[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), AND VARIANTS RP3 GLN-98; VAL-215; ARG-250 AND 296-THR--ILE-300 DEL. DOI=10.1038/ng0596-35; PubMed=8673101 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "A gene (RPGR) with homology to the RCC1 guanine nucleotide exchange factor is mutated in X-linked retinitis pigmentosa (RP3)."; Nat. Genet. 13:35-42(1996).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS RP3 CYS-130; SER-235 AND SER-275. TISSUE=Retina; DOI=10.1093/hmg/5.7.1035; PubMed=8817343 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Positional cloning of the gene for X-linked retinitis pigmentosa 3: homology with the guanine-nucleotide-exchange factor RCC1."; Hum. Mol. Genet. 5:1035-1041(1996).
[3]	SEQUENCE REVISION. Berger W.; Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3). TISSUE=Retina; DOI=10.1093/hmg/8.8.1571; PubMed=10401007 [NCBI, ExPASy, EBI, Israel, Japan] Kirschner R., Rosenberg T., Schultz-Heienbrok R., Lenzner S., Feil S., Roepman R., Cremers F.P.M., Ropers H.-H., Berger W.; "RPGR transcription studies in mouse and human tissues reveal a retina-specific isoform that is disrupted in a patient with X-linked retinitis pigmentosa."; Hum. Mol. Genet. 8:1571-1578(1999).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2). DOI=10.1007/s004390100572; PubMed=11702207 [NCBI, ExPASy, EBI, Israel, Japan] Kirschner R., Erturk D., Zeitz C., Sahin S., Ramser J., Cremers F.P.M., Ropers H.-H., Berger W.; "DNA sequence comparison of human and mouse retinitis pigmentosa GTPase regulator (RPGR) identifies tissue-specific exons and putative regulatory elements."; Hum. Genet. 109:271-278(2001).
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[7]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 525-840 (ISOFORM 1), AND VARIANTS RP3 GLN-98 AND ARG-250. DOI=10.1038/78182; PubMed=10932196 [NCBI, ExPASy, EBI, Israel, Japan] Vervoort R., Lennon A.A., Bird A.C., Tulloch B., Axton R., Miano M.G., Meindl A., Meitinger T., Ciccodicola A., Wright A.F.; "Mutational hot spot within a new RPGR exon in X-linked retinitis pigmentosa."; Nat. Genet. 25:462-466(2000).
[8]	INTERACTION WITH RPGRIP1. DOI=10.1093/hmg/9.14.2095; PubMed=10958648 [NCBI, ExPASy, EBI, Israel, Japan] Roepman R., Bernoud-Hubac N., Schick D.E., Maugeri A., Berger W., Ropers H.-H., Cremers F.P.M., Ferreira P.A.; "The retinitis pigmentosa GTPase regulator (RPGR) interacts with novel transport-like proteins in the outer segments of rod photoreceptors."; Hum. Mol. Genet. 9:2095-2105(2000).
[9]	TISSUE SPECIFICITY. DOI=10.1093/hmg/11.16.1899; PubMed=12140192 [NCBI, ExPASy, EBI, Israel, Japan] Mavlyutov T.A., Zhao H., Ferreira P.A.; "Species-specific subcellular localization of RPGR and RPGRIP isoforms: implications for the phenotypic variability of congenital retinopathies among species."; Hum. Mol. Genet. 11:1899-1907(2002).
[10]	VARIANTS RP3 VAL-60; VAL-75 AND GLY-262, AND VARIANTS LYS-425; VAL-431 AND GLU-566. DOI=10.1086/301646; PubMed=9399904 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Spectrum of mutations in the RPGR gene that are identified in 20% of families with X-linked retinitis pigmentosa."; Am. J. Hum. Genet. 61:1287-1292(1997).
[11]	VARIANT RP3 VAL-60. DOI=10.1016/S0161-6420(98)91231-3; PubMed=9855162 [NCBI, ExPASy, EBI, Israel, Japan] Fishman G.A., Grover S., Jacobson S.G., Alexander K.R., Derlacki D.J., Wu W., Buraczynska M., Swaroop A.; "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."; Ophthalmology 105:2286-2296(1998).
[12]	VARIANTS RP3 ASN-99 AND VAL-289. DOI=10.1038/sj.ejhg.5200352; PubMed=10482958 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Mutation analysis of the RPGR gene reveals novel mutations in south European patients with X-linked retinitis pigmentosa."; Eur. J. Hum. Genet. 7:687-694(1999).
[13]	VARIANTS ILE-76; LYS-425 AND GLU-566. DOI=10.1007/s004390051064; PubMed=10480356 [NCBI, ExPASy, EBI, Israel, Japan] Zito I., Thiselton D.L., Gorin M.B., Stout J.T., Plant C., Bird A.C., Bhattacharya S.S., Hardcastle A.J.; "Identification of novel RPGR (retinitis pigmentosa GTPase regulator) mutations in a subset of X-linked retinitis pigmentosa families segregating with the RP3 locus."; Hum. Genet. 105:57-62(1999).
[14]	INVOLVEMENT IN RP15. DOI=10.1086/303091; PubMed=10970770 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "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."; Am. J. Hum. Genet. 67:1000-1003(2000).
[15]	VARIANT RP3 ARG-302. DOI=10.1002/(SICI)1098-1004(200004)15:4<386::AID-HUMU23>3.0.CO;2-4; PubMed=10737996 [NCBI, ExPASy, EBI, Israel, Japan] Zito I., Gorin M.B., Plant C., Bird A.C., Bhattacharya S.S., Hardcastle A.J.; "Novel mutations of the RPGR gene in RP3 families."; Hum. Mutat. 15:386-386(2000).
[16]	VARIANTS LYS-425; GLN-526 DEL; MET-533 AND GLU-566. DOI=10.1002/1098-1004(200009)16:3<273::AID-HUMU19>3.0.CO;2-W; PubMed=10980543 [NCBI, ExPASy, EBI, Israel, Japan] Zito I., Morris A., Tyson P., Winship I., Sharp D., Gilbert D., Thiselton D.L., Bhattacharya S.S., Hardcastle A.J.; "Sequence variation within the RPGR gene: evidence for a founder complex allele."; Hum. Mutat. 16:273-274(2000).
[17]	VARIANTS RP3 ARG-43; GLU-43; VAL-60; GLY-127; TYR-302 AND ASP-436, AND VARIANTS ASP-345; LYS-425; VAL-431 AND GLU-566. PubMed=10937588 [NCBI, ExPASy, EBI, Israel, Japan] Sharon D., Bruns G.A.P., McGee T.L., Sandberg M.A., Berson E.L., Dryja T.P.; "X-linked retinitis pigmentosa: mutation spectrum of the RPGR and RP2 genes and correlation with visual function."; Invest. Ophthalmol. Vis. Sci. 41:2712-2721(2000).
[18]	VARIANT RP3 ASP-436. DOI=10.1002/1098-1004(200102)17:2<151::AID-HUMU7>3.3.CO;2-N; PubMed=11180598 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Five novel RPGR mutations in families with X-linked retinitis pigmentosa."; Hum. Mutat. 17:151-151(2001).
[19]	INVOLVEMENT IN CORDX1, AND VARIANT ASP-345. DOI=10.1086/339620; PubMed=11857109 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "X-linked cone-rod dystrophy (locus COD1): identification of mutations in RPGR exon ORF15."; Am. J. Hum. Genet. 70:1049-1053(2002).
[20]	VARIANTS RP3 GLY-127; ARG-173; TYR-250; LEU-258 DEL; ARG-267; GLY-285 AND ASP-436. DOI=10.1086/340848; PubMed=11992260 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "A comprehensive mutation analysis of RP2 and RPGR in a North American cohort of families with X-linked retinitis pigmentosa."; Am. J. Hum. Genet. 70:1545-1554(2002).
[21]	VARIANTS RP3 ASN-312; TYR-312 AND ARG-320. DOI=10.1086/379379; PubMed=14564670 [NCBI, ExPASy, EBI, Israel, Japan] Sharon D., Sandberg M.A., Rabe V.W., Stillberger M., Dryja T.P., Berson E.L.; "RP2 and RPGR mutations and clinical correlations in patients with X-linked retinitis pigmentosa."; Am. J. Hum. Genet. 73:1131-1146(2003).
[22]	VARIANTS RP3 LEU-152 AND VAL-215. DOI=10.1167/iovs.02-0605; PubMed=12657579 [NCBI, ExPASy, EBI, Israel, Japan] Bader I., Brandau O., Achatz H., Apfelstedt-Sylla E., Hergersberg M., Lorenz B., Wissinger B., Wittwer B., Rudolph G., Meindl A., Meitinger T.; "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."; Invest. Ophthalmol. Vis. Sci. 44:1458-1463(2003).
[23]	INVOLVEMENT IN RPDSI. DOI=10.1136/jmg.40.8.609; PubMed=12920075 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "RPGR mutation associated with retinitis pigmentosa, impaired hearing, and sinorespiratory infections."; J. Med. Genet. 40:609-615(2003).
[24]	VARIANT RPDSI ARG-173. DOI=10.1136/jmg.40.11.e118; PubMed=14627685 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Clinical and immunohistochemical evidence for an X linked retinitis pigmentosa syndrome with recurrent infections and hearing loss in association with an RPGR mutation."; J. Med. Genet. 40:E118-E118(2003).

Comments

FUNCTION: Could be a guanine-nucleotide releasing factor.
SUBUNIT: Interacts with RPGRIP1.
SUBCELLULAR LOCATION: Golgi apparatus (By similarity).

ALTERNATIVE PRODUCTS: 5 named isoforms [FASTA] produced by alternative splicing. Additional isoforms seem to exist.

Name	1
Isoform ID	Q92834-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	Q92834-2
Features which should be applied to build the isoform sequence: VSP_005548.

Name	3
Isoform ID	Q92834-3
Features which should be applied to build the isoform sequence: VSP_005548, VSP_005549, VSP_005550.

Name	4
Isoform ID	Q92834-4
Features which should be applied to build the isoform sequence: VSP_005547, VSP_005548.

Name	5
Isoform ID	Q92834-5
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_009183, VSP_009184.

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.
PTM: Prenylated (By similarity).
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.
DISEASE: 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.
DISEASE: Defects in RPGR are the cause of X-linked retinitis pigmentosa with deafness and sinorespiratory infections (RPDSI) [MIM:300455]. The phenotype has similarities with primary ciliary dyskinesia and Usher syndrome.
DISEASE: 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.
SIMILARITY: Contains 6 RCC1 repeats.
WEB RESOURCE: Name=Mutations of the RPGR gene; Note=Retina International's Scientific Newsletter; URL="http://www.retina-international.com/sci-news/rpgrmut.htm";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=RPGR";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U57629; AAC50481.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X97668; CAA66258.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ238395; CAB54002.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ318463; CAC86116.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC031624; AAH31624.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF286471; AAG00550.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00023757; -.
IPI00215806; -.
IPI00215807; -.
IPI00215808; -.
IPI00397031; -.

RefSeq

NP_000319.1; -.

UniGene

Hs.61438

3D structure databases

HSSP

P18754; 1I2M. [HSSP ENTRY / PDB]

ModBase

Q92834.

Organism-specific databases

GC0XM038013; -.

HIX0016727; -.

HGNC:10295; RPGR.

HPA001593; -.

300029; phenotype. [NCBI / EBI]
300389; phenotype. [NCBI / EBI]
300455; phenotype. [NCBI / EBI]
304020; phenotype. [NCBI / EBI]
312610; gene. [NCBI / EBI]

Orphanet

49382; Achromatopsia.
1872; Cone rod dystrophy.
244; Primary ciliary dyskinesia.
791; Retinitis pigmentosa.

PharmGKB

PA34656; -.

Gene expression databases

Q92834; -.

Q92834; -.

HS_RPGR; -.

ENSG00000156313; Homo sapiens.

Ontologies

GO:0005794;	Cellular component: Golgi apparatus (inferred from sequence or structural similarity from UniProtKB).
GO:0005739;	Cellular component: mitochondrion (inferred from direct assay from HPA).
GO:0005085;	Molecular function: guanyl-nucleotide exchange factor activity (inferred from electronic annotation from UniProtKB-KW).
GO:0005515;	Molecular function: protein binding (traceable author statement from ProtInc).
GO:0006886;	Biological process: intracellular protein transport (traceable author statement from ProtInc).
GO:0050896;	Biological process: response to stimulus (inferred from electronic annotation from UniProtKB-KW).
GO:0007605;	Biological process: sensory perception of sound (inferred from electronic annotation from UniProtKB-KW).
GO:0007601;	Biological process: visual perception (inferred from mutant phenotype from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR000408; Reg_chr_condens.
IPR009091; Reg_csome_cond/b-lactamase_inh.
Graphical view of domain structure.

Gene3D

G3DSA:2.130.10.30; Reg_csome_cond/b-lactamase_inh; 1.

Pfam

PF00415; RCC1; 4.
Pfam graphical view of domain structure.

PRINTS

PR00633; RCCNDNSATION.

PROSITE

PS00625; RCC1_1; FALSE_NEG.
PS00626; RCC1_2; 4.
PS50012; RCC1_3; 6.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

Q92834; -.

Genome annotation databases

Ensembl

ENSG00000156313; Homo sapiens. [Contig view]

GeneID

6103; -.

KEGG

hsa:6103; -.

Phylogenomic databases

HOVERGEN

Q92834; -.

OMA

Q92834; NNNEPLP.

Other

23741; -.

RPGR; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Cone-rod dystrophy; Deafness; Disease mutation; Golgi apparatus; Guanine-nucleotide releasing factor; Lipoprotein; Methylation; Polymorphism; Prenylation; Repeat; Retinitis pigmentosa; Sensory transduction; Vision.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1017`	`1017`	`X-linked retinitis pigmentosa GTPase regulator.`	`PRO_0000206638`
`PROPEP`	`1018 1020`	`3`	`Removed in mature form (Potential).`	`PRO_0000370844`
`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.`
`COMPBIAS`	`530 903`	`374`	`Glu-rich.`
`MOD_RES`	`1017 1017`		`Cysteine methyl ester (Potential).`
`LIPID`	`1017 1017`		`S-geranylgeranyl cysteine (Potential).`
`VAR_SEQ`	`354 415`		`Missing (in isoform 4).`	`VSP_005547`
`VAR_SEQ`	`473 480`		`YLLDEMTK -> THHEPEFQ (in isoform 5).`	`VSP_009183`
`VAR_SEQ`	`481 1020`		`Missing (in isoform 5).`	`VSP_009184`
`VAR_SEQ`	`585 789`		`Missing (in isoform 2, isoform 3 and isoform 4).`	`VSP_005548`
`VAR_SEQ`	`841 851`		`DHEFSKTEELK -> YSASHSQIVSV (in isoform 3).`	`VSP_005549`
`VAR_SEQ`	`852 1020`		`Missing (in isoform 3).`	`VSP_005550`
`VARIANT`	`43 43`	`1`	`G -> E (in RP3).`	`VAR_018057`
`VARIANT`	`43 43`	`1`	`G -> R (in RP3).`	`VAR_018058`
`VARIANT`	`60 60`	`1`	`G -> V (in RP3).`	`VAR_008501`
`VARIANT`	`75 75`	`1`	`I -> V (in RP3; could be a polymorphism).`	`VAR_008503`
`VARIANT`	`76 76`	`1`	`S -> I (in dbSNP:rs1801685 [NCBI]).`	`VAR_013624`
`VARIANT`	`98 98`	`1`	`H -> Q (in RP3).`	`VAR_008504`
`VARIANT`	`99 99`	`1`	`T -> N (in RP3).`	`VAR_013625`
`VARIANT`	`127 127`	`1`	`R -> G (in RP3).`	`VAR_018059`
`VARIANT`	`130 130`	`1`	`F -> C (in RP3).`	`VAR_006850`
`VARIANT`	`152 152`	`1`	`S -> L (in RP3).`	`VAR_025949`
`VARIANT`	`173 173`	`1`	`G -> R (in RP3 and RPDSI).`	`VAR_018060`
`VARIANT`	`184 184`	`1`	`Q -> H (in dbSNP:rs5963403 [NCBI]).`	`VAR_033259`
`VARIANT`	`215 215`	`1`	`G -> V (in RP3).`	`VAR_008505`
`VARIANT`	`235 235`	`1`	`P -> S (in RP3).`	`VAR_006851`
`VARIANT`	`250 250`	`1`	`C -> R (in RP3).`	`VAR_008506`
`VARIANT`	`250 250`	`1`	`C -> Y (in RP3).`	`VAR_018061`
`VARIANT`	`258 258`	`1`	`Missing (in RP3).`	`VAR_018062`
`VARIANT`	`262 262`	`1`	`A -> G (in RP3; could be a polymorphism).`	`VAR_008507`
`VARIANT`	`267 267`	`1`	`G -> E (in RP3).`	`VAR_018063`
`VARIANT`	`267 267`	`1`	`G -> R (in RP3).`	`VAR_026127`
`VARIANT`	`275 275`	`1`	`G -> S (in RP3).`	`VAR_006852`
`VARIANT`	`285 285`	`1`	`E -> G (in RP3).`	`VAR_026128`
`VARIANT`	`289 289`	`1`	`I -> V (in RP3).`	`VAR_013626`
`VARIANT`	`296 300`	`5`	`Missing (in RP3).`	`VAR_013627`
`VARIANT`	`302 302`	`1`	`C -> R (in RP3).`	`VAR_011561`
`VARIANT`	`302 302`	`1`	`C -> Y (in RP3).`	`VAR_018064`
`VARIANT`	`312 312`	`1`	`D -> N (in RP3).`	`VAR_018065`
`VARIANT`	`312 312`	`1`	`D -> Y (in RP3).`	`VAR_018066`
`VARIANT`	`320 320`	`1`	`G -> R (in RP3).`	`VAR_018067`
`VARIANT`	`345 345`	`1`	`N -> D (rare polymorphism; dbSNP:rs41305223 [NCBI]).`	`VAR_018068`
`VARIANT`	`425 425`	`1`	`R -> K (in dbSNP:rs1801687 [NCBI]).`	`VAR_008508`
`VARIANT`	`431 431`	`1`	`I -> V.`	`VAR_008509`
`VARIANT`	`436 436`	`1`	`G -> D (in RP3).`	`VAR_008510`
`VARIANT`	`526 526`	`1`	`Missing.`	`VAR_011562`
`VARIANT`	`533 533`	`1`	`T -> M (in dbSNP:rs41312104 [NCBI]).`	`VAR_011563`
`VARIANT`	`566 566`	`1`	`G -> E (in dbSNP:rs1801688 [NCBI]).`	`VAR_008511`
`CONFLICT`	`1 3`		`MRE -> MAKLRRSTTTAL (in Ref. 4).`
`CONFLICT`	`190 190`		`K -> N (in Ref. 4; CAC86116).`

Sequence information

Length: 1020 AA [This is the length of the unprocessed precursor]

Molecular weight: 113387 Da [This is the MW of the unprocessed precursor]

CRC64: EAB16275A9A436C3 [This is a checksum on the sequence]

        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

Q92834 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools