEQEEEIEEGEEEEREGEEEGGEEEGEGEGEREEEGEGEEEGEGEEEGEGEEEGEG
FT                   EEEGEGEEEGEGEEEGEGEEEGEGEEDGEGEEDGEGEEEGEGEEEGEREEDGEGEEDGE
FT                   GEEEGEGEEEGEGEEEGEGEEEGEGEGEEEGEGEWEGEEEGEGEEEGEGEEEGEGEEEG
FT                   EGEEEGEGEEEGGEDDEGEELEKKKGDITEEEEEEEEGQEGDEREREEHGSCEDDVEED
FT                   KTYDREEGEYKKAIGKVADNESQEDRKQSPKVSKINGSMKYGRHGTYSEKPITNLGKTQ
FT                   PSKMPMESRQLVENGLLGSERFWSDVLPLYLELK (in isoform 5)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_045292"
FT   VAR_SEQ         904..943
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:9677393"
FT                   /id="VSP_005553"
FT   VAR_SEQ         904..907
FT                   /note="GHMY -> DFLL (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:9677393"
FT                   /id="VSP_005554"
FT   VAR_SEQ         908..1001
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:9677393"
FT                   /id="VSP_005555"
FT   CONFLICT        226
FT                   /note="N -> S (in Ref. 3; CAC86115)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        606
FT                   /note="K -> R (in Ref. 2; CAB54041 and 6; AEO00588)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        697
FT                   /note="S -> N (in Ref. 2; CAB54041 and 6; AEO00588)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1001 AA;  111801 MW;  021997395B74E6CA CRC64;
     MAESESLVPD TGAVFTFGKT KFAENIPSKF WFKNDIPICL SCGDEHTAIV TGNNKLYMFG
     SNNWGQLGLG SKAAIIKPTC IKALKPEKVK LAACGRNHTL VSTDTGGVYA AGGNNEGQLG
     LGDTDDRDTF HQIVFFTPAD TIKQLSAGAN TSAALTEDGK LFMWGDNSEG QIGLEDKSNV
     CIPHEVTVGK PISWISCGYY HSAFVTMDGE LYTFGEPENG KLGLPNELLM NHRSPQRVLG
     IPERVIQVAC GGGHTVVLTE KVVYAFGLGQ FGQLGLGTFL FETSEPKIIE RIKDQKICHI
     SCGENHTALM TELGLLYTFG DGRHGKLGLG MENFTNQFFP TLCSNFLRFA VQLIACGGCH
     MLVFATPRLG TIDEPKFEDV YEPYISTGSF SINDLSPRSS LNRSLSARLR RRERERPPCS
     ASMVGTLPPL EGTSASTSAY FYPSSPPFHL SVNNYPEKSP SESMEPLDSD YFEDKMNKDT
     ETENSSAVDS ENFGETNDIL NMTHMMTTSS NEKLLDFSPI QKQQNQDTFE KVMESTPCTE
     NEDSYEYEEM SKIKEVTVYK QYLAKGIYMI RPAEILEAFS DEEVGNGLDQ VEEPRVFTDG
     KGLQSKQVGK ESDEEIVSEK KTEVMEVADV KKIRESEENS KSDSLFDDLP DKTMNSESED
     NKDIAEERRS SEQNMTFDSE TELVEEPDSY MECERHSEQD SAEELEQPKL VEYSSEEKDE
     KDEKDDDEVE TENLWYDRNC TEQETENVFR ATRFFPKFDL KHDHLSGIPE EQEGPEDSEG
     NVVVEQVVQA QKENLEFEGD RKEAKAEAPS DVITEKEAPQ LSETVKPEEG EMDEEISILN
     VEDTVEEERK EGEKEIVEEG SIPETEGSET IDITDEKLDE VLKEEDSASL LQRALREYNE
     NPKGHMYDRV KSSSSEILGG NDPTSKDIKK AKKISFFNRM SLTGQKLMQN TNDPLPEIKP
     IGDQIALQSD KKDANQNHMG QNLQDSTTPN MEGKSKSCTI L
 
 
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