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Q9R0X5

- RPGR_MOUSE

UniProt

Q9R0X5 - RPGR_MOUSE

Protein

X-linked retinitis pigmentosa GTPase regulator

Gene

Rpgr

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (06 Feb 2013)
      Previous versions | rss
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    Functioni

    Could be a guanine-nucleotide releasing factor By similarity. Plays a role in ciliogenesis By similarity. Probably regulates cilia formation by regulating actin stress filaments and cell contractility By similarity. May be involved in microtubule organization and regulation of transport in primary cilia By similarity. Plays an important role in photoreceptor integrity. Isoform 5 may play a critical role in spermatogenesis and in intraflagellar transport processes.By similarity2 Publications

    GO - Molecular functioni

    1. guanyl-nucleotide exchange factor activity Source: UniProtKB-KW
    2. protein binding Source: IntAct

    GO - Biological processi

    1. cilium assembly Source: Ensembl
    2. eye photoreceptor cell development Source: MGI
    3. intraciliary transport Source: UniProtKB
    4. response to stimulus Source: UniProtKB-KW
    5. visual perception Source: UniProtKB

    Keywords - Molecular functioni

    Guanine-nucleotide releasing factor

    Keywords - Biological processi

    Cilium biogenesis/degradation, Sensory transduction, Vision

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    X-linked retinitis pigmentosa GTPase regulator
    Short name:
    mRpgr
    Gene namesi
    Name:Rpgr
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1344037. Rpgr.

    Subcellular locationi

    Golgi apparatus 4 Publications. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. ciliary basal body Source: UniProtKB
    3. cilium Source: MGI
    4. cytoplasm Source: MGI
    5. Golgi apparatus Source: UniProtKB
    6. photoreceptor outer segment Source: Ensembl
    7. sperm flagellum Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cilium, Cytoplasm, Cytoskeleton, Golgi apparatus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 998998X-linked retinitis pigmentosa GTPase regulatorPRO_0000206639Add
    BLAST
    Propeptidei999 – 10013Removed in mature formSequence AnalysisPRO_0000370845

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei998 – 9981Cysteine methyl esterSequence Analysis
    Lipidationi998 – 9981S-geranylgeranyl cysteine1 Publication

    Post-translational modificationi

    Prenylated.1 Publication

    Keywords - PTMi

    Lipoprotein, Methylation, Prenylation

    Proteomic databases

    PaxDbiQ9R0X5.
    PRIDEiQ9R0X5.

    PTM databases

    PhosphoSiteiQ9R0X5.

    Expressioni

    Tissue specificityi

    Colocalizes with either CEP290, DFNB31 or RPGRIP1 in the photoreceptor connecting cilium, a thin bridge linking the cell body and the light-sensing outer segment. Expressed in kidney. Isoforms 1 and 5 expressed in retina (at protein level). Widely expressed with highest levels in brain and testis and low levels in eye.9 Publications

    Developmental stagei

    At postnatal day 3 isoform 1 is expressed in the retina in a narrow band at the developing photoreceptor layer; expression in this band persists through to postnatal day 14 but becomes severely diminished in the adult retina. Isoform 5 is first detected in the retina at postnatal day 14 and is expressed at increased levels in the adult retina (at protein level). Expressed throughout embryonic development from day 7 of gestation. Also expressed in adult.2 Publications

    Gene expression databases

    CleanExiMM_RPGR.
    GenevestigatoriQ9R0X5.

    Interactioni

    Subunit structurei

    Interacts with RPGRIP1 By similarity. Interacts with PDE6D. Interacts with NPM1 By similarity. Interacts with RPGRIP1L By similarity. Isoform 5 interacts (via N-terminus) with SMC1A and SMC3. Isoform 5 interacts with CEP290. Interacts with DFNB31.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Dfnb31Q80VW5-122EBI-6915646,EBI-6915655

    Protein-protein interaction databases

    BioGridi202963. 1 interaction.
    DIPiDIP-46319N.
    IntActiQ9R0X5. 1 interaction.
    STRINGi10090.ENSMUSP00000037358.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9R0X5.
    SMRiQ9R0X5. Positions 7-367.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati54 – 10552RCC1 1Add
    BLAST
    Repeati106 – 15853RCC1 2Add
    BLAST
    Repeati159 – 20850RCC1 3Add
    BLAST
    Repeati209 – 26153RCC1 4Add
    BLAST
    Repeati262 – 31352RCC1 5Add
    BLAST
    Repeati314 – 36754RCC1 6Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi530 – 885356Glu-richAdd
    BLAST

    Sequence similaritiesi

    Contains 6 RCC1 repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5184.
    HOGENOMiHOG000231314.
    HOVERGENiHBG026899.
    InParanoidiQ9R0X5.
    TreeFamiTF331400.

    Family and domain databases

    Gene3Di2.130.10.30. 1 hit.
    InterProiIPR009091. RCC1/BLIP-II.
    IPR000408. Reg_chr_condens.
    [Graphical view]
    PfamiPF00415. RCC1. 6 hits.
    [Graphical view]
    PRINTSiPR00633. RCCNDNSATION.
    SUPFAMiSSF50985. SSF50985. 1 hit.
    PROSITEiPS00626. RCC1_2. 3 hits.
    PS50012. RCC1_3. 6 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q9R0X5-1) [UniParc]FASTAAdd to Basket

    Also known as: ex1-19

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAESESLVPD TGAVFTFGKT KFAENIPSKF WFKNDIPICL SCGDEHTAIV     50
    TGNNKLYMFG SNNWGQLGLG SKAAIIKPTC IKALKPEKVK LAACGRNHTL 100
    VSTDTGGVYA AGGNNEGQLG LGDTDDRDTF HQIVFFTPAD TIKQLSAGAN 150
    TSAALTEDGK LFMWGDNSEG QIGLEDKSNV CIPHEVTVGK PISWISCGYY 200
    HSAFVTMDGE LYTFGEPENG KLGLPNELLM NHRSPQRVLG IPERVIQVAC 250
    GGGHTVVLTE KVVYAFGLGQ FGQLGLGTFL FETSEPKIIE RIKDQKICHI 300
    SCGENHTALM TELGLLYTFG DGRHGKLGLG MENFTNQFFP TLCSNFLRFA 350
    VQLIACGGCH MLVFATPRLG TIDEPKFEDV YEPYISTGSF SINDLSPRSS 400
    LNRSLSARLR RRERERPPCS ASMVGTLPPL EGTSASTSAY FYPSSPPFHL 450
    SVNNYPEKSP SESMEPLDSD YFEDKMNKDT ETENSSAVDS ENFGETNDIL 500
    NMTHMMTTSS NEKLLDFSPI QKQQNQDTFE KVMESTPCTE NEDSYEYEEM 550
    SKIKEVTVYK QYLAKGIYMI RPAEILEAFS DEEVGNGLDQ VEEPRVFTDG 600
    KGLQSKQVGK ESDEEIVSEK KTEVMEVADV KKIRESEENS KSDSLFDDLP 650
    DKTMNSESED NKDIAEERRS SEQNMTFDSE TELVEEPDSY MECERHSEQD 700
    SAEELEQPKL VEYSSEEKDE KDEKDDDEVE TENLWYDRNC TEQETENVFR 750
    ATRFFPKFDL KHDHLSGIPE EQEGPEDSEG NVVVEQVVQA QKENLEFEGD 800
    RKEAKAEAPS DVITEKEAPQ LSETVKPEEG EMDEEISILN VEDTVEEERK 850
    EGEKEIVEEG SIPETEGSET IDITDEKLDE VLKEEDSASL LQRALREYNE 900
    NPKGHMYDRV KSSSSEILGG NDPTSKDIKK AKKISFFNRM SLTGQKLMQN 950
    TNDPLPEIKP IGDQIALQSD KKDANQNHMG QNLQDSTTPN MEGKSKSCTI 1000
    L 1001
    Length:1,001
    Mass (Da):111,801
    Last modified:February 6, 2013 - v2
    Checksum:i021997395B74E6CA
    GO
    Isoform 2 (identifier: Q9R0X5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         525-817: Missing.

    Show »
    Length:708
    Mass (Da):77,884
    Checksum:i1960A6183DB7F93D
    GO
    Isoform 3 (identifier: Q9R0X5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         525-817: Missing.
         904-943: Missing.

    Show »
    Length:668
    Mass (Da):73,427
    Checksum:i1B7ACEC74AFBE2D0
    GO
    Isoform 4 (identifier: Q9R0X5-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         260-469: Missing.
         525-817: Missing.
         904-907: GHMY → DFLL
         908-1001: Missing.

    Show »
    Length:404
    Mass (Da):44,323
    Checksum:i419389829C4A7BB3
    GO
    Isoform 5 (identifier: Q9R0X5-5) [UniParc]FASTAAdd to Basket

    Also known as: ORF15

    The sequence of this isoform differs from the canonical sequence as follows:
         818-1001: APQLSETVKP...EGKSKSCTIL → VSESERESGG...DVLPLYLELK

    Note: No experimental confirmation available.

    Show »
    Length:1,305
    Mass (Da):146,029
    Checksum:iC2630A87241006B5
    GO

    Sequence cautioni

    The sequence AAC40190.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAB30628.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAM22657.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti226 – 2261N → S in CAC86115. (PubMed:11702207)Curated
    Sequence conflicti606 – 6061K → R in CAB54041. (PubMed:10401007)Curated
    Sequence conflicti606 – 6061K → R in AEO00588. (PubMed:22323458)Curated
    Sequence conflicti697 – 6971S → N in CAB54041. (PubMed:10401007)Curated
    Sequence conflicti697 – 6971S → N in AEO00588. (PubMed:22323458)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei260 – 469210Missing in isoform 4. 1 PublicationVSP_005551Add
    BLAST
    Alternative sequencei525 – 817293Missing in isoform 2, isoform 3 and isoform 4. 1 PublicationVSP_005552Add
    BLAST
    Alternative sequencei818 – 1001184APQLS…SCTIL → VSESERESGGEREDRSEGDG DQICEKVSLETEHLQRAQGK QERKKGKDKRARCILDMKER EEDKGWEKGSEGGDKMKRDE GNQEKRKKEMEERDAGDERS EEEEGEEEEPEEGEKEEGGE EEEGTSEDQSREDEGDRQEK EGRREGKGRQEDGREGWKEG EEQEQEEEIEEGEEEEREGE EEGGEEEGEGEGEREEEGEG EEEGEGEEEGEGEEEGEGEE EGEGEEEGEGEEEGEGEEEG EGEEDGEGEEDGEGEEEGEG EEEGEREEDGEGEEDGEGEE EGEGEEEGEGEEEGEGEEEG EGEGEEEGEGEWEGEEEGEG EEEGEGEEEGEGEEEGEGEE EGEGEEEGGEDDEGEELEKK KGDITEEEEEEEEGQEGDER EREEHGSCEDDVEEDKTYDR EEGEYKKAIGKVADNESQED RKQSPKVSKINGSMKYGRHG TYSEKPITNLGKTQPSKMPM ESRQLVENGLLGSERFWSDV LPLYLELK in isoform 5. CuratedVSP_045292Add
    BLAST
    Alternative sequencei904 – 94340Missing in isoform 3. 1 PublicationVSP_005553Add
    BLAST
    Alternative sequencei904 – 9074GHMY → DFLL in isoform 4. 1 PublicationVSP_005554
    Alternative sequencei908 – 100194Missing in isoform 4. 1 PublicationVSP_005555Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF044677 mRNA. Translation: AAC40190.1. Different initiation.
    AJ238396 mRNA. Translation: CAB54041.1.
    AJ318464 Genomic DNA. Translation: CAC86115.1.
    AL671042 Genomic DNA. Translation: CAM22657.1. Different initiation.
    AK017192 mRNA. Translation: BAB30628.3. Different initiation.
    BX005236 Genomic DNA. No translation available.
    HQ260316 Genomic DNA. Translation: AEO00588.1.
    RefSeqiNP_035415.1. NM_011285.2.
    UniGeneiMm.247556.

    Genome annotation databases

    GeneIDi19893.
    KEGGimmu:19893.
    UCSCiuc009sqh.2. mouse.
    uc009sqj.2. mouse. [Q9R0X5-4]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF044677 mRNA. Translation: AAC40190.1 . Different initiation.
    AJ238396 mRNA. Translation: CAB54041.1 .
    AJ318464 Genomic DNA. Translation: CAC86115.1 .
    AL671042 Genomic DNA. Translation: CAM22657.1 . Different initiation.
    AK017192 mRNA. Translation: BAB30628.3 . Different initiation.
    BX005236 Genomic DNA. No translation available.
    HQ260316 Genomic DNA. Translation: AEO00588.1 .
    RefSeqi NP_035415.1. NM_011285.2.
    UniGenei Mm.247556.

    3D structure databases

    ProteinModelPortali Q9R0X5.
    SMRi Q9R0X5. Positions 7-367.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202963. 1 interaction.
    DIPi DIP-46319N.
    IntActi Q9R0X5. 1 interaction.
    STRINGi 10090.ENSMUSP00000037358.

    PTM databases

    PhosphoSitei Q9R0X5.

    Proteomic databases

    PaxDbi Q9R0X5.
    PRIDEi Q9R0X5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 19893.
    KEGGi mmu:19893.
    UCSCi uc009sqh.2. mouse.
    uc009sqj.2. mouse. [Q9R0X5-4 ]

    Organism-specific databases

    CTDi 6103.
    MGIi MGI:1344037. Rpgr.

    Phylogenomic databases

    eggNOGi COG5184.
    HOGENOMi HOG000231314.
    HOVERGENi HBG026899.
    InParanoidi Q9R0X5.
    TreeFami TF331400.

    Miscellaneous databases

    ChiTaRSi RPGR. mouse.
    NextBioi 297416.
    PROi Q9R0X5.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_RPGR.
    Genevestigatori Q9R0X5.

    Family and domain databases

    Gene3Di 2.130.10.30. 1 hit.
    InterProi IPR009091. RCC1/BLIP-II.
    IPR000408. Reg_chr_condens.
    [Graphical view ]
    Pfami PF00415. RCC1. 6 hits.
    [Graphical view ]
    PRINTSi PR00633. RCCNDNSATION.
    SUPFAMi SSF50985. SSF50985. 1 hit.
    PROSITEi PS00626. RCC1_2. 3 hits.
    PS50012. RCC1_3. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Biochemical characterization and subcellular localization of the mouse retinitis pigmentosa GTPase regulator."
      Yan D., Swain P.K., Breuer D., Tucker R.M., Wu W., Fujita R., Rehemtulla A., Burke D., Swaroop A.
      J. Biol. Chem. 273:19656-19663(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, ISOPRENYLATION.
      Tissue: Brain.
    2. "RPGR transcription studies in mouse and human tissues reveal a retina-specific isoform that is disrupted in a patient with X-linked retinitis pigmentosa."
      Kirschner R., Rosenberg T., Schultz-Heienbrok R., Lenzner S., Feil S., Roepman R., Cremers F.P.M., Ropers H.-H., Berger W.
      Hum. Mol. Genet. 8:1571-1578(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Testis.
    3. "DNA sequence comparison of human and mouse retinitis pigmentosa GTPase regulator (RPGR) identifies tissue-specific exons and putative regulatory elements."
      Kirschner R., Erturk D., Zeitz C., Sahin S., Ramser J., Cremers F.P.M., Ropers H.-H., Berger W.
      Hum. Genet. 109:271-278(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1).
      Strain: 129/SvEvTacfBr.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-845 (ISOFORMS 2/3).
      Strain: C57BL/6J.
      Tissue: Ovary and Uterus.
    6. "RpgrORF15 connects to the usher protein network through direct interactions with multiple whirlin isoforms."
      Wright R.N., Hong D.H., Perkins B.
      Invest. Ophthalmol. Vis. Sci. 53:1519-1529(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 525-1001 (ISOFORM 5), INTERACTION WITH DFNB31, TISSUE SPECIFICITY.
      Strain: 129/Sv.
    7. "The retinitis pigmentosa GTPase regulator, RPGR, interacts with the delta subunit of rod cyclic GMP phosphodiesterase."
      Linari M., Ueffing M., Manson F., Wright A., Meitinger T., Becker J.
      Proc. Natl. Acad. Sci. U.S.A. 96:1315-1320(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDE6D.
    8. "Species-specific subcellular localization of RPGR and RPGRIP isoforms: implications for the phenotypic variability of congenital retinopathies among species."
      Mavlyutov T.A., Zhao H., Ferreira P.A.
      Hum. Mol. Genet. 11:1899-1907(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    9. "RPGR ORF15 isoform co-localizes with RPGRIP1 at centrioles and basal bodies and interacts with nucleophosmin."
      Shu X., Fry A.M., Tulloch B., Manson F.D., Crabb J.W., Khanna H., Faragher A.J., Lennon A., He S., Trojan P., Giessl A., Wolfrum U., Vervoort R., Swaroop A., Wright A.F.
      Hum. Mol. Genet. 14:1183-1197(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    10. "RPGR-ORF15, which is mutated in retinitis pigmentosa, associates with SMC1, SMC3, and microtubule transport proteins."
      Khanna H., Hurd T.W., Lillo C., Shu X., Parapuram S.K., He S., Akimoto M., Wright A.F., Margolis B., Williams D.S., Swaroop A.
      J. Biol. Chem. 280:33580-33587(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMC1A AND SMC3, SUBCELLULAR LOCATION.
    11. "In-frame deletion in a novel centrosomal/ciliary protein CEP290/NPHP6 perturbs its interaction with RPGR and results in early-onset retinal degeneration in the rd16 mouse."
      Chang B., Khanna H., Hawes N., Jimeno D., He S., Lillo C., Parapuram S.K., Cheng H., Scott A., Hurd R.E., Sayer J.A., Otto E.A., Attanasio M., O'Toole J.F., Jin G., Shou C., Hildebrandt F., Williams D.S., Heckenlively J.R., Swaroop A.
      Hum. Mol. Genet. 15:1847-1857(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTS WITH CEP290, TISSUE SPECIFICITY.
    12. "Overexpression of RPGR leads to male infertility in mice due to defects in flagellar assembly."
      Brunner S., Colman D., Travis A.J., Luhmann U.F., Shi W., Feil S., Imsand C., Nelson J., Grimm C., Rulicke T., Fundele R., Neidhardt J., Berger W.
      Biol. Reprod. 79:608-617(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    13. Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    14. "Expression and localization of the ciliary disease protein retinitis pigmentosa GTPase regulator in mammalian kidney."
      Patil S.B., Verma R., Venkatareddy M., Khanna H.
      Kidney Int. 78:622-623(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    15. "Misexpression of the constitutive Rpgr(ex1-19) variant leads to severe photoreceptor degeneration."
      Wright R.N., Hong D.H., Perkins B.
      Invest. Ophthalmol. Vis. Sci. 52:5189-5201(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    16. "Rd9 is a naturally occurring mouse model of a common form of retinitis pigmentosa caused by mutations in RPGR-ORF15."
      Thompson D.A., Khan N.W., Othman M.I., Chang B., Jia L., Grahek G., Wu Z., Hiriyanna S., Nellissery J., Li T., Khanna H., Colosi P., Swaroop A., Heckenlively J.R.
      PLoS ONE 7:E35865-E35865(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MOUSE MODEL OF X-LINKED RETINOSA PIGMENTOSA.

    Entry informationi

    Entry nameiRPGR_MOUSE
    AccessioniPrimary (citable) accession number: Q9R0X5
    Secondary accession number(s): A2ADP3
    , G9BBQ2, O88408, Q9CU92
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: February 6, 2013
    Last modified: October 1, 2014
    This is version 118 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Male transgenic mice carrying multiple copies of the Rpgr transgene are infertile showing normal mating but no progeny; these mice also exhibit reduced sperm numbers as well as morphological and functional defects in the sperm flagellum.1 Publication
    Male BL/6 and BALB/c transgenic mice with an in-frame deletion of exon 4 of Rpgr show retinal degeneration that is rod or cone dominated, respectively.1 Publication
    Overexpression of isoform 1 results in atypical accumulation of Rpgr in photoreceptor outer segments, abnormal photoreceptor morphology and severe retinal degeneration.1 Publication
    In a mouse model of X-linked retinosa pigmentosa, where a 32bp duplication leads to a frameshift in the reading frame and a premature stop codon in isoform 5 (ORF15), mice exhibited retinal pathology including pigment loss and a slow progressive decrease in outer nuclear layer thickness.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3