Reviewed, UniProtKB/Swiss-Prot Q92834 (RPGR_HUMAN)

Names and origin

Protein names

Recommended name:
    X-linked retinitis pigmentosa GTPase regulator

Gene names

Name:	RPGR
Synonyms:	RP3, XLRP3

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1020 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Could be a guanine-nucleotide releasing factor.
Subunit structure	Interacts with RPGRIP1. Ref.8
Subcellular location	Golgi apparatus By similarity.
Tissue specificity	Heart, brain, placenta, lung, liver, muscle, kidney, retina, pancreas and fetal retinal pigment epithelium. Isoform 3 is found only in the retina. Colocalizes with RPGRIP1 in the outer segment of rod photoreceptors and cone outer segments. Ref.9
Post-translational modification	Prenylated By similarity.
Involvement in disease	Defects in RPGR are the cause of retinitis pigmentosa type 3 (RP3) [MIM:300389]; also known as X-linked retinitis pigmentosa 3 (XLRP-3). RP leads to degeneration of retinal photoreceptor cells. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. RP3 is a form of choroidoretinal degeneration which is distinguished from other types by the presence in heterozygous women, with no visual defects, of a brilliant, scintillating, golden-hued, patchy appearance most striking around the macula, called a tapetal-like retinal reflex. Ref.1 Ref.2 Ref.7 Ref.10 Ref.11 Ref.12 Ref.15 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Defects in RPGR are the cause of retinitis pigmentosa type 15 (RP15) [MIM:300029]. RP15 belongs to the X-linked forms of retinitis pigmentosa (XLRP) which are among the most severe, because of their early onset, often leading to significant vision loss before the 4th decade. Defects in RPGR are the cause of retinitis pigmentosa with deafness and sinorespiratory infections (RPDSI) [MIM:300455]. RPDSI is characterized by the association of primary ciliary dyskinesia and Usher syndrome features. The phenotype has similarities with primary ciliary dyskinesia and Usher syndrome. Defects in RPGR are the cause of cone-rod dystrophy X-linked type 1 (CORDX1) [MIM:304020]; also known as cone dystrophy 1 (CO1). CORDs are inherited retinal dystrophies belonging to the group of pigmentary retinopathies. CORDs are characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa. In CORDX1 the degree of rod-photoreceptor involvement can be variable, with degeneration increasing as the disease progresses. Affected individuals (essentially all of whom are males) present with decreased visual acuity, myopia, photophobia, abnormal color vision, full peripheral visual fields, decreased photopic electroretinographic responses, and granularity of the macular retinal pigment epithelium. Although penetrance appears to be nearly 100%, there is variable expressivity with respect to age at onset and severity of symptoms. Ref.19
Sequence similarities	Contains 6 RCC1 repeats.

Ontologies

Keywords
Biological process	Sensory transduction Vision
Cellular component	Golgi apparatus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Cone-rod dystrophy Deafness Disease mutation Retinitis pigmentosa
Domain	Repeat
Molecular function	Guanine-nucleotide releasing factor
PTM	Lipoprotein Methylation Prenylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	intracellular protein transport Traceable author statement. Source: ProtInc response to stimulus Inferred from electronic annotation. Source: UniProtKB-KW visual perception Ref.10 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	Golgi apparatus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	guanyl-nucleotide exchange factor activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q92834-1)

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.

Isoform 2 (identifier: Q92834-2)

The sequence of this isoform differs from the canonical sequence as follows:
     585-789: Missing.

Isoform 3 (identifier: Q92834-3)

The sequence of this isoform differs from the canonical sequence as follows:
     585-789: Missing.
     841-851: DHEFSKTEELK → YSASHSQIVSV
     852-1020: Missing.

Isoform 4 (identifier: Q92834-4)

The sequence of this isoform differs from the canonical sequence as follows:
     354-415: Missing.
     585-789: Missing.

Isoform 5 (identifier: Q92834-5)

The sequence of this isoform differs from the canonical sequence as follows:
     473-480: YLLDEMTK → THHEPEFQ
     481-1020: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1017	1017	X-linked retinitis pigmentosa GTPase regulator		PRO_0000206638
	Propeptide	1018 – 1020	3	Removed in mature form Potential		PRO_0000370844
Regions
	Repeat	54 – 105	52	RCC1 1
	Repeat	106 – 158	53	RCC1 2
	Repeat	159 – 208	50	RCC1 3
	Repeat	209 – 261	53	RCC1 4
	Repeat	262 – 313	52	RCC1 5
	Repeat	314 – 367	54	RCC1 6
	Compositional bias	530 – 903	374	Glu-rich
Amino acid modifications
	Modified residue	1017	1	Cysteine methyl ester Potential
	Lipidation	1017	1	S-geranylgeranyl cysteine Potential
Natural variations
	Alternative sequence	354 – 415	62	Missing in isoform 4.		VSP_005547
	Alternative sequence	473 – 480	8	YLLDEMTK → THHEPEFQ in isoform 5.		VSP_009183
	Alternative sequence	481 – 1020	540	Missing in isoform 5.		VSP_009184
	Alternative sequence	585 – 789	205	Missing in isoform 2, isoform 3 and isoform 4.		VSP_005548
	Alternative sequence	841 – 851	11	DHEFSKTEELK → YSASHSQIVSV in isoform 3.		VSP_005549
	Alternative sequence	852 – 1020	169	Missing in isoform 3.		VSP_005550
	Natural variant	43	1	G → E in RP3. Ref.17		VAR_018057
	Natural variant	43	1	G → R in RP3. Ref.17		VAR_018058
	Natural variant	60	1	G → V in RP3. Ref.10 Ref.11 Ref.17		VAR_008501
	Natural variant	75	1	I → V in RP3; could be a polymorphism. Ref.10		VAR_008503
	Natural variant	76	1	S → I: dbSNP rs1801685. Ref.13		VAR_013624
	Natural variant	98	1	H → Q in RP3. Ref.1 Ref.7		VAR_008504
	Natural variant	99	1	T → N in RP3. Ref.12		VAR_013625
	Natural variant	127	1	R → G in RP3. Ref.17 Ref.20		VAR_018059
	Natural variant	130	1	F → C in RP3. Ref.2		VAR_006850
	Natural variant	152	1	S → L in RP3. Ref.22		VAR_025949
	Natural variant	173	1	G → R in RP3 and RPDSI. Ref.20 Ref.24		VAR_018060
	Natural variant	184	1	Q → H: dbSNP rs5963403.		VAR_033259
	Natural variant	215	1	G → V in RP3. Ref.1 Ref.22		VAR_008505
	Natural variant	235	1	P → S in RP3. Ref.2		VAR_006851
	Natural variant	250	1	C → R in RP3. Ref.1 Ref.7		VAR_008506
	Natural variant	250	1	C → Y in RP3. Ref.20		VAR_018061
	Natural variant	258	1	Missing in RP3.		VAR_018062
	Natural variant	262	1	A → G in RP3; could be a polymorphism. Ref.10		VAR_008507
	Natural variant	267	1	G → E in RP3.		VAR_018063
	Natural variant	267	1	G → R in RP3. Ref.20		VAR_026127
	Natural variant	275	1	G → S in RP3. Ref.2		VAR_006852
	Natural variant	285	1	E → G in RP3. Ref.20		VAR_026128
	Natural variant	289	1	I → V in RP3. Ref.12		VAR_013626
	Natural variant	296 – 300	5	Missing in RP3.		VAR_013627
	Natural variant	302	1	C → R in RP3. Ref.15		VAR_011561
	Natural variant	302	1	C → Y in RP3. Ref.17		VAR_018064
	Natural variant	312	1	D → N in RP3. Ref.21		VAR_018065
	Natural variant	312	1	D → Y in RP3. Ref.21		VAR_018066
	Natural variant	320	1	G → R in RP3. Ref.21		VAR_018067
	Natural variant	345	1	N → D Rare polymorphism. dbSNP rs41305223. Ref.17 Ref.19		VAR_018068
	Natural variant	425	1	R → K: dbSNP rs1801687. Ref.10 Ref.17 Ref.13 Ref.16		VAR_008508
	Natural variant	431	1	I → V		VAR_008509
	Natural variant	436	1	G → D in RP3. Ref.17 Ref.18 Ref.20		VAR_008510
	Natural variant	526	1	Missing		VAR_011562
	Natural variant	533	1	T → M: dbSNP rs41312104. Ref.16		VAR_011563
	Natural variant	566	1	G → E: dbSNP rs1801688. Ref.10 Ref.17 Ref.13 Ref.16		VAR_008511
Experimental info
	Sequence conflict	1 – 3	3	MRE → MAKLRRSTTTAL Ref.4
	Sequence conflict	190	1	K → N in CAC86116. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 19, 2002. Version 2. Checksum: EAB16275A9A436C3	FASTA	1,020	113,387
	10 20 30 40 50 60 MREPEELMPD SGAVFTFGKS KFAENNPGKF WFKNDVPVHL SCGDEHSAVV TGNNKLYMFG 70 80 90 100 110 120 SNNWGQLGLG SKSAISKPTC VKALKPEKVK LAACGRNHTL VSTEGGNVYA TGGNNEGQLG 130 140 150 160 170 180 LGDTEERNTF HVISFFTSEH KIKQLSAGSN TSAALTEDGR LFMWGDNSEG QIGLKNVSNV 190 200 210 220 230 240 CVPQQVTIGK PVSWISCGYY HSAFVTTDGE LYVFGEPENG KLGLPNQLLG NHRTPQLVSE 250 260 270 280 290 300 IPEKVIQVAC GGEHTVVLTE NAVYTFGLGQ FGQLGLGTFL FETSEPKVIE NIRDQTISYI 310 320 330 340 350 360 SCGENHTALI TDIGLMYTFG DGRHGKLGLG LENFTNHFIP TLCSNFLRFI VKLVACGGCH 370 380 390 400 410 420 MVVFAAPHRG VAKEIEFDEI NDTCLSVATF LPYSSLTSGN VLQRTLSARM RRRERERSPD 430 440 450 460 470 480 SFSMRRTLPP IEGTLGLSAC FLPNSVFPRC SERNLQESVL SEQDLMQPEE PDYLLDEMTK 490 500 510 520 530 540 EAEIDNSSTV ESLGETTDIL NMTHIMSLNS NEKSLKLSPV QKQKKQQTIG ELTQDTALTE 550 560 570 580 590 600 NDDSDEYEEM SEMKEGKACK QHVSQGIFMT QPATTIEAFS DEEVGNDTGQ VGPQADTDGE 610 620 630 640 650 660 GLQKEVYRHE NNNGVDQLDA KEIEKESDGG HSQKESEAEE IDSEKETKLA EIAGMKDLRE 670 680 690 700 710 720 REKSTKKMSP FFGNLPDRGM NTESEENKDF VKKRESCKQD VIFDSERESV EKPDSYMEGA 730 740 750 760 770 780 SESQQGIADG FQQPEAIEFS SGEKEDDEVE TDQNIRYGRK LIEQGNEKET KPIISKSMAK 790 800 810 820 830 840 YDFKCDRLSE IPEEKEGAED SKGNGIEEQE VEANEENVKV HGGRKEKTEI LSDDLTDKAE 850 860 870 880 890 900 DHEFSKTEEL KLEDVDEEIN AENVESKKKT VGDDESVPTG YHSKTEGAER TNDDSSAETI 910 920 930 940 950 960 EKKEKANLEE RAICEYNENP KGYMLDDADS SSLEILENSE TTPSKDMKKT KKIFLFKRVP 970 980 990 1000 1010 1020 SINQKIVKNN NEPLPEIKSI GDQIILKSDN KDADQNHMSQ NHQNIPPTNT ERRSKSCTIL
	Isoform 2. Checksum: 70D84EAD988348D1	FASTA	815	90,245
	10 20 30 40 50 60 MREPEELMPD SGAVFTFGKS KFAENNPGKF WFKNDVPVHL SCGDEHSAVV TGNNKLYMFG 70 80 90 100 110 120 SNNWGQLGLG SKSAISKPTC VKALKPEKVK LAACGRNHTL VSTEGGNVYA TGGNNEGQLG 130 140 150 160 170 180 LGDTEERNTF HVISFFTSEH KIKQLSAGSN TSAALTEDGR LFMWGDNSEG QIGLKNVSNV 190 200 210 220 230 240 CVPQQVTIGK PVSWISCGYY HSAFVTTDGE LYVFGEPENG KLGLPNQLLG NHRTPQLVSE 250 260 270 280 290 300 IPEKVIQVAC GGEHTVVLTE NAVYTFGLGQ FGQLGLGTFL FETSEPKVIE NIRDQTISYI 310 320 330 340 350 360 SCGENHTALI TDIGLMYTFG DGRHGKLGLG LENFTNHFIP TLCSNFLRFI VKLVACGGCH 370 380 390 400 410 420 MVVFAAPHRG VAKEIEFDEI NDTCLSVATF LPYSSLTSGN VLQRTLSARM RRRERERSPD 430 440 450 460 470 480 SFSMRRTLPP IEGTLGLSAC FLPNSVFPRC SERNLQESVL SEQDLMQPEE PDYLLDEMTK 490 500 510 520 530 540 EAEIDNSSTV ESLGETTDIL NMTHIMSLNS NEKSLKLSPV QKQKKQQTIG ELTQDTALTE 550 560 570 580 590 600 NDDSDEYEEM SEMKEGKACK QHVSQGIFMT QPATTIEAFS DEEVEIPEEK EGAEDSKGNG 610 620 630 640 650 660 IEEQEVEANE ENVKVHGGRK EKTEILSDDL TDKAEDHEFS KTEELKLEDV DEEINAENVE 670 680 690 700 710 720 SKKKTVGDDE SVPTGYHSKT EGAERTNDDS SAETIEKKEK ANLEERAICE YNENPKGYML 730 740 750 760 770 780 DDADSSSLEI LENSETTPSK DMKKTKKIFL FKRVPSINQK IVKNNNEPLP EIKSIGDQII 790 800 810 LKSDNKDADQ NHMSQNHQNI PPTNTERRSK SCTIL
	Isoform 3. Checksum: BE8E98184F0404A6	FASTA	646	70,981
	10 20 30 40 50 60 MREPEELMPD SGAVFTFGKS KFAENNPGKF WFKNDVPVHL SCGDEHSAVV TGNNKLYMFG 70 80 90 100 110 120 SNNWGQLGLG SKSAISKPTC VKALKPEKVK LAACGRNHTL VSTEGGNVYA TGGNNEGQLG 130 140 150 160 170 180 LGDTEERNTF HVISFFTSEH KIKQLSAGSN TSAALTEDGR LFMWGDNSEG QIGLKNVSNV 190 200 210 220 230 240 CVPQQVTIGK PVSWISCGYY HSAFVTTDGE LYVFGEPENG KLGLPNQLLG NHRTPQLVSE 250 260 270 280 290 300 IPEKVIQVAC GGEHTVVLTE NAVYTFGLGQ FGQLGLGTFL FETSEPKVIE NIRDQTISYI 310 320 330 340 350 360 SCGENHTALI TDIGLMYTFG DGRHGKLGLG LENFTNHFIP TLCSNFLRFI VKLVACGGCH 370 380 390 400 410 420 MVVFAAPHRG VAKEIEFDEI NDTCLSVATF LPYSSLTSGN VLQRTLSARM RRRERERSPD 430 440 450 460 470 480 SFSMRRTLPP IEGTLGLSAC FLPNSVFPRC SERNLQESVL SEQDLMQPEE PDYLLDEMTK 490 500 510 520 530 540 EAEIDNSSTV ESLGETTDIL NMTHIMSLNS NEKSLKLSPV QKQKKQQTIG ELTQDTALTE 550 560 570 580 590 600 NDDSDEYEEM SEMKEGKACK QHVSQGIFMT QPATTIEAFS DEEVEIPEEK EGAEDSKGNG 610 620 630 640 IEEQEVEANE ENVKVHGGRK EKTEILSDDL TDKAEYSASH SQIVSV
	Isoform 4. Checksum: A84202BD00B84930	FASTA	753	83,394
	10 20 30 40 50 60 MREPEELMPD SGAVFTFGKS KFAENNPGKF WFKNDVPVHL SCGDEHSAVV TGNNKLYMFG 70 80 90 100 110 120 SNNWGQLGLG SKSAISKPTC VKALKPEKVK LAACGRNHTL VSTEGGNVYA TGGNNEGQLG 130 140 150 160 170 180 LGDTEERNTF HVISFFTSEH KIKQLSAGSN TSAALTEDGR LFMWGDNSEG QIGLKNVSNV 190 200 210 220 230 240 CVPQQVTIGK PVSWISCGYY HSAFVTTDGE LYVFGEPENG KLGLPNQLLG NHRTPQLVSE 250 260 270 280 290 300 IPEKVIQVAC GGEHTVVLTE NAVYTFGLGQ FGQLGLGTFL FETSEPKVIE NIRDQTISYI 310 320 330 340 350 360 SCGENHTALI TDIGLMYTFG DGRHGKLGLG LENFTNHFIP TLCSNFLRFI VKLERSPDSF 370 380 390 400 410 420 SMRRTLPPIE GTLGLSACFL PNSVFPRCSE RNLQESVLSE QDLMQPEEPD YLLDEMTKEA 430 440 450 460 470 480 EIDNSSTVES LGETTDILNM THIMSLNSNE KSLKLSPVQK QKKQQTIGEL TQDTALTEND 490 500 510 520 530 540 DSDEYEEMSE MKEGKACKQH VSQGIFMTQP ATTIEAFSDE EVEIPEEKEG AEDSKGNGIE 550 560 570 580 590 600 EQEVEANEEN VKVHGGRKEK TEILSDDLTD KAEDHEFSKT EELKLEDVDE EINAENVESK 610 620 630 640 650 660 KKTVGDDESV PTGYHSKTEG AERTNDDSSA ETIEKKEKAN LEERAICEYN ENPKGYMLDD 670 680 690 700 710 720 ADSSSLEILE NSETTPSKDM KKTKKIFLFK RVPSINQKIV KNNNEPLPEI KSIGDQIILK 730 740 750 SDNKDADQNH MSQNHQNIPP TNTERRSKSC TIL
	Isoform 5. Checksum: 6766EA259A232631	FASTA	480	52,628
	10 20 30 40 50 60 MREPEELMPD SGAVFTFGKS KFAENNPGKF WFKNDVPVHL SCGDEHSAVV TGNNKLYMFG 70 80 90 100 110 120 SNNWGQLGLG SKSAISKPTC VKALKPEKVK LAACGRNHTL VSTEGGNVYA TGGNNEGQLG 130 140 150 160 170 180 LGDTEERNTF HVISFFTSEH KIKQLSAGSN TSAALTEDGR LFMWGDNSEG QIGLKNVSNV 190 200 210 220 230 240 CVPQQVTIGK PVSWISCGYY HSAFVTTDGE LYVFGEPENG KLGLPNQLLG NHRTPQLVSE 250 260 270 280 290 300 IPEKVIQVAC GGEHTVVLTE NAVYTFGLGQ FGQLGLGTFL FETSEPKVIE NIRDQTISYI 310 320 330 340 350 360 SCGENHTALI TDIGLMYTFG DGRHGKLGLG LENFTNHFIP TLCSNFLRFI VKLVACGGCH 370 380 390 400 410 420 MVVFAAPHRG VAKEIEFDEI NDTCLSVATF LPYSSLTSGN VLQRTLSARM RRRERERSPD 430 440 450 460 470 480 SFSMRRTLPP IEGTLGLSAC FLPNSVFPRC SERNLQESVL SEQDLMQPEE PDTHHEPEFQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A gene (RPGR) with homology to the RCC1 guanine nucleotide exchange factor is mutated in X-linked retinitis pigmentosa (RP3)." Meindl A., Dry K.L., Herrmann K., Manson F.D., Ciccodicola A., Edgar A.J., Carvalho M.R.S., Achatz H., Hellebrand H., Lennon A.A., Migliaccio C., Porter K., Zrenner E., Bird A.C., Jay M., Lorenz B., Wittwer B., D'Urso M., Meitinger T., Wright A.F. Nat. Genet. 13:35-42(1996) [PubMed: 8673101] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), VARIANTS RP3 GLN-98; VAL-215; ARG-250 AND 296-THR--ILE-300 DEL.
[2]	"Positional cloning of the gene for X-linked retinitis pigmentosa 3: homology with the guanine-nucleotide-exchange factor RCC1." Roepman R., van Duijnhoven G., Rosenberg T., Pinckers A.J.L.G., Bleeker-Wagemakers L.M., Bergen A.A.B., Post J., Beck A., Reinhardt R., Ropers H.-H., Cremers F., Berger W. Hum. Mol. Genet. 5:1035-1041(1996) [PubMed: 8817343] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS RP3 CYS-130; SER-235 AND SER-275. Tissue: Retina.
[3]	Berger W. Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[4]	"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: 10401007] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3). Tissue: Retina.
[5]	"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: 11702207] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
[7]	"Mutational hot spot within a new RPGR exon in X-linked retinitis pigmentosa." Vervoort R., Lennon A.A., Bird A.C., Tulloch B., Axton R., Miano M.G., Meindl A., Meitinger T., Ciccodicola A., Wright A.F. Nat. Genet. 25:462-466(2000) [PubMed: 10932196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 525-840 (ISOFORM 1), VARIANTS RP3 GLN-98 AND ARG-250.
[8]	"The retinitis pigmentosa GTPase regulator (RPGR) interacts with novel transport-like proteins in the outer segments of rod photoreceptors." Roepman R., Bernoud-Hubac N., Schick D.E., Maugeri A., Berger W., Ropers H.-H., Cremers F.P.M., Ferreira P.A. Hum. Mol. Genet. 9:2095-2105(2000) [PubMed: 10958648] [Abstract] Cited for: INTERACTION WITH RPGRIP1.
[9]	"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: 12140192] [Abstract] Cited for: TISSUE SPECIFICITY.
[10]	"Spectrum of mutations in the RPGR gene that are identified in 20% of families with X-linked retinitis pigmentosa." Buraczynska M., Wu W., Fujita R., Buraczynska K., Phelps E., Andreasson S., Bennett J., Birch D.G., Fishman G.A., Hoffman D.R., Inana G., Jacobson S.G., Musarella M.A., Sieving P.A., Swaroop A. Am. J. Hum. Genet. 61:1287-1292(1997) [PubMed: 9399904] [Abstract] Cited for: VARIANTS RP3 VAL-60; VAL-75 AND GLY-262, VARIANTS LYS-425; VAL-431 AND GLU-566.
[11]	"X-linked retinitis pigmentosa in two families with a missense mutation in the RPGR gene and putative change of glycine to valine at codon 60." Fishman G.A., Grover S., Jacobson S.G., Alexander K.R., Derlacki D.J., Wu W., Buraczynska M., Swaroop A. Ophthalmology 105:2286-2296(1998) [PubMed: 9855162] [Abstract] Cited for: VARIANT RP3 VAL-60.
[12]	"Mutation analysis of the RPGR gene reveals novel mutations in south European patients with X-linked retinitis pigmentosa." Miano M.G., Testa F., Strazzullo M., Trujillo M., De Bernardo C., Grammatico B., Simonelli F., Mangino M., Torrente I., Ruberto G., Beneyto M., Antinolo G., Rinaldi E., Danesino C., Ventruto V., D'Urso M., Ayuso C., Baiget M., Ciccodicola A. Eur. J. Hum. Genet. 7:687-694(1999) [PubMed: 10482958] [Abstract] Cited for: VARIANTS RP3 ASN-99 AND VAL-289.
[13]	"Identification of novel RPGR (retinitis pigmentosa GTPase regulator) mutations in a subset of X-linked retinitis pigmentosa families segregating with the RP3 locus." Zito I., Thiselton D.L., Gorin M.B., Stout J.T., Plant C., Bird A.C., Bhattacharya S.S., Hardcastle A.J. Hum. Genet. 105:57-62(1999) [PubMed: 10480356] [Abstract] Cited for: VARIANTS ILE-76; LYS-425 AND GLU-566.
[14]	"Remapping of the RP15 locus for X-linked cone-rod degeneration to Xp11.4-p21.1, and identification of a de novo insertion in the RPGR exon ORF15." Mears A.J., Hiriyanna S., Vervoort R., Yashar B., Gieser L., Fahrner S., Daiger S.P., Heckenlively J.R., Sieving P.A., Wright A.F., Swaroop A. Am. J. Hum. Genet. 67:1000-1003(2000) [PubMed: 10970770] [Abstract] Cited for: INVOLVEMENT IN RP15.
[15]	"Novel mutations of the RPGR gene in RP3 families." Zito I., Gorin M.B., Plant C., Bird A.C., Bhattacharya S.S., Hardcastle A.J. Hum. Mutat. 15:386-386(2000) [PubMed: 10737996] [Abstract] Cited for: VARIANT RP3 ARG-302.
[16]	"Sequence variation within the RPGR gene: evidence for a founder complex allele." Zito I., Morris A., Tyson P., Winship I., Sharp D., Gilbert D., Thiselton D.L., Bhattacharya S.S., Hardcastle A.J. Hum. Mutat. 16:273-274(2000) [PubMed: 10980543] [Abstract] Cited for: VARIANTS LYS-425; GLN-526 DEL; MET-533 AND GLU-566.
[17]	"X-linked retinitis pigmentosa: mutation spectrum of the RPGR and RP2 genes and correlation with visual function." Sharon D., Bruns G.A.P., McGee T.L., Sandberg M.A., Berson E.L., Dryja T.P. Invest. Ophthalmol. Vis. Sci. 41:2712-2721(2000) [PubMed: 10937588] [Abstract] Cited for: VARIANTS RP3 ARG-43; GLU-43; VAL-60; GLY-127; TYR-302 AND ASP-436, VARIANTS ASP-345; LYS-425; VAL-431 AND GLU-566.
[18]	"Five novel RPGR mutations in families with X-linked retinitis pigmentosa." Guevara-Fujita M., Fahrner S., Buraczynska K., Cook J., Wheaton D., Cortes F., Vicencio C., Pena M., Fishman G.A., Mintz-Hittner H., Birch D.G., Hoffman D.R., Mears A.J., Fujita R., Swaroop A. Hum. Mutat. 17:151-151(2001) [PubMed: 11180598] [Abstract] Cited for: VARIANT RP3 ASP-436.
[19]	"X-linked cone-rod dystrophy (locus COD1): identification of mutations in RPGR exon ORF15." Demirci F.Y.K., Rigatti B.W., Wen G., Radak A.L., Mah T.S., Baic C.L., Traboulsi E.I., Alitalo T., Ramser J., Gorin M.B. Am. J. Hum. Genet. 70:1049-1053(2002) [PubMed: 11857109] [Abstract] Cited for: INVOLVEMENT IN CORDX1, VARIANT ASP-345.
[20]	"A comprehensive mutation analysis of RP2 and RPGR in a North American cohort of families with X-linked retinitis pigmentosa." Breuer D.K., Yashar B.M., Filippova E., Hiriyanna S., Lyons R.H., Mears A.J., Asaye B., Acar C., Vervoort R., Wright A.F., Musarella M.A., Wheeler P., MacDonald I., Iannaccone A., Birch D., Hoffman D.R., Fishman G.A., Heckenlively J.R. , Jacobson S.G., Sieving P.A., Swaroop A. Am. J. Hum. Genet. 70:1545-1554(2002) [PubMed: 11992260] [Abstract] Cited for: VARIANTS RP3 GLY-127; ARG-173; TYR-250; LEU-258 DEL; ARG-267; GLY-285 AND ASP-436.
[21]	"RP2 and RPGR mutations and clinical correlations in patients with X-linked retinitis pigmentosa." Sharon D., Sandberg M.A., Rabe V.W., Stillberger M., Dryja T.P., Berson E.L. Am. J. Hum. Genet. 73:1131-1146(2003) [PubMed: 14564670] [Abstract] Cited for: VARIANTS RP3 ASN-312; TYR-312 AND ARG-320.
[22]	"X-linked retinitis pigmentosa: RPGR mutations in most families with definite X linkage and clustering of mutations in a short sequence stretch of exon ORF15." Bader I., Brandau O., Achatz H., Apfelstedt-Sylla E., Hergersberg M., Lorenz B., Wissinger B., Wittwer B., Rudolph G., Meindl A., Meitinger T. Invest. Ophthalmol. Vis. Sci. 44:1458-1463(2003) [PubMed: 12657579] [Abstract] Cited for: VARIANTS RP3 LEU-152 AND VAL-215.
[23]	"RPGR mutation associated with retinitis pigmentosa, impaired hearing, and sinorespiratory infections." Zito I., Downes S.M., Patel R.J., Cheetham M.E., Ebenezer N.D., Jenkins S.A., Bhattacharya S.S., Webster A.R., Holder G.E., Bird A.C., Bamiou D.E., Hardcastle A.J. J. Med. Genet. 40:609-615(2003) [PubMed: 12920075] [Abstract] Cited for: INVOLVEMENT IN RPDSI.
[24]	"Clinical and immunohistochemical evidence for an X linked retinitis pigmentosa syndrome with recurrent infections and hearing loss in association with an RPGR mutation." Iannaccone A., Breuer D.K., Wang X.F., Kuo S.F., Normando E.M., Filippova E., Baldi A., Hiriyanna S., MacDonald C.B., Baldi F., Cosgrove D., Morton C.C., Swaroop A., Jablonski M.M. J. Med. Genet. 40:E118-E118(2003) [PubMed: 14627685] [Abstract] Cited for: VARIANT RPDSI ARG-173.
+	Additional computationally mapped references.

Web resources

Mutations of the RPGR gene

Retina International's Scientific Newsletter

GeneReviews

Cross-references

Sequence databases
EMBLGenBankDDBJ	U57629 mRNA. Translation: AAC50481.1. X97668 mRNA. Translation: CAA66258.1. AJ238395 mRNA. Translation: CAB54002.1. AJ318463 Genomic DNA. Translation: CAC86116.1. BC031624 mRNA. Translation: AAH31624.1. AF286471 Genomic DNA. Translation: AAG00550.1.
IPI	IPI00023757. IPI00215806. IPI00215807. IPI00215808. IPI00397031.
RefSeq	NP_000319.1.
UniGene	Hs.61438
3D structure databases
HSSP	HSSP built from PDB template 1I2M based on UniProtKB P18754.
ModBase	Search...
Protein-protein interaction databases
STRING	Q92834.
PTM databases
PhosphoSite	Q92834.
Proteomic databases
PRIDE	Q92834.
Genome annotation databases
Ensembl	ENST00000309513; ENSP00000308783; ENSG00000156313; Homo sapiens. [Genome view] ENST00000318842; ENSP00000322219; ENSG00000156313; Homo sapiens. [Genome view] ENST00000338898; ENSP00000340208; ENSG00000156313; Homo sapiens. [Genome view] ENST00000339363; ENSP00000343671; ENSG00000156313; Homo sapiens. [Genome view] ENST00000342811; ENSP00000339531; ENSG00000156313; Homo sapiens. [Genome view] ENST00000378505; ENSP00000367766; ENSG00000156313; Homo sapiens. [Genome view]
GeneID	6103.
KEGG	hsa:6103.
UCSC	uc004deb.1. human.
Organism-specific databases
CTD	6103.
GeneCards	GC0XM038013.
H-InvDB	HIX0016727.
HGNC	HGNC:10295. RPGR.
HPA	HPA001593.
MIM	300029. phenotype. 300389. phenotype. 300455. phenotype. 304020. phenotype. 312610. gene.
Orphanet	49382. Achromatopsia. 1872. Cone rod dystrophy. 244. Primary ciliary dyskinesia. 791. Retinitis pigmentosa.
PharmGKB	PA34656.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q92834.
OMA	NNNEPLP.
Gene expression databases
ArrayExpress	Q92834.
Bgee	Q92834.
CleanEx	HS_RPGR.
Genevestigator	Q92834.
GermOnline	ENSG00000156313. Homo sapiens.
Family and domain databases
InterPro	IPR000408. Reg_chr_condens. IPR009091. Reg_csome_cond/b-lactamase_inh. [Graphical view]
Gene3D	G3DSA:2.130.10.30. Reg_csome_cond/b-lactamase_inh. 1 hit.
Pfam	PF00415. RCC1. 4 hits. [Graphical view]
PRINTS	PR00633. RCCNDNSATION.
PROSITE	PS00625. RCC1_1. False negative. PS00626. RCC1_2. 4 hits. PS50012. RCC1_3. 6 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	23741.
SOURCE	Search...

Entry information

Entry name

RPGR_HUMAN

Accession

Primary (citable) accession number: Q92834
Secondary accession number(s): O00702 , O00737, Q8N5T6, Q93039, Q9HD29, Q9UMR1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	September 19, 2002
Last modified:	November 3, 2009
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.