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Retinal-specific ATP-binding cassette transporter (ATP-binding cassette sub-family A member 4) (RIM ABC transporter) (RIM protein) (RmP) (Stargardt disease protein)

 ABCA4_HUMAN             Reviewed;        2273 AA.
P78363; O15112; O60438; O60915; Q0QD48; Q4LE31;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 3.
22-NOV-2017, entry version 183.
RecName: Full=Retinal-specific ATP-binding cassette transporter;
AltName: Full=ATP-binding cassette sub-family A member 4;
AltName: Full=RIM ABC transporter;
Short=RIM protein;
Short=RmP;
AltName: Full=Stargardt disease protein;
Name=ABCA4; Synonyms=ABCR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], VARIANTS STGD1, AND VARIANTS HIS-846;
GLN-943 AND ASP-1817.
PubMed=9054934; DOI=10.1038/ng0397-236;
Allikmets R., Singh N., Sun H., Shroyer N.F., Hutchinson A.,
Chidambaram A., Gerrard B., Baird L., Stauffer D., Peiffer A.,
Rattner A., Smallwood P.M., Li Y., Anderson K.L., Lewis R.A.,
Nathans J., Leppert M., Dean M., Lupski J.R.;
"A photoreceptor cell-specific ATP-binding transporter gene (ABCR) is
mutated in recessive Stargardt macular dystrophy.";
Nat. Genet. 15:236-246(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9202155; DOI=10.1016/S0014-5793(97)00517-6;
Azarian S.M., Travis G.H.;
"The photoreceptor rim protein is an ABC transporter encoded by the
gene for recessive Stargardt's disease (ABCR).";
FEBS Lett. 409:247-252(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS STGD1 TRP-18 AND CYS-212,
AND VARIANT ASP-1817.
PubMed=9503029; DOI=10.1006/geno.1997.5164;
Gerber S., Rozet J.-M., van de Pol T.J.R., Hoyng C.B., Munnich A.,
Blankenagel A., Kaplan J., Cremers F.P.M.;
"Complete exon-intron structure of the retina-specific ATP binding
transporter gene (ABCR) allows the identification of novel mutations
underlying Stargardt disease.";
Genomics 48:139-142(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS STGD1.
PubMed=9490294; DOI=10.1007/s004390050649;
Nasonkin I., Illing M., Koehler M.R., Schmid M., Molday R.S.,
Weber B.H.F.;
"Mapping of the rod photoreceptor ABC transporter (ABCR) to 1p21-p22.1
and identification of novel mutations in Stargardt's disease.";
Hum. Genet. 102:21-26(1998).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-943.
TISSUE=Brain;
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M.,
Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
"Preparation of a set of expression-ready clones of mammalian long
cDNAs encoding large proteins by the ORF trap cloning method.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-29.
TISSUE=Retina;
PubMed=17286855; DOI=10.1186/1471-2164-8-42;
Roni V., Carpio R., Wissinger B.;
"Mapping of transcription start sites of human retina expressed
genes.";
BMC Genomics 8:42-42(2007).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10075733; DOI=10.1074/jbc.274.12.8269;
Sun H., Molday R.S., Nathans J.;
"Retinal stimulates ATP hydrolysis by purified and reconstituted ABCR,
the photoreceptor-specific ATP-binding cassette transporter
responsible for Stargardt disease.";
J. Biol. Chem. 274:8269-8281(1999).
[9]
DISEASE.
PubMed=9466990; DOI=10.1093/hmg/7.3.355;
Cremers F.P.M., van de Pol D.J.R., van Driel M.A., den Hollander A.I.,
van Haren F.J.J., Knoers N.V.A.M., Tijmes N., Bergen A.A.B.,
Rohrschneider K., Blankenagel A., Pinckers A.J.L.G., Deutman A.F.,
Hoyng C.B.;
"Autosomal recessive retinitis pigmentosa and cone-rod dystrophy
caused by splice site mutations in the Stargardt's disease gene
ABCR.";
Hum. Mol. Genet. 7:355-362(1998).
[10]
MEMBRANE TOPOLOGY, AND GLYCOSYLATION AT ASN-98; ASN-415; ASN-444;
ASN-504; ASN-1469; ASN-1529; ASN-1588 AND ASN-1662.
PubMed=11320094; DOI=10.1074/jbc.M101902200;
Bungert S., Molday L.L., Molday R.S.;
"Membrane topology of the ATP binding cassette transporter ABCR and
its relationship to ABC1 and related ABCA transporters: identification
of N-linked glycosylation sites.";
J. Biol. Chem. 276:23539-23546(2001).
[11]
VARIANTS ARMD2, AND VARIANTS.
PubMed=9295268; DOI=10.1126/science.277.5333.1805;
Allikmets R., Shroyer N.F., Singh N., Seddon J.M., Lewis R.A.,
Bernstein P.S., Peiffer A., Zabriskie N.A., Li Y., Hutchinson A.,
Dean M., Lupski J.R., Leppert M.;
"Mutation of the Stargardt disease gene (ABCR) in age-related macular
degeneration.";
Science 277:1805-1807(1997).
[12]
VARIANTS STGD1 TRP-18; CYS-212; HIS-636; MET-1019; VAL-1038; CYS-1108;
TRP-1640; SER-1977 AND HIS-2107, AND VARIANTS FFM PRO-11; PRO-541;
VAL-1038; GLU-1091; CYS-1508; PHE-1970 AND ARG-1971.
PubMed=9781034; DOI=10.1038/sj.ejhg.5200221;
Rozet J.-M., Gerber S., Souied E., Perrault I., Chatelin S., Ghazi I.,
Leowski C., Dufier J.-L., Munnich A., Kaplan J.;
"Spectrum of ABCR gene mutations in autosomal recessive macular
dystrophies.";
Eur. J. Hum. Genet. 6:291-295(1998).
[13]
VARIANTS STGD1.
PubMed=9973280; DOI=10.1086/302251;
Lewis R.A., Shroyer N.F., Singh N., Allikmets R., Hutchinson A.,
Li Y., Lupski J.R., Leppert M., Dean M.;
"Genotype/phenotype analysis of a photoreceptor-specific ATP-binding
cassette transporter gene, ABCR, in Stargardt disease.";
Am. J. Hum. Genet. 64:422-434(1999).
[14]
VARIANTS STGD1, AND VARIANTS.
PubMed=10090887; DOI=10.1086/302323;
Maugeri A., van Driel M.A., van de Pol D.J.R., Klevering B.J.,
van Haren F.J.J., Tijmes N., Bergen A.A.B., Rohrschneider K.,
Blankenagel A., Pinckers A.J.L.G., Dahl N., Brunner H.G.,
Deutman A.F., Hoyng C.B., Cremers F.P.M.;
"The 2588G-->C mutation in the ABCR gene is a mild frequent founder
mutation in the western European population and allows the
classification of ABCR Mutations in patients with Stargardt disease.";
Am. J. Hum. Genet. 64:1024-1035(1999).
[15]
VARIANT STGD1 TYR-54, AND VARIANT ALA-863.
PubMed=10612508; DOI=10.1016/S0002-9394(99)00236-6;
Zhang K., Garibaldi D.C., Kniazeva M., Albini T., Chiang M.F.,
Kerrigan M., Sunness J.S., Han M., Allikmets R.;
"A novel mutation in the ABCR gene in four patients with autosomal
recessive Stargardt disease.";
Am. J. Ophthalmol. 128:720-724(1999).
[16]
VARIANTS STGD1 VAL-60; ARG-206; ASN-300; PRO-541; ALA-849; PRO-974;
VAL-1038; CYS-1108; LEU-1408; ARG-1488; ASP-1652; PRO-1729; GLU-1961;
TRP-2038; TRP-2077; HIS-2107; ARG-2128 AND TYR-2150.
PubMed=10206579; DOI=10.1001/archopht.117.4.504;
Fishman G.A., Stone E.M., Grover S., Derlacki D.J., Haines H.L.,
Hockey R.R.;
"Variation of clinical expression in patients with Stargardt dystrophy
and sequence variations in the ABCR gene.";
Arch. Ophthalmol. 117:504-510(1999).
[17]
VARIANTS GLU-1961 AND ASN-2177.
PubMed=10880298; DOI=10.1086/303018;
Allikmets R., Tammur J., Hutchinson A., Lewis R.A., Shroyer N.F.,
Dalakishvili K., Lupski J.R., Steiner K., Pauleikhoff D., Holz F.G.,
Weber B.H.F., Dean M., Atkinson A., Gail M.H., Bernstein P.S.,
Singh N., Peiffer A., Zabriskie N.A., Leppert M., Seddon J.M.,
Zhang K., Sunness J.S., Udar N.S., Yelchits S., Silva-Garcia R.,
Small K.W., Simonelli F., Testa F., D'Urso M., Brancato R.,
Rinaldi E., Ingvast S., Taube A., Wadelius C., Souied E., Ducroq D.,
Kaplan J., Assink J.J.M., ten Brink J.B., de Jong P.T.V.M.,
Bergen A.A.B., Maugeri A., van Driel M.A., Hoyng C.B., Cremers F.P.M.,
Paloma E., Coco R., Balcells S., Gonzalez-Duarte R., Kermani S.,
Stanga P., Bhattacharya S.S., Bird A.C.;
"Further evidence for an association of ABCR alleles with age-related
macular degeneration.";
Am. J. Hum. Genet. 67:487-491(2000).
[18]
VARIANTS STGD1 GLU-60; THR-60; GLU-65; LEU-68; ARG-72; CYS-212;
SER-230; SER-247; VAL-328; LYS-471; PRO-541; GLN-572; ARG-607;
LYS-635; CYS-653; TYR-764; ARG-765; ALA-901; ILE-959; LYS-1036;
VAL-1038; PRO-1063; ASP-1087; CYS-1097; CYS-1108; LEU-1380; LYS-1399;
PRO-1430; VAL-1440; HIS-1443; LEU-1486; TYR-1488; MET-1537; PRO-1689;
LEU-1705; THR-1733; ARG-1748; PRO-1763; LYS-1885; HIS-1898; GLU-1961;
ARG-1975; SER-1977; GLY-2077; TRP-2077 AND VAL-2241, AND VARIANTS
GLN-152; HIS-212; ARG-423; ILE-552; ARG-914; GLN-943; THR-1562;
ILE-1868; MET-1921; LEU-1948; PHE-1970; ALA-2059; ASN-2177 AND
VAL-2216.
PubMed=10958763; DOI=10.1086/303090;
Rivera A., White K., Stoehr H., Steiner K., Hemmrich N., Grimm T.,
Jurklies B., Lorenz B., Scholl H.P.N., Apfelstedt-Sylla E.,
Weber B.H.F.;
"A comprehensive survey of sequence variation in the ABCA4 (ABCR) gene
in Stargardt disease and age-related macular degeneration.";
Am. J. Hum. Genet. 67:800-813(2000).
[19]
VARIANTS CORD3 GLU-65; CYS-212; PRO-541; ALA-863; GLY-863 DEL;
VAL-1038; LYS-1122; TYR-1490 AND ASP-1598.
PubMed=10958761; DOI=10.1086/303079;
Maugeri A., Klevering B.J., Rohrschneider K., Blankenagel A.,
Brunner H.G., Deutman A.F., Hoyng C.B., Cremers F.P.M.;
"Mutations in the ABCA4 (ABCR) gene are the major cause of autosomal
recessive cone-rod dystrophy.";
Am. J. Hum. Genet. 67:960-966(2000).
[20]
VARIANTS STGD1 ASP-340; GLN-572; ALA-863; SER-965; VAL-1038; ALA-1780
AND HIS-1898, AND VARIANT GLN-943.
PubMed=10746567; DOI=10.1007/s004390051034;
Shroyer N.F., Lewis R.A., Lupski J.R.;
"Complex inheritance of ABCR mutations in Stargardt disease: linkage
disequilibrium, complex alleles, and pseudodominance.";
Hum. Genet. 106:244-248(2000).
[21]
VARIANTS STGD1.
PubMed=10634594;
Papaioannou M., Ocaka L., Bessant D., Lois N., Bird A.C., Payne A.,
Bhattacharya S.S.;
"An analysis of ABCR mutations in British patients with recessive
retinal dystrophies.";
Invest. Ophthalmol. Vis. Sci. 41:16-19(2000).
[22]
VARIANTS STGD1 CYS-212; ASP-767; ILE-897; VAL-1038; LYS-1087;
LYS-1399; GLN-1640 AND GLU-1961, AND VARIANT HIS-212.
PubMed=10711710;
Simonelli F., Testa F., de Crecchio G., Rinaldi E., Hutchinson A.,
Atkinson A., Dean M., D'Urso M., Allikmets R.;
"New ABCR mutations and clinical phenotype in Italian patients with
Stargardt disease.";
Invest. Ophthalmol. Vis. Sci. 41:892-897(2000).
[23]
CHARACTERIZATION OF VARIANTS, AND MUTAGENESIS OF GLY-966; LYS-969;
GLY-1975 AND LYS-1978.
PubMed=11017087; DOI=10.1038/79994;
Sun H., Smallwood P.M., Nathans J.;
"Biochemical defects in ABCR protein variants associated with human
retinopathies.";
Nat. Genet. 26:242-246(2000).
[24]
VARIANT STGD1 ASN-972, AND VARIANTS GLN-943; ILE-1868 AND LEU-1948.
PubMed=11594993; DOI=10.1034/j.1600-0420.2001.790520.x;
Eksandh L., Ekstroem U., Abrahamson M., Bauer B., Andreasson S.;
"Different clinical expressions in two families with Stargardt's
macular dystrophy (STGD1).";
Acta Ophthalmol. Scand. 79:524-530(2001).
[25]
VARIANTS RETINAL TOXICITY CYS-1129; ARG-1201 AND HIS-2107, AND
VARIANTS HIS-212; ARG-423; ILE-1868 AND ILE-2255.
PubMed=11384574; DOI=10.1016/S0002-9394(01)00838-8;
Shroyer N.F., Lewis R.A., Lupski J.R.;
"Analysis of the ABCR (ABCA4) gene in 4-aminoquinoline retinopathy: is
retinal toxicity by chloroquine and hydroxychloroquine related to
Stargardt disease?";
Am. J. Ophthalmol. 131:761-766(2001).
[26]
VARIANTS GLU-1961 AND ASN-2177.
PubMed=11346402; DOI=10.1001/archopht.119.5.745;
Guymer R.H., Heon E., Lotery A.J., Munier F.L., Schorderet D.F.,
Baird P.N., McNeil R.J., Haines H.L., Sheffield V.C., Stone E.M.;
"Variation of codons 1961 and 2177 of the Stargardt disease gene is
not associated with age-related macular degeneration.";
Arch. Ophthalmol. 119:745-751(2001).
[27]
VARIANTS FFM GLY-339; ALA-863; TRP-943; ARG-991; VAL-1038; CYS-1108;
ARG-1488; THR-1562; GLN-1640; PHE-2027; GLN-2030 AND CYS-2106, AND
VARIANTS HIS-212; ARG-423; GLN-943; THR-1148; ILE-1868 AND ILE-2255.
PubMed=11379881; DOI=10.1007/s004390100493;
Yatsenko A.N., Shroyer N.F., Lewis R.A., Lupski J.R.;
"Late-onset Stargardt disease is associated with missense mutations
that map outside known functional regions of ABCR (ABCA4).";
Hum. Genet. 108:346-355(2001).
[28]
VARIANTS STGD1 SER-686; TRP-1055; ASP-1799; ASP-1805; PRO-1940 AND
HIS-2107, VARIANTS FFM MET-1253 AND PRO-1940, VARIANTS CORD3 CYS-212
AND ARG-2060, AND VARIANTS GLN-943; LEU-1948 AND ILE-2255.
PubMed=11385708; DOI=10.1002/humu.1133;
Paloma E., Martinez-Mir A., Vilageliu L., Gonzalez-Duarte R.,
Balcells S.;
"Spectrum of ABCA4 (ABCR) gene mutations in Spanish patients with
autosomal recessive macular dystrophies.";
Hum. Mutat. 17:504-510(2001).
[29]
VARIANTS STGD1, AND VARIANTS.
PubMed=11328725;
Webster A.R., Heon E., Lotery A.J., Vandenburgh K., Casavant T.L.,
Oh K.T., Beck G., Fishman G.A., Lam B.L., Levin A., Heckenlively J.R.,
Jacobson S.G., Weleber R.G., Sheffield V.C., Stone E.M.;
"An analysis of allelic variation in the ABCA4 gene.";
Invest. Ophthalmol. Vis. Sci. 42:1179-1189(2001).
[30]
VARIANTS STGD1 13-LYS--TRP-15 DEL; TYR-54; LYS-58; VAL-60; GLU-65;
GLU-77; HIS-190; PRO-244; ARG-309; CYS-525; CYS-537; PRO-541; PRO-549;
ARG-550; GLN-602; ARG-607; MET-643; ASP-767; PRO-797; ARG-821;
THR-824; ALA-863; ALA-935; TRP-943; ALA-989; VAL-1038; CYS-1108;
LEU-1108; LYS-1122; ARG-1201; GLN-1300; LEU-1380; PRO-1388; ARG-1408;
LEU-1486; ARG-1488; TYR-1490; MET-1526; ASN-1532; THR-1562; TRP-1640;
LEU-1776; THR-1846; GLU-1961; SER-1977; PHE-2027; GLN-2030; PRO-2035;
LEU-2050; CYS-2107; HIS-2107; TRP-2139; ARG-2150 AND TYR-2150,
VARIANTS CORD3 GLN-1640 AND ASP-2146, AND VARIANTS HIS-212; ARG-423;
GLN-943; THR-1637; ILE-1868 AND LEU-1948.
PubMed=11527935;
Briggs C.E., Rucinski D., Rosenfeld P.J., Hirose T., Berson E.L.,
Dryja T.P.;
"Mutations in ABCR (ABCA4) in patients with Stargardt macular
degeneration or cone-rod degeneration.";
Invest. Ophthalmol. Vis. Sci. 42:2229-2236(2001).
[31]
VARIANT ARG-423.
PubMed=12111378; DOI=10.1007/s100380200041;
Iida A., Saito S., Sekine A., Mishima C., Kitamura Y., Kondo K.,
Harigae S., Osawa S., Nakamura Y.;
"Catalog of 605 single-nucleotide polymorphisms (SNPs) among 13 genes
encoding human ATP-binding cassette transporters: ABCA4, ABCA7, ABCA8,
ABCD1, ABCD3, ABCD4, ABCE1, ABCF1, ABCG1, ABCG2, ABCG4, ABCG5, and
ABCG8.";
J. Hum. Genet. 47:285-310(2002).
[32]
VARIANT [LARGE SCALE ANALYSIS] MET-224.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[33]
VARIANTS ARMD2 GLU-762; LEU-1129; CYS-1724; SER-1977; ASN-2047 AND
TYR-2137, AND VARIANT ILE-552.
PubMed=19028736; DOI=10.1136/bjo.2008.145193;
Aguirre-Lamban J., Riveiro-Alvarez R., Maia-Lopes S.,
Cantalapiedra D., Vallespin E., Avila-Fernandez A.,
Villaverde-Montero C., Trujillo-Tiebas M.J., Ramos C., Ayuso C.;
"Molecular analysis of the ABCA4 gene for reliable detection of
allelic variations in Spanish patients: identification of 21 novel
variants.";
Br. J. Ophthalmol. 93:614-621(2009).
[34]
VARIANTS STGD1 VAL-156; CYS-212; LYS-380; ARG-550; PRO-572; TRP-602;
ARG-607; CYS-653; ASP-767; ILE-897; ALA-901; MET-931; SER-965;
MET-1019; HIS-1108; LEU-1129; LEU-1380; ILE-1433; LEU-1486; TYR-1490;
GLN-1640; TRP-1640; ARG-1748; ASP-1799; PRO-1940; GLU-1961; SER-1977;
PHE-2027; ARG-2060; HIS-2107; TYR-2150 AND VAL-2241.
PubMed=18977788; DOI=10.1136/bjo.2008.148155;
Riveiro-Alvarez R., Aguirre-Lamban J., Lopez-Martinez M.A.,
Trujillo-Tiebas M.J., Cantalapiedra D., Vallespin E.,
Avila-Fernandez A., Ramos C., Ayuso C.;
"Frequency of ABCA4 mutations in 278 Spanish controls: an insight into
the prevalence of autosomal recessive Stargardt disease.";
Br. J. Ophthalmol. 93:1359-1364(2009).
[35]
VARIANT STGD1 TRP-602.
PubMed=24444108; DOI=10.1186/1471-2350-15-11;
Ortube M.C., Strom S.P., Nelson S.F., Nusinowitz S., Martinez A.,
Gorin M.B.;
"Whole exome sequencing detects homozygosity for ABCA4 p.Arg602Trp
missense mutation in a pediatric patient with rapidly progressive
retinal dystrophy.";
BMC Med. Genet. 15:11-11(2014).
-!- FUNCTION: In the visual cycle, acts as an inward-directed retinoid
flipase, retinoid substrates imported by ABCA4 from the
extracellular or intradiscal (rod) membrane surfaces to the
cytoplasmic membrane surface are all-trans-retinaldehyde (ATR) and
N-retinyl-phosphatidyl-ethanolamine (NR-PE). Once transported to
the cytoplasmic surface, ATR is reduced to vitamin A by trans-
retinol dehydrogenase (tRDH) and then transferred to the retinal
pigment epithelium (RPE) where it is converted to 11-cis-retinal.
May play a role in photoresponse, removing ATR/NR-PE from the
extracellular photoreceptor surfaces during bleach recovery.
{ECO:0000269|PubMed:10075733}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10075733};
Multi-pass membrane protein {ECO:0000269|PubMed:10075733}.
Note=Localized to outer segment disk edges of rods and cones, with
around one million copies/photoreceptor.
-!- TISSUE SPECIFICITY: Retinal-specific. Seems to be exclusively
found in the rims of rod photoreceptor cells.
-!- DISEASE: Stargardt disease 1 (STGD1) [MIM:248200]: A common
hereditary macular degeneration. It is characterized by decreased
central vision, atrophy of the macula and underlying retinal
pigment epithelium, and frequent presence of prominent flecks in
the posterior pole of the retina. {ECO:0000269|PubMed:10090887,
ECO:0000269|PubMed:10206579, ECO:0000269|PubMed:10612508,
ECO:0000269|PubMed:10634594, ECO:0000269|PubMed:10711710,
ECO:0000269|PubMed:10746567, ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:11328725, ECO:0000269|PubMed:11385708,
ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:11594993,
ECO:0000269|PubMed:18977788, ECO:0000269|PubMed:24444108,
ECO:0000269|PubMed:9054934, ECO:0000269|PubMed:9490294,
ECO:0000269|PubMed:9503029, ECO:0000269|PubMed:9781034,
ECO:0000269|PubMed:9973280}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Fundus flavimaculatus (FFM) [MIM:248200]: Autosomal
recessive retinal disorder very similar to Stargardt disease. In
contrast to Stargardt disease, FFM is characterized by later onset
and slowly progressive course. {ECO:0000269|PubMed:11379881,
ECO:0000269|PubMed:11385708, ECO:0000269|PubMed:9781034}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Macular degeneration, age-related, 2 (ARMD2)
[MIM:153800]: A form of age-related macular degeneration, a
multifactorial eye disease and the most common cause of
irreversible vision loss in the developed world. In most patients,
the disease is manifest as ophthalmoscopically visible yellowish
accumulations of protein and lipid that lie beneath the retinal
pigment epithelium and within an elastin-containing structure
known as Bruch membrane. {ECO:0000269|PubMed:19028736,
ECO:0000269|PubMed:9295268}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Cone-rod dystrophy 3 (CORD3) [MIM:604116]: An inherited
retinal dystrophy 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, due to cone photoreceptors degenerating at a
higher rate than rod photoreceptors. {ECO:0000269|PubMed:10958761,
ECO:0000269|PubMed:11385708, ECO:0000269|PubMed:11527935}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Retinitis pigmentosa 19 (RP19) [MIM:601718]: A retinal
dystrophy belonging to the group of pigmentary retinopathies.
Retinitis pigmentosa is characterized by retinal pigment deposits
visible on fundus examination and primary loss of rod
photoreceptor cells followed by secondary loss of cone
photoreceptors. 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. RP19 is characterized by choroidal atrophy.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAE06122.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Mutations of the ABCA4 gene; Note=Retina
International's Scientific Newsletter;
URL="http://www.retina-international.org/files/sci-news/abcrmut.htm";
-!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
proteins;
URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=P78363";
-----------------------------------------------------------------------
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EMBL; U88667; AAC51144.1; -; mRNA.
EMBL; AF000148; AAC23915.1; -; mRNA.
EMBL; Y15635; CAA75729.1; -; Genomic_DNA.
EMBL; Y15636; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15637; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15638; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15639; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15640; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15641; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15642; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15643; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15644; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15645; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15646; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15647; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15648; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15649; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15650; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15651; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15652; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15653; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15654; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15655; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15656; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15657; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15658; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15659; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15660; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15661; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15662; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15663; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15664; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15665; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15666; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15667; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15668; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15669; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15670; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15671; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15672; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15673; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15674; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15675; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15676; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15677; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15678; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15679; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15680; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15681; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15682; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15683; CAA75729.1; JOINED; Genomic_DNA.
EMBL; Y15684; CAA75729.1; JOINED; Genomic_DNA.
EMBL; AF001945; AAC05632.1; -; mRNA.
EMBL; AB210040; BAE06122.1; ALT_INIT; mRNA.
EMBL; AC093579; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC105278; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; DQ426859; ABD90529.1; -; mRNA.
CCDS; CCDS747.1; -.
RefSeq; NP_000341.2; NM_000350.2.
UniGene; Hs.416707; -.
ProteinModelPortal; P78363; -.
SMR; P78363; -.
BioGrid; 106542; 1.
ELM; P78363; -.
STRING; 9606.ENSP00000359245; -.
SwissLipids; SLP:000000347; -.
TCDB; 3.A.1.211.2; the atp-binding cassette (abc) superfamily.
iPTMnet; P78363; -.
PhosphoSitePlus; P78363; -.
BioMuta; ABCA4; -.
DMDM; 6707663; -.
EPD; P78363; -.
PaxDb; P78363; -.
PeptideAtlas; P78363; -.
PRIDE; P78363; -.
DNASU; 24; -.
Ensembl; ENST00000370225; ENSP00000359245; ENSG00000198691.
GeneID; 24; -.
KEGG; hsa:24; -.
UCSC; uc001dqh.4; human.
CTD; 24; -.
DisGeNET; 24; -.
EuPathDB; HostDB:ENSG00000198691.11; -.
GeneCards; ABCA4; -.
GeneReviews; ABCA4; -.
H-InvDB; HIX0028510; -.
HGNC; HGNC:34; ABCA4.
MalaCards; ABCA4; -.
MIM; 153800; phenotype.
MIM; 248200; phenotype.
MIM; 601691; gene.
MIM; 601718; phenotype.
MIM; 604116; phenotype.
neXtProt; NX_P78363; -.
OpenTargets; ENSG00000198691; -.
Orphanet; 279; Age-related macular degeneration.
Orphanet; 1872; Cone rod dystrophy.
Orphanet; 791; Retinitis pigmentosa.
Orphanet; 827; Stargardt disease.
PharmGKB; PA24379; -.
eggNOG; KOG0059; Eukaryota.
eggNOG; COG1131; LUCA.
GeneTree; ENSGT00760000118965; -.
HOGENOM; HOG000231547; -.
HOVERGEN; HBG050436; -.
InParanoid; P78363; -.
KO; K05644; -.
OMA; WAVIPMM; -.
OrthoDB; EOG091G007E; -.
PhylomeDB; P78363; -.
TreeFam; TF105191; -.
Reactome; R-HSA-2453864; Retinoid cycle disease events.
Reactome; R-HSA-2453902; The canonical retinoid cycle in rods (twilight vision).
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
ChiTaRS; ABCA4; human.
GeneWiki; ABCA4; -.
GenomeRNAi; 24; -.
PRO; PR:P78363; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000198691; -.
CleanEx; HS_ABCA4; -.
ExpressionAtlas; P78363; baseline and differential.
Genevisible; P78363; HS.
GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome.
GO; GO:0005524; F:ATP binding; TAS:ProtInc.
GO; GO:0016887; F:ATPase activity; IDA:BHF-UCL.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; TAS:ProtInc.
GO; GO:0005395; F:eye pigment precursor transporter activity; TAS:Reactome.
GO; GO:0090555; F:phosphatidylethanolamine-translocating ATPase activity; IDA:BHF-UCL.
GO; GO:0005215; F:transporter activity; TAS:ProtInc.
GO; GO:0006649; P:phospholipid transfer to membrane; IEA:Ensembl.
GO; GO:0045332; P:phospholipid translocation; IDA:BHF-UCL.
GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
GO; GO:0007603; P:phototransduction, visible light; TAS:ProtInc.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0006810; P:transport; TAS:ProtInc.
GO; GO:0007601; P:visual perception; TAS:ProtInc.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR026082; ABC_A.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR005951; ABCA4/ABCR.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR19229; PTHR19229; 1.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
TIGRFAMs; TIGR01257; rim_protein; 1.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
Age-related macular degeneration; ATP-binding; Complete proteome;
Cone-rod dystrophy; Disease mutation; Disulfide bond; Glycoprotein;
Membrane; Nucleotide-binding; Polymorphism; Reference proteome;
Repeat; Retinitis pigmentosa; Sensory transduction; Stargardt disease;
Transmembrane; Transmembrane helix; Transport; Vision.
CHAIN 1 2273 Retinal-specific ATP-binding cassette
transporter.
/FTId=PRO_0000093301.
TOPO_DOM 1 21 Cytoplasmic.
TRANSMEM 22 42 Helical. {ECO:0000255}.
TOPO_DOM 43 646 Extracellular.
TRANSMEM 647 667 Helical. {ECO:0000255}.
TRANSMEM 700 720 Helical. {ECO:0000255}.
TRANSMEM 731 751 Helical. {ECO:0000255}.
TRANSMEM 760 780 Helical. {ECO:0000255}.
TRANSMEM 836 856 Helical. {ECO:0000255}.
TOPO_DOM 857 1376 Cytoplasmic.
TRANSMEM 1377 1397 Helical. {ECO:0000255}.
TOPO_DOM 1398 1727 Extracellular.
TRANSMEM 1728 1748 Helical. {ECO:0000255}.
TRANSMEM 1760 1780 Helical. {ECO:0000255}.
TRANSMEM 1793 1813 Helical. {ECO:0000255}.
TRANSMEM 1832 1852 Helical. {ECO:0000255}.
TRANSMEM 1874 1894 Helical. {ECO:0000255}.
TOPO_DOM 1895 2273 Cytoplasmic.
DOMAIN 929 1160 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 1938 2170 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 963 970 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1972 1979 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11320094}.
CARBOHYD 415 415 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11320094}.
CARBOHYD 444 444 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11320094}.
CARBOHYD 504 504 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11320094}.
CARBOHYD 1469 1469 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11320094}.
CARBOHYD 1529 1529 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11320094}.
CARBOHYD 1588 1588 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11320094}.
CARBOHYD 1662 1662 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11320094}.
DISULFID 75 324 {ECO:0000250}.
DISULFID 1488 1502 {ECO:0000250}.
VARIANT 11 11 L -> P (in FFM; dbSNP:rs62645946).
{ECO:0000269|PubMed:9781034}.
/FTId=VAR_012493.
VARIANT 13 15 Missing (in STGD1).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012494.
VARIANT 18 18 R -> W (in STGD1; dbSNP:rs121909205).
{ECO:0000269|PubMed:9503029,
ECO:0000269|PubMed:9781034}.
/FTId=VAR_008398.
VARIANT 24 24 R -> H (in STGD1; dbSNP:rs62645958).
/FTId=VAR_008399.
VARIANT 54 54 C -> Y (in STGD1; dbSNP:rs150774447).
{ECO:0000269|PubMed:10612508,
ECO:0000269|PubMed:11527935}.
/FTId=VAR_008400.
VARIANT 58 58 N -> K (in STGD1; dbSNP:rs61748524).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012495.
VARIANT 60 60 A -> E (in STGD1).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012496.
VARIANT 60 60 A -> T (in STGD1; dbSNP:rs61751411).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012497.
VARIANT 60 60 A -> V (in STGD1; dbSNP:rs55732384).
{ECO:0000269|PubMed:10206579,
ECO:0000269|PubMed:11527935}.
/FTId=VAR_008492.
VARIANT 65 65 G -> E (in STGD1 and CORD3;
dbSNP:rs62654395).
{ECO:0000269|PubMed:10958761,
ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:11527935}.
/FTId=VAR_008401.
VARIANT 68 68 P -> L (in STGD1; dbSNP:rs62654397).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012498.
VARIANT 68 68 P -> R (in STGD1; dbSNP:rs62654397).
/FTId=VAR_012499.
VARIANT 72 72 G -> R (in STGD1; dbSNP:rs61751412).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012500.
VARIANT 75 75 C -> G (in STGD1; dbSNP:rs61748526).
/FTId=VAR_008402.
VARIANT 77 77 V -> E (in STGD1; dbSNP:rs61748527).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012501.
VARIANT 96 96 N -> D (in STGD1; dbSNP:rs61748529).
/FTId=VAR_008403.
VARIANT 96 96 N -> H (in STGD1; dbSNP:rs61748529).
/FTId=VAR_008404.
VARIANT 100 100 S -> P (in STGD1; dbSNP:rs61748530).
/FTId=VAR_012502.
VARIANT 152 152 R -> Q (in dbSNP:rs62646862).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012503.
VARIANT 156 156 I -> V (in STGD1; dbSNP:rs62646863).
{ECO:0000269|PubMed:18977788}.
/FTId=VAR_012504.
VARIANT 190 190 Q -> H (in STGD1; dbSNP:rs281865397).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012505.
VARIANT 192 192 A -> T (in STGD1; dbSNP:rs61748535).
/FTId=VAR_008405.
VARIANT 206 206 S -> R (in STGD1; reduced basal and
retinal-stimulated ATP-hydrolysis;
dbSNP:rs61748536).
{ECO:0000269|PubMed:10206579}.
/FTId=VAR_012506.
VARIANT 212 212 R -> C (in STGD1 and CORD3; common
mutation in southern Europe; reduced ATP-
binding capacity; dbSNP:rs61750200).
{ECO:0000269|PubMed:10711710,
ECO:0000269|PubMed:10958761,
ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:11385708,
ECO:0000269|PubMed:18977788,
ECO:0000269|PubMed:9503029,
ECO:0000269|PubMed:9781034}.
/FTId=VAR_008406.
VARIANT 212 212 R -> H (in dbSNP:rs6657239).
{ECO:0000269|PubMed:10711710,
ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:11379881,
ECO:0000269|PubMed:11384574,
ECO:0000269|PubMed:11527935}.
/FTId=VAR_012507.
VARIANT 220 220 R -> C (in STGD1; dbSNP:rs61748538).
/FTId=VAR_012508.
VARIANT 224 224 T -> M (in a breast cancer sample;
somatic mutation; dbSNP:rs373540612).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035736.
VARIANT 230 230 C -> S (in STGD1).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012509.
VARIANT 244 244 L -> P (in STGD1; dbSNP:rs62646864).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012510.
VARIANT 247 247 N -> S (in STGD1; dbSNP:rs62645950).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012511.
VARIANT 249 249 D -> G (in STGD1; dbSNP:rs62646865).
/FTId=VAR_008407.
VARIANT 300 300 T -> N (in STGD1; dbSNP:rs61748544).
{ECO:0000269|PubMed:10206579}.
/FTId=VAR_008408.
VARIANT 309 309 P -> R (in STGD1; dbSNP:rs61748545).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012512.
VARIANT 328 328 E -> V (in STGD1; dbSNP:rs61751419).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012513.
VARIANT 333 333 R -> W (in STGD1; dbSNP:rs61748546).
/FTId=VAR_012514.
VARIANT 336 336 S -> C (in STGD1; dbSNP:rs61748547).
/FTId=VAR_008409.
VARIANT 339 339 W -> G (in FFM; dbSNP:rs61751420).
{ECO:0000269|PubMed:11379881}.
/FTId=VAR_012515.
VARIANT 340 340 Y -> D (in STGD1; dbSNP:rs61748548).
{ECO:0000269|PubMed:10746567}.
/FTId=VAR_008410.
VARIANT 380 380 N -> K (in STGD1; dbSNP:rs61748549).
{ECO:0000269|PubMed:18977788}.
/FTId=VAR_012516.
VARIANT 407 407 A -> V (in STGD1 and CORD3;
dbSNP:rs61751264).
/FTId=VAR_008411.
VARIANT 423 423 H -> R (in dbSNP:rs3112831).
{ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:11379881,
ECO:0000269|PubMed:11384574,
ECO:0000269|PubMed:11527935,
ECO:0000269|PubMed:12111378}.
/FTId=VAR_012517.
VARIANT 445 445 S -> R (in STGD1; dbSNP:rs61748552).
/FTId=VAR_008412.
VARIANT 471 471 E -> K (in ARMD2 and STGD1; ATP-binding
capacity and retinal stimulation as in
wild-type; dbSNP:rs1800548).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_008413.
VARIANT 523 523 D -> E (in STGD1; dbSNP:rs62646868).
/FTId=VAR_008414.
VARIANT 525 525 F -> C (in STGD1).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012518.
VARIANT 537 537 R -> C (in STGD1; dbSNP:rs61748556).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012519.
VARIANT 541 541 L -> P (in STGD1, FFM and CORD3; reduced
ATP-binding capacity; abolishes retinal-
stimulated ATP hydrolysis;
dbSNP:rs61751392).
{ECO:0000269|PubMed:10206579,
ECO:0000269|PubMed:10958761,
ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:11527935,
ECO:0000269|PubMed:9781034}.
/FTId=VAR_008415.
VARIANT 549 549 A -> P (in STGD1; dbSNP:rs61748557).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012520.
VARIANT 550 550 G -> R (in STGD1; dbSNP:rs61748558).
{ECO:0000269|PubMed:11527935,
ECO:0000269|PubMed:18977788}.
/FTId=VAR_012521.
VARIANT 552 552 V -> I (in dbSNP:rs145525174).
{ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:19028736}.
/FTId=VAR_012522.
VARIANT 572 572 R -> P (in STGD1; dbSNP:rs61748559).
{ECO:0000269|PubMed:18977788}.
/FTId=VAR_008416.
VARIANT 572 572 R -> Q (in STGD1; dbSNP:rs61748559).
{ECO:0000269|PubMed:10746567,
ECO:0000269|PubMed:10958763}.
/FTId=VAR_008417.
VARIANT 602 602 R -> Q (in STGD1; dbSNP:rs61749410).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012523.
VARIANT 602 602 R -> W (in STGD1; dbSNP:rs61749409).
{ECO:0000269|PubMed:18977788,
ECO:0000269|PubMed:24444108}.
/FTId=VAR_008418.
VARIANT 607 607 G -> R (in STGD1; dbSNP:rs61749412).
{ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:11527935,
ECO:0000269|PubMed:18977788}.
/FTId=VAR_012524.
VARIANT 607 607 G -> W (in STGD1; dbSNP:rs61749412).
/FTId=VAR_012525.
VARIANT 608 608 F -> I (in STGD1; dbSNP:rs61752398).
/FTId=VAR_008419.
VARIANT 635 635 Q -> K (in STGD1; dbSNP:rs61749414).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012526.
VARIANT 636 636 Q -> H (in STGD1; dbSNP:rs61752400).
{ECO:0000269|PubMed:9781034}.
/FTId=VAR_012527.
VARIANT 643 643 V -> G (in dbSNP:rs61754024).
/FTId=VAR_008420.
VARIANT 643 643 V -> M (in STGD1; dbSNP:rs61749417).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012528.
VARIANT 645 645 D -> N (in STGD1; dbSNP:rs61749418).
/FTId=VAR_008421.
VARIANT 653 653 R -> C (in STGD1; dbSNP:rs61749420).
{ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:18977788}.
/FTId=VAR_012529.
VARIANT 686 686 L -> S (in STGD1; dbSNP:rs61752402).
{ECO:0000269|PubMed:11385708}.
/FTId=VAR_012530.
VARIANT 716 716 T -> M (in STGD1; dbSNP:rs61749426).
/FTId=VAR_012531.
VARIANT 752 752 S -> I (in dbSNP:rs1801369).
/FTId=VAR_014703.
VARIANT 762 762 A -> E (in ARMD2).
{ECO:0000269|PubMed:19028736}.
/FTId=VAR_067427.
VARIANT 764 764 C -> Y (in STGD1; dbSNP:rs61749428).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012532.
VARIANT 765 765 S -> N (in STGD1; dbSNP:rs61749429).
/FTId=VAR_012534.
VARIANT 765 765 S -> R (in STGD1; dbSNP:rs61752404).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012533.
VARIANT 767 767 V -> D (in STGD1; dbSNP:rs61751395).
{ECO:0000269|PubMed:10711710,
ECO:0000269|PubMed:11527935,
ECO:0000269|PubMed:18977788}.
/FTId=VAR_012535.
VARIANT 797 797 L -> P (in STGD1; dbSNP:rs61749432).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012536.
VARIANT 818 818 G -> E (in ARMD2 and STGD1; reduced ATP-
binding capacity; dbSNP:rs61750202).
/FTId=VAR_008422.
VARIANT 821 821 W -> R (in STGD1; dbSNP:rs61749433).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_008423.
VARIANT 824 824 I -> T (in STGD1).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012537.
VARIANT 846 846 D -> H (in dbSNP:rs61754027).
{ECO:0000269|PubMed:9054934}.
/FTId=VAR_008493.
VARIANT 849 849 V -> A (in STGD1; dbSNP:rs61749435).
{ECO:0000269|PubMed:10206579}.
/FTId=VAR_012538.
VARIANT 851 851 G -> D (in STGD1; highly reduced ATP-
binding capacity; dbSNP:rs61749436).
/FTId=VAR_008424.
VARIANT 854 854 A -> T (in STGD1; dbSNP:rs61749437).
/FTId=VAR_012539.
VARIANT 863 863 G -> A (in STGD1, FFM and CORD3; mild
alteration probably leading to disease
phenotype only in combination with a more
severe allele; frequent mutation in
northern Europe in linkage disequilibrium
with the polymorphic variant Q-943;
reduced ATP-binding capacity and retinal-
stimulated ATP hydrolysis;
dbSNP:rs76157638).
{ECO:0000269|PubMed:10612508,
ECO:0000269|PubMed:10746567,
ECO:0000269|PubMed:10958761,
ECO:0000269|PubMed:11379881,
ECO:0000269|PubMed:11527935}.
/FTId=VAR_008425.
VARIANT 863 863 Missing (in STGD1 and CORD3; reduced ATP-
binding capacity and retinal-stimulated
ATP hydrolysis).
{ECO:0000269|PubMed:10958761}.
/FTId=VAR_012540.
VARIANT 873 873 F -> L (in STGD1; dbSNP:rs62642570).
/FTId=VAR_012541.
VARIANT 897 897 T -> I (in STGD1; dbSNP:rs61749440).
{ECO:0000269|PubMed:10711710,
ECO:0000269|PubMed:18977788}.
/FTId=VAR_012542.
VARIANT 901 901 T -> A (in dbSNP:rs61754030).
{ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:18977788}.
/FTId=VAR_008426.
VARIANT 914 914 H -> R. {ECO:0000269|PubMed:10958763}.
/FTId=VAR_012543.
VARIANT 931 931 V -> M (in STGD1; dbSNP:rs58331765).
{ECO:0000269|PubMed:18977788}.
/FTId=VAR_008427.
VARIANT 935 935 V -> A (in STGD1; dbSNP:rs61749444).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012544.
VARIANT 943 943 R -> Q (in linkage disequilibrium with A-
863 in the European population;
dbSNP:rs1801581).
{ECO:0000269|PubMed:10746567,
ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:11379881,
ECO:0000269|PubMed:11385708,
ECO:0000269|PubMed:11527935,
ECO:0000269|PubMed:11594993,
ECO:0000269|PubMed:9054934,
ECO:0000269|Ref.5}.
/FTId=VAR_008428.
VARIANT 943 943 R -> W (in STGD1 and FFM;
dbSNP:rs61749446).
{ECO:0000269|PubMed:11379881,
ECO:0000269|PubMed:11527935}.
/FTId=VAR_012545.
VARIANT 957 957 Q -> R (in STGD1; dbSNP:rs61749448).
/FTId=VAR_008429.
VARIANT 959 959 T -> I (in STGD1; dbSNP:rs61752409).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012546.
VARIANT 965 965 N -> S (in STGD1; reduced retinal-
stimulated ATP hydrolysis;
dbSNP:rs201471607).
{ECO:0000269|PubMed:10746567,
ECO:0000269|PubMed:18977788}.
/FTId=VAR_008430.
VARIANT 971 971 T -> N (in STGD1; highly reduced ATP-
binding capacity; abolishes retinal-
stimulated ATP hydrolysis;
dbSNP:rs61749450).
/FTId=VAR_012547.
VARIANT 972 972 T -> N (in STGD1; unknown pathological
significance; dbSNP:rs61749451).
{ECO:0000269|PubMed:11594993}.
/FTId=VAR_012548.
VARIANT 974 974 S -> P (in STGD1; dbSNP:rs281865400).
{ECO:0000269|PubMed:10206579}.
/FTId=VAR_012549.
VARIANT 978 978 G -> C (in STGD1; dbSNP:rs61749452).
/FTId=VAR_008431.
VARIANT 989 989 V -> A (in STGD1; dbSNP:rs61749454).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012550.
VARIANT 991 991 G -> R (in FFM; dbSNP:rs61749455).
{ECO:0000269|PubMed:11379881}.
/FTId=VAR_012551.
VARIANT 1014 1014 L -> R (in STGD1; dbSNP:rs61749456).
/FTId=VAR_012552.
VARIANT 1019 1019 T -> A (in STGD1; dbSNP:rs61749457).
/FTId=VAR_012553.
VARIANT 1019 1019 T -> M (in STGD1; dbSNP:rs201855602).
{ECO:0000269|PubMed:18977788,
ECO:0000269|PubMed:9781034}.
/FTId=VAR_012554.
VARIANT 1022 1022 E -> K (in STGD1; dbSNP:rs61749459).
/FTId=VAR_012555.
VARIANT 1031 1031 K -> E (in STGD1; dbSNP:rs61750060).
/FTId=VAR_012556.
VARIANT 1036 1036 E -> K (in STGD1; dbSNP:rs61750061).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_008432.
VARIANT 1038 1038 A -> V (in STGD1, FFM and CORD3; frequent
mutation; reduced ATP-binding and
retinal-stimulated ATP hydrolysis;
dbSNP:rs61751374).
{ECO:0000269|PubMed:10206579,
ECO:0000269|PubMed:10711710,
ECO:0000269|PubMed:10746567,
ECO:0000269|PubMed:10958761,
ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:11379881,
ECO:0000269|PubMed:11527935,
ECO:0000269|PubMed:9781034}.
/FTId=VAR_008433.
VARIANT 1055 1055 R -> W (in STGD1; dbSNP:rs61752412).
{ECO:0000269|PubMed:11385708}.
/FTId=VAR_012557.
VARIANT 1063 1063 S -> P (in STGD1; dbSNP:rs61752413).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012558.
VARIANT 1071 1071 S -> L (in STGD1; reduced ATP-binding
capacity; dbSNP:rs61750065).
/FTId=VAR_008434.
VARIANT 1072 1072 V -> A (in STGD1).
/FTId=VAR_008435.
VARIANT 1087 1087 E -> D (in STGD1; dbSNP:rs61752416).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012559.
VARIANT 1087 1087 E -> K (in STGD1; dbSNP:rs61751398).
{ECO:0000269|PubMed:10711710}.
/FTId=VAR_008436.
VARIANT 1091 1091 G -> E (in FFM; dbSNP:rs61752417).
{ECO:0000269|PubMed:9781034}.
/FTId=VAR_012560.
VARIANT 1097 1097 R -> C (in STGD1).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012561.
VARIANT 1108 1108 R -> C (in STGD1 and FFM; reduced ATP-
binding capacity; dbSNP:rs61750120).
{ECO:0000269|PubMed:10206579,
ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:11379881,
ECO:0000269|PubMed:11527935,
ECO:0000269|PubMed:9781034}.
/FTId=VAR_012562.
VARIANT 1108 1108 R -> H (in STGD1; dbSNP:rs61750121).
{ECO:0000269|PubMed:18977788}.
/FTId=VAR_012563.
VARIANT 1108 1108 R -> L (in STGD1; dbSNP:rs61750121).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012564.
VARIANT 1112 1112 T -> N (in STGD1; dbSNP:rs61750122).
/FTId=VAR_008437.
VARIANT 1122 1122 E -> K (in STGD1 and CORD3;
dbSNP:rs61751399).
{ECO:0000269|PubMed:10958761,
ECO:0000269|PubMed:11527935}.
/FTId=VAR_008438.
VARIANT 1129 1129 R -> C (in STGD1; may predispose to
develop retinal toxicity after treatment
with chloroquine and hydroxychloroquine;
dbSNP:rs779426136).
{ECO:0000269|PubMed:11384574}.
/FTId=VAR_012565.
VARIANT 1129 1129 R -> L (in ARMD2 and STGD1; also found in
patients with fundus flavimaculatus;
reduced ATP-binding capacity;
dbSNP:rs1801269).
{ECO:0000269|PubMed:18977788,
ECO:0000269|PubMed:19028736}.
/FTId=VAR_008439.
VARIANT 1148 1148 K -> T. {ECO:0000269|PubMed:11379881}.
/FTId=VAR_012566.
VARIANT 1201 1201 L -> R (in STGD1; may predispose to
develop retinal toxicity after treatment
with chloroquine and hydroxychloroquine;
dbSNP:rs61750126).
{ECO:0000269|PubMed:11384574,
ECO:0000269|PubMed:11527935}.
/FTId=VAR_008440.
VARIANT 1204 1204 D -> N (in STGD1; dbSNP:rs61750127).
/FTId=VAR_008441.
VARIANT 1250 1250 L -> P (in STGD1; dbSNP:rs61750128).
/FTId=VAR_012567.
VARIANT 1253 1253 T -> M (in FFM; unknown pathological
significance; dbSNP:rs61752424).
{ECO:0000269|PubMed:11385708}.
/FTId=VAR_012568.
VARIANT 1300 1300 R -> Q (in STGD1; dbSNP:rs61750129).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012569.
VARIANT 1314 1314 P -> T (in dbSNP:rs61754041).
/FTId=VAR_008442.
VARIANT 1380 1380 P -> L (in STGD1; reduced ATP-binding
capacity; dbSNP:rs61750130).
{ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:11527935,
ECO:0000269|PubMed:18977788}.
/FTId=VAR_008443.
VARIANT 1388 1388 L -> P (in STGD1; dbSNP:rs61750131).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012570.
VARIANT 1399 1399 E -> K (in STGD1; dbSNP:rs62642573).
{ECO:0000269|PubMed:10711710,
ECO:0000269|PubMed:10958763}.
/FTId=VAR_012571.
VARIANT 1406 1406 H -> Y (in STGD1; dbSNP:rs61750133).
/FTId=VAR_008444.
VARIANT 1408 1408 W -> L (in STGD1; dbSNP:rs61750134).
{ECO:0000269|PubMed:10206579}.
/FTId=VAR_008445.
VARIANT 1408 1408 W -> R (in STGD1; reduced retinal-
stimulated ATP hydrolysis;
dbSNP:rs61750135).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_008446.
VARIANT 1428 1428 T -> M (in ARMD2; dbSNP:rs1800549).
/FTId=VAR_008447.
VARIANT 1429 1429 V -> A (in STGD1; dbSNP:rs61752432).
/FTId=VAR_008448.
VARIANT 1430 1430 L -> P (in STGD1).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012572.
VARIANT 1433 1433 V -> I (in STGD1; dbSNP:rs56357060).
{ECO:0000269|PubMed:18977788}.
/FTId=VAR_008449.
VARIANT 1439 1439 G -> D (in STGD1; dbSNP:rs61750140).
/FTId=VAR_008450.
VARIANT 1440 1440 F -> S (in STGD1; dbSNP:rs61750141).
/FTId=VAR_008451.
VARIANT 1440 1440 F -> V (in STGD1; dbSNP:rs61752433).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012573.
VARIANT 1443 1443 R -> H (in STGD1; dbSNP:rs61750142).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012574.
VARIANT 1486 1486 P -> L (in STGD1; dbSNP:rs61750145).
{ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:11527935,
ECO:0000269|PubMed:18977788}.
/FTId=VAR_008452.
VARIANT 1488 1488 C -> F (in STGD1; dbSNP:rs61750147).
/FTId=VAR_012575.
VARIANT 1488 1488 C -> R (in STGD1 and FFM; reduced
retinal-stimulated ATP hydrolysis;
dbSNP:rs61750146).
{ECO:0000269|PubMed:10206579,
ECO:0000269|PubMed:11379881,
ECO:0000269|PubMed:11527935}.
/FTId=VAR_008453.
VARIANT 1488 1488 C -> Y (in STGD1; dbSNP:rs61750147).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012576.
VARIANT 1490 1490 C -> Y (in STGD1 and CORD3; reduced
retinal-stimulated ATP hydrolysis;
dbSNP:rs61751402).
{ECO:0000269|PubMed:10958761,
ECO:0000269|PubMed:11527935,
ECO:0000269|PubMed:18977788}.
/FTId=VAR_008454.
VARIANT 1508 1508 G -> C (in FFM).
{ECO:0000269|PubMed:9781034}.
/FTId=VAR_012577.
VARIANT 1513 1513 Q -> R (in STGD1; dbSNP:rs281865402).
/FTId=VAR_012578.
VARIANT 1517 1517 R -> S (in ARMD2; dbSNP:rs1800550).
/FTId=VAR_008455.
VARIANT 1525 1525 L -> P (in STGD1; dbSNP:rs61750151).
/FTId=VAR_012579.
VARIANT 1526 1526 T -> M (in STGD1; reduced retinal-
stimulated ATP hydrolysis;
dbSNP:rs61750152).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_008456.
VARIANT 1532 1532 D -> N (in STGD1; dbSNP:rs62642574).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_008457.
VARIANT 1537 1537 T -> M (in STGD1; dbSNP:rs62642575).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012580.
VARIANT 1562 1562 I -> T (in STGD1, FFM, ARMD2 and CORD3;
dbSNP:rs1762111).
{ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:11379881,
ECO:0000269|PubMed:11527935}.
/FTId=VAR_008458.
VARIANT 1578 1578 G -> R (in ARMD2; dbSNP:rs1800551).
/FTId=VAR_008459.
VARIANT 1598 1598 A -> D (in CORD3; dbSNP:rs61750155).
{ECO:0000269|PubMed:10958761}.
/FTId=VAR_012581.
VARIANT 1631 1631 L -> P (in STGD1; dbSNP:rs61750158).
/FTId=VAR_008460.
VARIANT 1637 1637 A -> T (rare polymorphism;
dbSNP:rs61754056).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012582.
VARIANT 1640 1640 R -> Q (in STGD1, FFM and CORD3;
dbSNP:rs61751403).
{ECO:0000269|PubMed:10711710,
ECO:0000269|PubMed:11379881,
ECO:0000269|PubMed:11527935,
ECO:0000269|PubMed:18977788}.
/FTId=VAR_012583.
VARIANT 1640 1640 R -> W (in STGD1 and CORD3;
dbSNP:rs61751404).
{ECO:0000269|PubMed:11527935,
ECO:0000269|PubMed:18977788,
ECO:0000269|PubMed:9781034}.
/FTId=VAR_008461.
VARIANT 1652 1652 Y -> D (in STGD1; dbSNP:rs61750560).
{ECO:0000269|PubMed:10206579}.
/FTId=VAR_008462.
VARIANT 1681 1685 Missing (in STGD1; highly reduced ATP-
binding capacity).
/FTId=VAR_012584.
VARIANT 1689 1689 S -> P (in STGD1; dbSNP:rs61753020).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012585.
VARIANT 1693 1693 V -> I (in STGD1; dbSNP:rs61750563).
/FTId=VAR_012586.
VARIANT 1696 1696 S -> N (in STGD1; dbSNP:rs61750564).
/FTId=VAR_008463.
VARIANT 1703 1703 Q -> K (in STGD1).
/FTId=VAR_008464.
VARIANT 1705 1705 R -> L (in STGD1; dbSNP:rs61753021).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012587.
VARIANT 1724 1724 W -> C (in ARMD2).
{ECO:0000269|PubMed:19028736}.
/FTId=VAR_067428.
VARIANT 1729 1729 L -> P (in STGD1; dbSNP:rs61750567).
{ECO:0000269|PubMed:10206579}.
/FTId=VAR_008465.
VARIANT 1733 1733 M -> T (in STGD1; dbSNP:rs765563320).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012588.
VARIANT 1736 1736 S -> P (in STGD1; dbSNP:rs61750568).
/FTId=VAR_012589.
VARIANT 1748 1748 G -> R (in STGD1; dbSNP:rs61753025).
{ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:18977788}.
/FTId=VAR_012590.
VARIANT 1761 1763 Missing (in STGD1; highly reduced ATP-
binding capacity).
/FTId=VAR_012591.
VARIANT 1763 1763 L -> P (in STGD1; dbSNP:rs61753028).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012592.
VARIANT 1776 1776 P -> L (in STGD1; dbSNP:rs281865404).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012593.
VARIANT 1780 1780 P -> A (in STGD1; dbSNP:rs121909207).
{ECO:0000269|PubMed:10746567}.
/FTId=VAR_012594.
VARIANT 1794 1794 A -> D (in STGD1; dbSNP:rs61751406).
/FTId=VAR_008466.
VARIANT 1799 1799 N -> D (in STGD1; dbSNP:rs61750574).
{ECO:0000269|PubMed:11385708,
ECO:0000269|PubMed:18977788}.
/FTId=VAR_012595.
VARIANT 1805 1805 N -> D (in STGD1; dbSNP:rs61753029).
{ECO:0000269|PubMed:11385708}.
/FTId=VAR_012596.
VARIANT 1817 1817 E -> D (in dbSNP:rs1129480).
{ECO:0000269|PubMed:9054934,
ECO:0000269|PubMed:9503029}.
/FTId=VAR_012597.
VARIANT 1820 1820 R -> P (in STGD1; dbSNP:rs62646875).
/FTId=VAR_008467.
VARIANT 1838 1838 H -> Y (in STGD1; dbSNP:rs62642562).
/FTId=VAR_008468.
VARIANT 1843 1843 R -> W (in STGD1; dbSNP:rs62642576).
/FTId=VAR_008469.
VARIANT 1846 1846 I -> T (in dbSNP:rs61750575).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_008494.
VARIANT 1868 1868 N -> I (slightly reduced retinal-
stimulated ATP hydrolysis;
dbSNP:rs1801466).
{ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:11379881,
ECO:0000269|PubMed:11384574,
ECO:0000269|PubMed:11527935,
ECO:0000269|PubMed:11594993}.
/FTId=VAR_008470.
VARIANT 1884 1884 V -> E (in STGD1; dbSNP:rs62642578).
/FTId=VAR_012598.
VARIANT 1885 1885 E -> K (in STGD1; dbSNP:rs62642563).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012599.
VARIANT 1886 1886 G -> E (in STGD1; highly reduced ATP-
binding capacity; dbSNP:rs62642579).
/FTId=VAR_008471.
VARIANT 1890 1890 Missing (in STGD1).
/FTId=VAR_008472.
VARIANT 1896 1896 V -> D (in STGD1; dbSNP:rs61750636).
/FTId=VAR_012600.
VARIANT 1898 1898 R -> H (in STGD1 and ARMD2;
dbSNP:rs1800552).
{ECO:0000269|PubMed:10746567,
ECO:0000269|PubMed:10958763}.
/FTId=VAR_008473.
VARIANT 1921 1921 V -> M (in dbSNP:rs61753032).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012601.
VARIANT 1940 1940 L -> P (in STGD1 and FFM;
dbSNP:rs61753033).
{ECO:0000269|PubMed:11385708,
ECO:0000269|PubMed:18977788}.
/FTId=VAR_012602.
VARIANT 1948 1948 P -> L (in dbSNP:rs56142141).
{ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:11385708,
ECO:0000269|PubMed:11527935,
ECO:0000269|PubMed:11594993}.
/FTId=VAR_008474.
VARIANT 1961 1961 G -> E (in STGD1 and FFM; frequent
mutation; may be associated with ARMD2;
inhibition of ATP hydrolysis by retinal;
dbSNP:rs1800553).
{ECO:0000269|PubMed:10206579,
ECO:0000269|PubMed:10711710,
ECO:0000269|PubMed:10880298,
ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:11346402,
ECO:0000269|PubMed:11527935,
ECO:0000269|PubMed:18977788}.
/FTId=VAR_008475.
VARIANT 1970 1970 L -> F (in ARMD2 and FFM;
dbSNP:rs28938473).
{ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:9781034}.
/FTId=VAR_008476.
VARIANT 1971 1971 L -> R (in FFM; highly reduced ATP-
binding capacity; abolishes basal and
retinal-stimulated ATP hydrolysis;
dbSNP:rs61753034).
{ECO:0000269|PubMed:9781034}.
/FTId=VAR_012603.
VARIANT 1975 1975 G -> R (in STGD1; dbSNP:rs61753036).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012604.
VARIANT 1977 1977 G -> S (in STGD1 and ARMD2; highly
reduced ATP-binding capacity; inhibition
of ATP hydrolysis by retinal;
dbSNP:rs61750639).
{ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:11527935,
ECO:0000269|PubMed:18977788,
ECO:0000269|PubMed:19028736,
ECO:0000269|PubMed:9781034}.
/FTId=VAR_008477.
VARIANT 2027 2027 L -> F (in STGD1 and FFM; highly reduced
ATP-binding capacity; dbSNP:rs61751408).
{ECO:0000269|PubMed:11379881,
ECO:0000269|PubMed:11527935,
ECO:0000269|PubMed:18977788}.
/FTId=VAR_008478.
VARIANT 2030 2030 R -> Q (in STGD1 and FFM;
dbSNP:rs61750641).
{ECO:0000269|PubMed:11379881,
ECO:0000269|PubMed:11527935}.
/FTId=VAR_008480.
VARIANT 2035 2035 L -> P (in STGD1; dbSNP:rs61750642).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012605.
VARIANT 2038 2038 R -> W (in STGD1; highly reduced ATP-
binding capacity; dbSNP:rs61750643).
{ECO:0000269|PubMed:10206579}.
/FTId=VAR_008495.
VARIANT 2047 2047 I -> N (in ARMD2).
{ECO:0000269|PubMed:19028736}.
/FTId=VAR_067429.
VARIANT 2050 2050 V -> L (in STGD1; dbSNP:rs41292677).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_008481.
VARIANT 2059 2059 G -> A. {ECO:0000269|PubMed:10958763}.
/FTId=VAR_012606.
VARIANT 2060 2060 L -> R (in CORD3; dbSNP:rs61753039).
{ECO:0000269|PubMed:11385708,
ECO:0000269|PubMed:18977788}.
/FTId=VAR_012607.
VARIANT 2071 2071 Y -> F (in STGD1).
/FTId=VAR_012608.
VARIANT 2077 2077 R -> G (in STGD1; dbSNP:rs61750645).
{ECO:0000269|PubMed:10958763}.
/FTId=VAR_012609.
VARIANT 2077 2077 R -> W (in STGD1; highly reduced ATP-
binding capacity; dbSNP:rs61750645).
{ECO:0000269|PubMed:10206579,
ECO:0000269|PubMed:10958763}.
/FTId=VAR_008482.
VARIANT 2096 2096 E -> K (in STGD1; inhibition of ATP
hydrolysis by retinal; dbSNP:rs61750646).
/FTId=VAR_008483.
VARIANT 2106 2106 R -> C (in STGD1 and FFM; reduced ATP-
binding capacity; dbSNP:rs61750648).
{ECO:0000269|PubMed:11379881}.
/FTId=VAR_008484.
VARIANT 2107 2107 R -> C (in STGD1; dbSNP:rs2297669).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012610.
VARIANT 2107 2107 R -> H (in STGD1; may predispose to
develop retinal toxicity after treatment
with chloroquine and hydroxychloroquine;
dbSNP:rs62642564).
{ECO:0000269|PubMed:10206579,
ECO:0000269|PubMed:11384574,
ECO:0000269|PubMed:11385708,
ECO:0000269|PubMed:11527935,
ECO:0000269|PubMed:18977788,
ECO:0000269|PubMed:9781034}.
/FTId=VAR_008485.
VARIANT 2128 2128 H -> R (in STGD1; dbSNP:rs61750651).
{ECO:0000269|PubMed:10206579}.
/FTId=VAR_008486.
VARIANT 2131 2131 E -> K (in STGD1; dbSNP:rs61750652).
/FTId=VAR_008487.
VARIANT 2137 2137 C -> Y (in ARMD2).
{ECO:0000269|PubMed:19028736}.
/FTId=VAR_067430.
VARIANT 2139 2139 R -> W (in STGD1; dbSNP:rs61750653).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_008488.
VARIANT 2146 2146 G -> D (in CORD3; dbSNP:rs61753044).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012611.
VARIANT 2149 2149 R -> L (in STGD1; dbSNP:rs61750655).
/FTId=VAR_012612.
VARIANT 2150 2150 C -> R (in STGD1; dbSNP:rs61750656).
{ECO:0000269|PubMed:11527935}.
/FTId=VAR_012613.
VARIANT 2150 2150 C -> Y (in STGD1 and CORD3;
dbSNP:rs61751384).
{ECO:0000269|PubMed:10206579,
ECO:0000269|PubMed:11527935,
ECO:0000269|PubMed:18977788}.
/FTId=VAR_008489.
VARIANT 2160 2160 K -> R (in STGD1; dbSNP:rs281865405).
/FTId=VAR_008490.
VARIANT 2177 2177 D -> N (may be associated with ARMD2;
increased retinal-stimulated ATP
hydrolysis; dbSNP:rs1800555).
{ECO:0000269|PubMed:10880298,
ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:11346402}.
/FTId=VAR_008491.
VARIANT 2216 2216 A -> V. {ECO:0000269|PubMed:10958763}.
/FTId=VAR_012614.
VARIANT 2229 2229 L -> P (in STGD1; dbSNP:rs61750659).
/FTId=VAR_012615.
VARIANT 2241 2241 L -> V (in STGD1; dbSNP:rs61748521).
{ECO:0000269|PubMed:10958763,
ECO:0000269|PubMed:18977788}.
/FTId=VAR_012616.
VARIANT 2255 2255 S -> I (in dbSNP:rs6666652).
{ECO:0000269|PubMed:11379881,
ECO:0000269|PubMed:11384574,
ECO:0000269|PubMed:11385708}.
/FTId=VAR_009157.
VARIANT 2263 2263 R -> L (in STGD1; dbSNP:rs281865407).
/FTId=VAR_012617.
MUTAGEN 966 966 G->D: Abolishes basal and retinal-
stimulated ATP hydrolysis.
{ECO:0000269|PubMed:11017087}.
MUTAGEN 969 969 K->M: Abolishes basal and retinal-
stimulated ATP hydrolysis.
{ECO:0000269|PubMed:11017087}.
MUTAGEN 1975 1975 G->D: Inhibition of retinal-stimulated
ATP hydrolysis.
{ECO:0000269|PubMed:11017087}.
MUTAGEN 1978 1978 K->M: Inhibition of retinal-stimulated
ATP hydrolysis.
{ECO:0000269|PubMed:11017087}.
CONFLICT 722 722 G -> V (in Ref. 2; AAC23915).
{ECO:0000305}.
CONFLICT 849 849 V -> C (in Ref. 1; AAC51144).
{ECO:0000305}.
CONFLICT 882 882 G -> S (in Ref. 1; AAC51144 and 3;
CAA75729). {ECO:0000305}.
CONFLICT 941 941 C -> S (in Ref. 2; AAC23915).
{ECO:0000305}.
CONFLICT 1116 1116 S -> P (in Ref. 1; AAC51144).
{ECO:0000305}.
CONFLICT 1125 1126 LL -> HQ (in Ref. 1; AAC51144).
{ECO:0000305}.
CONFLICT 1395 1395 P -> L (in Ref. 1; AAC51144 and 3;
CAA75729). {ECO:0000305}.
CONFLICT 1465 1465 S -> C (in Ref. 4; AAC05632).
{ECO:0000305}.
CONFLICT 1518 1518 S -> T (in Ref. 4; AAC05632).
{ECO:0000305}.
CONFLICT 1733 1733 M -> V (in Ref. 2; AAC23915).
{ECO:0000305}.
CONFLICT 1989 1989 T -> N (in Ref. 2; AAC23915).
{ECO:0000305}.
CONFLICT 2119 2119 E -> K (in Ref. 1; AAC51144).
{ECO:0000305}.
SEQUENCE 2273 AA; 255944 MW; 6E7012D3041CD043 CRC64;
MGFVRQIQLL LWKNWTLRKR QKIRFVVELV WPLSLFLVLI WLRNANPLYS HHECHFPNKA
MPSAGMLPWL QGIFCNVNNP CFQSPTPGES PGIVSNYNNS ILARVYRDFQ ELLMNAPESQ
HLGRIWTELH ILSQFMDTLR THPERIAGRG IRIRDILKDE ETLTLFLIKN IGLSDSVVYL
LINSQVRPEQ FAHGVPDLAL KDIACSEALL ERFIIFSQRR GAKTVRYALC SLSQGTLQWI
EDTLYANVDF FKLFRVLPTL LDSRSQGINL RSWGGILSDM SPRIQEFIHR PSMQDLLWVT
RPLMQNGGPE TFTKLMGILS DLLCGYPEGG GSRVLSFNWY EDNNYKAFLG IDSTRKDPIY
SYDRRTTSFC NALIQSLESN PLTKIAWRAA KPLLMGKILY TPDSPAARRI LKNANSTFEE
LEHVRKLVKA WEEVGPQIWY FFDNSTQMNM IRDTLGNPTV KDFLNRQLGE EGITAEAILN
FLYKGPRESQ ADDMANFDWR DIFNITDRTL RLVNQYLECL VLDKFESYND ETQLTQRALS
LLEENMFWAG VVFPDMYPWT SSLPPHVKYK IRMDIDVVEK TNKIKDRYWD SGPRADPVED
FRYIWGGFAY LQDMVEQGIT RSQVQAEAPV GIYLQQMPYP CFVDDSFMII LNRCFPIFMV
LAWIYSVSMT VKSIVLEKEL RLKETLKNQG VSNAVIWCTW FLDSFSIMSM SIFLLTIFIM
HGRILHYSDP FILFLFLLAF STATIMLCFL LSTFFSKASL AAACSGVIYF TLYLPHILCF
AWQDRMTAEL KKAVSLLSPV AFGFGTEYLV RFEEQGLGLQ WSNIGNSPTE GDEFSFLLSM
QMMLLDAAVY GLLAWYLDQV FPGDYGTPLP WYFLLQESYW LGGEGCSTRE ERALEKTEPL
TEETEDPEHP EGIHDSFFER EHPGWVPGVC VKNLVKIFEP CGRPAVDRLN ITFYENQITA
FLGHNGAGKT TTLSILTGLL PPTSGTVLVG GRDIETSLDA VRQSLGMCPQ HNILFHHLTV
AEHMLFYAQL KGKSQEEAQL EMEAMLEDTG LHHKRNEEAQ DLSGGMQRKL SVAIAFVGDA
KVVILDEPTS GVDPYSRRSI WDLLLKYRSG RTIIMSTHHM DEADLLGDRI AIIAQGRLYC
SGTPLFLKNC FGTGLYLTLV RKMKNIQSQR KGSEGTCSCS SKGFSTTCPA HVDDLTPEQV
LDGDVNELMD VVLHHVPEAK LVECIGQELI FLLPNKNFKH RAYASLFREL EETLADLGLS
SFGISDTPLE EIFLKVTEDS DSGPLFAGGA QQKRENVNPR HPCLGPREKA GQTPQDSNVC
SPGAPAAHPE GQPPPEPECP GPQLNTGTQL VLQHVQALLV KRFQHTIRSH KDFLAQIVLP
ATFVFLALML SIVIPPFGEY PALTLHPWIY GQQYTFFSMD EPGSEQFTVL ADVLLNKPGF
GNRCLKEGWL PEYPCGNSTP WKTPSVSPNI TQLFQKQKWT QVNPSPSCRC STREKLTMLP
ECPEGAGGLP PPQRTQRSTE ILQDLTDRNI SDFLVKTYPA LIRSSLKSKF WVNEQRYGGI
SIGGKLPVVP ITGEALVGFL SDLGRIMNVS GGPITREASK EIPDFLKHLE TEDNIKVWFN
NKGWHALVSF LNVAHNAILR ASLPKDRSPE EYGITVISQP LNLTKEQLSE ITVLTTSVDA
VVAICVIFSM SFVPASFVLY LIQERVNKSK HLQFISGVSP TTYWVTNFLW DIMNYSVSAG
LVVGIFIGFQ KKAYTSPENL PALVALLLLY GWAVIPMMYP ASFLFDVPST AYVALSCANL
FIGINSSAIT FILELFENNR TLLRFNAVLR KLLIVFPHFC LGRGLIDLAL SQAVTDVYAR
FGEEHSANPF HWDLIGKNLF AMVVEGVVYF LLTLLVQRHF FLSQWIAEPT KEPIVDEDDD
VAEERQRIIT GGNKTDILRL HELTKIYPGT SSPAVDRLCV GVRPGECFGL LGVNGAGKTT
TFKMLTGDTT VTSGDATVAG KSILTNISEV HQNMGYCPQF DAIDELLTGR EHLYLYARLR
GVPAEEIEKV ANWSIKSLGL TVYADCLAGT YSGGNKRKLS TAIALIGCPP LVLLDEPTTG
MDPQARRMLW NVIVSIIREG RAVVLTSHSM EECEALCTRL AIMVKGAFRC MGTIQHLKSK
FGDGYIVTMK IKSPKDDLLP DLNPVEQFFQ GNFPGSVQRE RHYNMLQFQV SSSSLARIFQ
LLLSHKDSLL IEEYSVTQTT LDQVFVNFAK QQTESHDLPL HPRAAGASRQ AQD


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