ID CRUM1_HUMAN Reviewed; 1406 AA. AC P82279; A2A308; B7Z5T2; B9EG71; Q5K3A6; Q5TC28; Q5VUT1; Q6N027; AC Q8WWY0; Q8WWY1; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 2. DT 25-OCT-2017, entry version 177. DE RecName: Full=Protein crumbs homolog 1; DE Flags: Precursor; GN Name=CRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS RP12 VAL-161; RP TRP-250; MET-745; CYS-764; TYR-948; THR-1041 AND PRO-1071. RC TISSUE=Fetal brain, and Retina; RX PubMed=10508521; DOI=10.1038/13848; RA den Hollander A.I., ten Brink J.B., de Kok Y.J.M., van Soest S., RA van den Born L.I., van Driel M.A., van de Pol D.J.R., Payne A.M., RA Bhattacharya S.S., Kellner U., Hoyng C.B., Westerveld A., RA Brunner H.G., Bleeker-Wagemakers E.M., Deutman A.F., RA Heckenlively J.R., Cremers F.P.M., Bergen A.A.B.; RT "Mutations in a human homologue of Drosophila crumbs cause retinitis RT pigmentosa (RP12)."; RL Nat. Genet. 23:217-221(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RX PubMed=11734541; DOI=10.1093/hmg/10.24.2767; RA den Hollander A.I., Johnson K., de Kok Y.J.M., Klebes A., RA Brunner H.G., Knust E., Cremers F.P.M.; RT "CRB1 has a cytoplasmic domain that is functionally conserved between RT human and Drosophila."; RL Hum. Mol. Genet. 10:2767-2773(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), COMPLEX FORMATION WITH MPP4 RP AND MPP5, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Retina; RX PubMed=15914641; DOI=10.1167/iovs.04-1417; RA Kantardzhieva A., Gosens I., Alexeeva S., Punte I.M., Versteeg I., RA Krieger E., Neefjes-Mol C.A., den Hollander A.I., Letteboer S.J.F., RA Klooster J., Cremers F.P.M., Roepman R., Wijnholds J.; RT "MPP5 recruits MPP4 to the CRB1 complex in photoreceptors."; RL Invest. Ophthalmol. Vis. Sci. 46:2192-2201(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Retina; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cerebellum; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP INVOLVEMENT IN LCA8. RX PubMed=12567265; DOI=10.1076/opge.23.4.225.13879; RA Gerber S., Perrault I., Hanein S., Shalev S., Zlotogora J., Barbet F., RA Ducroq D., Dufier J.-L., Munnich A., Rozet J., Kaplan J.; RT "A novel mutation disrupting the cytoplasmic domain of CRB1 in a large RT consanguineous family of Palestinian origin affected with Leber RT congenital amaurosis."; RL Ophthalmic Genet. 23:225-235(2002). RN [10] RP VARIANTS LCA8 TYR-948 AND ARG-1100, VARIANTS RP12 CYS-433; CYS-764; RP HIS-837; SER-894; TYR-948 AND ARG-1181, AND VARIANTS MET-289; MET-821; RP HIS-1331 AND THR-1354. RX PubMed=11389483; DOI=10.1086/321263; RA den Hollander A.I., Heckenlively J.R., van den Born L.I., RA de Kok Y.J.M., van der Velde-Visser S.D., Kellner U., Jurklies B., RA van Schooneveld M.J., Blankenagel A., Rohrschneider K., Wissinger B., RA Cruysberg J.R.M., Deutman A.F., Brunner H.G., Apfelstedt-Sylla E., RA Hoyng C.B., Cremers F.P.M.; RT "Leber congenital amaurosis and retinitis pigmentosa with Coats-like RT exudative vasculopathy are associated with mutations in the crumbs RT homologue 1 (CRB1) gene."; RL Am. J. Hum. Genet. 69:198-203(2001). RN [11] RP ERRATUM. RA den Hollander A.I., Heckenlively J.R., van den Born L.I., RA de Kok Y.J.M., van der Velde-Visser S.D., Kellner U., Jurklies B., RA van Schooneveld M.J., Blankenagel A., Rohrschneider K., Wissinger B., RA Cruysberg J.R.M., Deutman A.F., Brunner H.G., Apfelstedt-Sylla E., RA Hoyng C.B., Cremers F.P.M.; RL Am. J. Hum. Genet. 69:1160-1160(2001). RN [12] RP VARIANTS LCA8 VAL-144; TYR-383; GLY-480; ARG-480; TYR-681; CYS-764; RP TYR-948; ARG-1205 AND HIS-1317, AND VARIANTS MET-289; GLN-769 AND RP HIS-1331. RX PubMed=11231775; DOI=10.1001/archopht.119.3.415; RA Lotery A.J., Jacobson S.G., Fishman G.A., Weleber R.G., Fulton A.B., RA Namperumalsamy P., Heon E., Levin A.V., Grover S., Rosenow J.R., RA Kopp K.K., Sheffield V.C., Stone E.M.; RT "Mutations in the CRB1 gene cause Leber congenital amaurosis."; RL Arch. Ophthalmol. 119:415-420(2001). RN [13] RP VARIANT RP12 SER-1321. RX PubMed=11559858; DOI=10.1076/opge.22.3.163.2222; RA Lotery A.J., Malik A., Shami S.A., Sindhi M., Chohan B., Maqbool C., RA Moore P.A., Denton M.J., Stone E.M.; RT "CRB1 mutations may result in retinitis pigmentosa without para- RT arteriolar RPE preservation."; RL Ophthalmic Genet. 22:163-169(2001). RN [14] RP VARIANTS RP12 ARG-846 AND PRO-1071, AND VARIANT LCA8 THR-989. RX PubMed=12573663; DOI=10.1016/S0014-4835(02)00304-4; RA Khaliq S., Abid A., Hameed A., Anwar K., Mohyuddin A., Azmat Z., RA Shami S.A., Ismail M., Mehdi S.Q.; RT "Mutation screening of Pakistani families with congenital eye RT disorders."; RL Exp. Eye Res. 76:343-348(2003). RN [15] RP VARIANTS LCA8 SER-749 DEL; CYS-764; TYR-948 AND PHE-1218. RX PubMed=12700176; DOI=10.1093/hmg/ddg117; RA Jacobson S.G., Cideciyan A.V., Aleman T.S., Pianta M.J., Sumaroka A., RA Schwartz S.B., Smilko E.E., Milam A.H., Sheffield V.C., Stone E.M.; RT "Crumbs homolog 1 (CRB1) mutations result in a thick human retina with RT abnormal lamination."; RL Hum. Mol. Genet. 12:1073-1078(2003). RN [16] RP VARIANTS RP12 SER-749 DEL; GLY-891; TYR-948; LEU-962 DEL AND THR-1100, RP AND VARIANTS THR-205; MET-289; GLU-679; HIS-769 AND HIS-1331. RX PubMed=12843338; DOI=10.1136/jmg.40.7.e89; RA Bernal S., Calaf M., Garcia-Hoyos M., Garcia-Sandoval B., Rosell J., RA Adan A., Ayuso C., Baiget M.; RT "Study of the involvement of the RGR, CRPB1, and CRB1 genes in the RT pathogenesis of autosomal recessive retinitis pigmentosa."; RL J. Med. Genet. 40:E89-E89(2003). RN [17] RP VARIANTS LCA8 TYR-584; GLN-710; THR-741; MET-745; CYS-764; THR-852; RP TYR-948; ILE-1025; ARG-1103; ARG-1107; PRO-1107 AND SER-1321. RX PubMed=15024725; DOI=10.1002/humu.20010; RA Hanein S., Perrault I., Gerber S., Tanguy G., Barbet F., Ducroq D., RA Calvas P., Dollfus H., Hamel C., Lopponen T., Munier F., Santos L., RA Shalev S., Zafeiriou D., Dufier J.-L., Munnich A., Rozet J.-M., RA Kaplan J.; RT "Leber congenital amaurosis: comprehensive survey of the genetic RT heterogeneity, refinement of the clinical definition, and genotype- RT phenotype correlations as a strategy for molecular diagnosis."; RL Hum. Mutat. 23:306-317(2004). RN [18] RP VARIANTS RP12 PHE-195; GLU-578; TYR-587; MET-745; CYS-764; THR-836; RP SER-850; TYR-948; ILE-986; THR-1100 AND HIS-1383, AND VARIANTS RP THR-205; GLN-905 AND SER-959. RX PubMed=15459956; DOI=10.1002/humu.20093; RA den Hollander A.I., Davis J., van der Velde-Visser S.D., RA Zonneveld M.N., Pierrottet C.O., Koenekoop R.K., Kellner U., RA van den Born L.I., Heckenlively J.R., Hoyng C.B., Handford P.A., RA Roepman R., Cremers F.P.M.; RT "CRB1 mutation spectrum in inherited retinal dystrophies."; RL Hum. Mutat. 24:355-369(2004). RN [19] RP VARIANT PPCRA MET-162. RX PubMed=15623792; DOI=10.1167/iovs.04-0734; RA McKay G.J., Clarke S., Davis J.A., Simpson D.A., Silvestri G.; RT "Pigmented paravenous chorioretinal atrophy is associated with a RT mutation within the crumbs homolog 1 (CRB1) gene."; RL Invest. Ophthalmol. Vis. Sci. 46:322-328(2005). RN [20] RP VARIANTS LCA8 PRO-753; CYS-764 AND TYR-948. RX PubMed=15691574; DOI=10.1016/j.ophtha.2004.08.023; RA Galvin J.A., Fishman G.A., Stone E.M., Koenekoop R.K.; RT "Clinical phenotypes in carriers of Leber congenital amaurosis RT mutations."; RL Ophthalmology 112:349-356(2005). RN [21] RP VARIANTS LCA8 ARG-480; TYR-681; PRO-753; CYS-764 AND TYR-948, AND RP VARIANT SER-488. RX PubMed=16205573; DOI=10.1097/00006982-200510000-00016; RA Galvin J.A., Fishman G.A., Stone E.M., Koenekoop R.K.; RT "Evaluation of genotype-phenotype associations in Leber congenital RT amaurosis."; RL Retina 25:919-929(2005). RN [22] RP VARIANT LCA8 TYR-564. RX PubMed=17128490; RA Vallespin E., Riveiro-Alvarez R., Aguirre-Lamban J., Cantalapiedra D., RA Tapias I., Garcia-Sandoval B., Trujillo-Tiebas M.J., Ayuso C.; RT "Gene symbol: CRB1. Disease: early onset retinitis pigmentosa."; RL Hum. Genet. 119:681-681(2006). RN [23] RP VARIANT LCA8 ARG-454. RX PubMed=16936081; DOI=10.1167/iovs.05-1637; RA Yzer S., Fishman G.A., Racine J., Al-Zuhaibi S., Chakor H., RA Dorfman A., Szlyk J., Lachapelle P., van den Born L.I., Allikmets R., RA Lopez I., Cremers F.P., Koenekoop R.K.; RT "CRB1 heterozygotes with regional retinal dysfunction: implications RT for genetic testing of Leber congenital amaurosis."; RL Invest. Ophthalmol. Vis. Sci. 47:3736-3744(2006). RN [24] RP VARIANT [LARGE SCALE ANALYSIS] MET-745. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). RN [25] RP VARIANT LCA8 PRO-535. RX PubMed=17438615; RA Vallespin E., Millan J.M., Riveiro-Alvarez R., Aguirre-Lamban J., RA Cantalapiedra D., Gallego J., Trujillo-Tiebas M.J., Ayuso C.; RT "Gene symbol: CRB1."; RL Hum. Genet. 120:914-914(2007). RN [26] RP VARIANTS LCA8 TYR-438; MET-745; THR-852 AND ARG-1103, AND VARIANT RP MET-289. RX PubMed=17724218; DOI=10.1167/iovs.07-0068; RA Simonelli F., Ziviello C., Testa F., Rossi S., Fazzi E., Bianchi P.E., RA Fossarello M., Signorini S., Bertone C., Galantuomo S., Brancati F., RA Valente E.M., Ciccodicola A., Rinaldi E., Auricchio A., Banfi S.; RT "Clinical and molecular genetics of Leber's congenital amaurosis: a RT multicenter study of Italian patients."; RL Invest. Ophthalmol. Vis. Sci. 48:4284-4290(2007). RN [27] RP VARIANTS LCA8 TYR-939; TYR-948 AND PHE-1332. RX PubMed=18055821; DOI=10.1167/iovs.07-0610; RA den Hollander A.I., Lopez I., Yzer S., Zonneveld M.N., Janssen I.M., RA Strom T.M., Hehir-Kwa J.Y., Veltman J.A., Arends M.L., Meitinger T., RA Musarella M.A., van den Born L.I., Fishman G.A., Maumenee I.H., RA Rohrschneider K., Cremers F.P., Koenekoop R.K.; RT "Identification of novel mutations in patients with Leber congenital RT amaurosis and juvenile RP by genome-wide homozygosity mapping with SNP RT microarrays."; RL Invest. Ophthalmol. Vis. Sci. 48:5690-5698(2007). RN [28] RP VARIANT LCA8 ASP-333, AND VARIANTS HIS-769 AND THR-937. RX PubMed=18682808; RA Seong M.W., Kim S.Y., Yu Y.S., Hwang J.M., Kim J.Y., Park S.S.; RT "Molecular characterization of Leber congenital amaurosis in RT Koreans."; RL Mol. Vis. 14:1429-1436(2008). RN [29] RP VARIANT RP12 ARG-1103. RX PubMed=19140180; DOI=10.1002/ajmg.a.32634; RA Benayoun L., Spiegel R., Auslender N., Abbasi A.H., Rizel L., RA Hujeirat Y., Salama I., Garzozi H.J., Allon-Shalev S., Ben-Yosef T.; RT "Genetic heterogeneity in two consanguineous families segregating RT early onset retinal degeneration: the pitfalls of homozygosity RT mapping."; RL Am. J. Med. Genet. A 149:650-656(2009). RN [30] RP VARIANTS RP12 PHE-27 AND TRP-1165. RX PubMed=19956407; RA Aldahmesh M.A., Safieh L.A., Alkuraya H., Al-Rajhi A., Shamseldin H., RA Hashem M., Alzahrani F., Khan A.O., Alqahtani F., Rahbeeni Z., RA Alowain M., Khalak H., Al-Hazzaa S., Meyer B.F., Alkuraya F.S.; RT "Molecular characterization of retinitis pigmentosa in Saudi Arabia."; RL Mol. Vis. 15:2464-2469(2009). RN [31] RP VARIANT LCA8 CYS-1161. RX PubMed=20108431; RA Vallespin E., Avila-Fernandez A., Velez-Monsalve C., Almoguera B., RA Martinez-Garcia M., Gomez-Dominguez B., Gonzalez-Roubaud C., RA Cantalapiedra D., Trujillo-Tiebas M.J., Ayuso C.; RT "Novel human pathological mutations. Gene symbol: CRB1. Disease: Leber RT congenital amaurosis."; RL Hum. Genet. 127:119-119(2010). RN [32] RP INVOLVEMENT IN RETINAL DYSTROPHIES, VARIANTS EARLY-ONSET RETINAL RP DYSTROPHY TYR-310; CYS-764 AND TYR-948, AND VARIANT VAL-491. RX PubMed=20683928; DOI=10.1002/humu.21336; RA Coppieters F., Casteels I., Meire F., De Jaegere S., Hooghe S., RA van Regemorter N., Van Esch H., Matuleviciene A., Nunes L., RA Meersschaut V., Walraedt S., Standaert L., Coucke P., Hoeben H., RA Kroes H.Y., Vande Walle J., de Ravel T., Leroy B.P., De Baere E.; RT "Genetic screening of LCA in Belgium: predominance of CEP290 and RT identification of potential modifier alleles in AHI1 of CEP290-related RT phenotypes."; RL Hum. Mutat. 31:E1709-E1766(2010). RN [33] RP VARIANTS RP12 TRP-45; VAL-710; MET-745; SER-850; TYR-948 AND HIS-1383, RP AND VARIANTS HIS-769 AND ILE-901. RX PubMed=20591486; DOI=10.1016/j.ophtha.2010.02.029; RA Clark G.R., Crowe P., Muszynska D., O'Prey D., O'Neill J., RA Alexander S., Willoughby C.E., McKay G.J., Silvestri G., Simpson D.A.; RT "Development of a diagnostic genetic test for simplex and autosomal RT recessive retinitis pigmentosa."; RL Ophthalmology 117:2169-2177(2010). RN [34] RP VARIANT RP12 LYS-1099. RX PubMed=21987686; DOI=10.1001/archophthalmol.2011.290; RA Azam M., Collin R.W., Malik A., Khan M.I., Shah S.T., Shah A.A., RA Hussain A., Sadeque A., Arimadyo K., Ajmal M., Azam A., Qureshi N., RA Bokhari H., Strom T.M., Cremers F.P., Qamar R., den Hollander A.I.; RT "Identification of novel mutations in Pakistani families with RT autosomal recessive retinitis pigmentosa."; RL Arch. Ophthalmol. 129:1377-1378(2011). RN [35] RP VARIANTS RP12 SER-157; TRP-250; LYS-312; CYS-675; VAL-710; MET-745; RP CYS-764; THR-836; ARG-846; TYR-948; SER-1012; ASN-1025 AND GLY-1174, RP VARIANTS LCA8 SER-850; THR-1003; ARG-1103; PRO-1107; GLY-1174 AND RP LEU-1381, VARIANTS EARLY-ONSET RETINAL DYSTROPHY THR-741 AND ASP-1365, RP AND VARIANT THR-205. RX PubMed=20956273; DOI=10.1136/bjo.2010.186882; RA Henderson R.H., Mackay D.S., Li Z., Moradi P., Sergouniotis P., RA Russell-Eggitt I., Thompson D.A., Robson A.G., Holder G.E., RA Webster A.R., Moore A.T.; RT "Phenotypic variability in patients with retinal dystrophies due to RT mutations in CRB1."; RL Br. J. Ophthalmol. 95:811-817(2011). RN [36] RP VARIANT RP12 LEU-1305. RX PubMed=22128245; RA Siemiatkowska A.M., Arimadyo K., Moruz L.M., Astuti G.D., RA de Castro-Miro M., Zonneveld M.N., Strom T.M., de Wijs I.J., RA Hoefsloot L.H., Faradz S.M., Cremers F.P., den Hollander A.I., RA Collin R.W.; RT "Molecular genetic analysis of retinitis pigmentosa in Indonesia using RT genome-wide homozygosity mapping."; RL Mol. Vis. 17:3013-3024(2011). RN [37] RP VARIANT LCA8 THR-741, AND VARIANTS LYS-222; MET-289 AND PRO-635. RX PubMed=21602930; DOI=10.1371/journal.pone.0019458; RA Li L., Xiao X., Li S., Jia X., Wang P., Guo X., Jiao X., Zhang Q., RA Hejtmancik J.F.; RT "Detection of variants in 15 genes in 87 unrelated Chinese patients RT with Leber congenital amaurosis."; RL PLoS ONE 6:E19458-E19458(2011). RN [38] RP INVOLVEMENT IN RETINAL DYSTROPHIES, VARIANTS RP12 TYR-584; PHE-740; RP THR-741; THR-836; TYR-948 AND ARG-1103, AND VARIANTS EARLY-ONSET RP RETINAL DYSTROPHY ASN-789 DEL; CYS-1198 AND SER-1223. RX PubMed=22065545; DOI=10.1002/humu.21653; RA Bujakowska K., Audo I., Mohand-Said S., Lancelot M.E., Antonio A., RA Germain A., Leveillard T., Letexier M., Saraiva J.P., Lonjou C., RA Carpentier W., Sahel J.A., Bhattacharya S.S., Zeitz C.; RT "CRB1 mutations in inherited retinal dystrophies."; RL Hum. Mutat. 33:306-315(2012). RN [39] RP VARIANTS RP12 ASN-534 AND MET-745. RX PubMed=22334370; DOI=10.1002/humu.22045; RA Neveling K., Collin R.W., Gilissen C., van Huet R.A., Visser L., RA Kwint M.P., Gijsen S.J., Zonneveld M.N., Wieskamp N., de Ligt J., RA Siemiatkowska A.M., Hoefsloot L.H., Buckley M.F., Kellner U., RA Branham K.E., den Hollander A.I., Hoischen A., Hoyng C., RA Klevering B.J., van den Born L.I., Veltman J.A., Cremers F.P., RA Scheffer H.; RT "Next-generation genetic testing for retinitis pigmentosa."; RL Hum. Mutat. 33:963-972(2012). CC -!- FUNCTION: Plays a role in photoreceptor morphogenesis in the CC retina. May maintain cell polarization and adhesion. CC -!- SUBUNIT: Forms a complex with MPDZ (By similarity). Forms a CC complex with MPP4 and MPP5. {ECO:0000250}. CC -!- INTERACTION: CC Q8NI35:PATJ; NbExp=2; IntAct=EBI-1048648, EBI-724390; CC -!- SUBCELLULAR LOCATION: Isoform 1: Apical cell membrane; Single-pass CC type I membrane protein. Note=Distributed at the apical membrane CC of all retinal epithelial cells. Located in the apical membrane of CC the adherens junction in outer limiting membrane (OLM) of the CC retina. CC -!- SUBCELLULAR LOCATION: Isoform 2: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=P82279-1; Sequence=Displayed; CC Name=2; CC IsoId=P82279-2; Sequence=VSP_014728, VSP_014729; CC Note=Variant in position: 1361:R->H (found in a patient with CC Leber congenital amaurosis, unknown pathological significance).; CC Name=3; CC IsoId=P82279-3; Sequence=VSP_014725; CC Note=No experimental confirmation available.; CC Name=4; CC IsoId=P82279-4; Sequence=VSP_014724, VSP_014726, VSP_014727; CC Note=No experimental confirmation available.; CC Name=5; CC IsoId=P82279-5; Sequence=VSP_045332; CC -!- TISSUE SPECIFICITY: Preferential expression in retina, also CC expressed in brain, testis, fetal brain and fetal eye. CC {ECO:0000269|PubMed:15914641}. CC -!- PTM: Extensively glycosylated. CC -!- DISEASE: Note=CRB1 mutations have been found in various retinal CC dystrophies, chronic and disabling disorders of visual function. CC They predominantly involve the posterior portion of the ocular CC fundus, due to degeneration in the sensory layer of the retina, CC retinal pigment epithelium, Bruch membrane, choroid, or a CC combination of these tissues. Onset of inherited retinal CC dystrophies is painless, bilateral and typically progressive. Most CC people experience gradual peripheral vision loss or tunnel vision, CC and difficulties with poor illumination and night vision. Central CC vision is usually unaffected, so the person may still be able to CC read. However, it can also deteriorate to cause total blindness. CC Examples of retinal dystrophies are retinitis pigmentosa, Leber CC congenital amaurosis, cone-rod dystrophy among others. CC {ECO:0000269|PubMed:20683928, ECO:0000269|PubMed:22065545}. CC -!- DISEASE: Retinitis pigmentosa 12 (RP12) [MIM:600105]: A retinal CC dystrophy belonging to the group of pigmentary retinopathies. CC Retinitis pigmentosa is characterized by retinal pigment deposits CC visible on fundus examination and primary loss of rod CC photoreceptor cells followed by secondary loss of cone CC photoreceptors. Patients typically have night vision blindness and CC loss of midperipheral visual field. As their condition progresses, CC they lose their far peripheral visual field and eventually central CC vision as well. RP12 is an autosomal recessive, severe form often CC manifesting in early childhood. Patients experiment progressive CC visual field loss with severe visual impairment before the age of CC twenty. Some patients have a preserved paraarteriolar retinal CC pigment epithelium (PPRPE) and hypermetropia. CC {ECO:0000269|PubMed:10508521, ECO:0000269|PubMed:11389483, CC ECO:0000269|PubMed:11559858, ECO:0000269|PubMed:12573663, CC ECO:0000269|PubMed:12843338, ECO:0000269|PubMed:15459956, CC ECO:0000269|PubMed:19140180, ECO:0000269|PubMed:19956407, CC ECO:0000269|PubMed:20591486, ECO:0000269|PubMed:20956273, CC ECO:0000269|PubMed:21987686, ECO:0000269|PubMed:22065545, CC ECO:0000269|PubMed:22128245, ECO:0000269|PubMed:22334370}. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- DISEASE: Leber congenital amaurosis 8 (LCA8) [MIM:613835]: A CC severe dystrophy of the retina, typically becoming evident in the CC first years of life. Visual function is usually poor and often CC accompanied by nystagmus, sluggish or near-absent pupillary CC responses, photophobia, high hyperopia and keratoconus. CC {ECO:0000269|PubMed:11231775, ECO:0000269|PubMed:11389483, CC ECO:0000269|PubMed:12567265, ECO:0000269|PubMed:12573663, CC ECO:0000269|PubMed:12700176, ECO:0000269|PubMed:15024725, CC ECO:0000269|PubMed:15691574, ECO:0000269|PubMed:16205573, CC ECO:0000269|PubMed:16936081, ECO:0000269|PubMed:17128490, CC ECO:0000269|PubMed:17438615, ECO:0000269|PubMed:17724218, CC ECO:0000269|PubMed:18055821, ECO:0000269|PubMed:18682808, CC ECO:0000269|PubMed:20108431, ECO:0000269|PubMed:20956273, CC ECO:0000269|PubMed:21602930}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- DISEASE: Pigmented paravenous chorioretinal atrophy (PPCRA) CC [MIM:172870]: Unusual retinal degeneration characterized by CC accumulation of pigmentation along retinal veins. PPCRA is CC dominantly inherited, but exhibited variable expressivity. Males CC are more likely to exhibit a severe phenotype, whereas females may CC remain virtually asymptomatic even in later years. The PPCRA CC phenotype is associated with a mutation in CRB1 gene which is CC likely to affect the structure of the CRB1 protein. CC {ECO:0000269|PubMed:15623792}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the Crumbs protein family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAE45845.1; Type=Erroneous termination; Positions=567; Note=Translated as Trp.; Evidence={ECO:0000305}; CC Sequence=CAI16644.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Mutations of the CRB1 gene; Note=Retina CC International's Scientific Newsletter; CC URL="http://www.retina-international.org/files/sci-news/crb1mut.htm"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF154671; AAF01361.1; -; mRNA. DR EMBL; AY043323; AAL10680.1; -; mRNA. DR EMBL; AY043324; AAL10681.1; -; mRNA. DR EMBL; AY043325; AAL10682.1; -; mRNA. DR EMBL; AJ748821; CAG38658.1; -; mRNA. DR EMBL; BX640729; CAE45845.1; ALT_SEQ; mRNA. DR EMBL; AK299368; BAH13018.1; -; mRNA. DR EMBL; AL513325; CAH72584.1; -; Genomic_DNA. DR EMBL; AL136322; CAH72584.1; JOINED; Genomic_DNA. DR EMBL; AL139136; CAH72584.1; JOINED; Genomic_DNA. DR EMBL; AL139136; CAI15310.1; -; Genomic_DNA. DR EMBL; AL136322; CAI15310.1; JOINED; Genomic_DNA. DR EMBL; AL139136; CAI15311.1; -; Genomic_DNA. DR EMBL; AL513325; CAI15311.1; JOINED; Genomic_DNA. DR EMBL; AL136322; CAI15311.1; JOINED; Genomic_DNA. DR EMBL; AL136322; CAI16644.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL136322; CAI16645.1; -; Genomic_DNA. DR EMBL; AL139136; CAI16645.1; JOINED; Genomic_DNA. DR EMBL; AL136322; CAI16646.1; -; Genomic_DNA. DR EMBL; AL513325; CAI16646.1; JOINED; Genomic_DNA. DR EMBL; AL139136; CAI16646.1; JOINED; Genomic_DNA. DR EMBL; AL513325; CAM17208.1; -; Genomic_DNA. DR EMBL; AL136322; CAM17208.1; JOINED; Genomic_DNA. DR EMBL; AL139136; CAM17208.1; JOINED; Genomic_DNA. DR EMBL; AL139136; CAM21656.1; -; Genomic_DNA. DR EMBL; AL136322; CAM21656.1; JOINED; Genomic_DNA. DR EMBL; AL513325; CAM21656.1; JOINED; Genomic_DNA. DR EMBL; AL136322; CAM23328.1; -; Genomic_DNA. DR EMBL; AL139136; CAM23328.1; JOINED; Genomic_DNA. DR EMBL; AL513325; CAM23328.1; JOINED; Genomic_DNA. DR EMBL; AL356315; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471067; EAW91277.1; -; Genomic_DNA. DR EMBL; BC136271; AAI36272.1; -; mRNA. DR CCDS; CCDS1390.1; -. [P82279-1] DR CCDS; CCDS53454.1; -. [P82279-3] DR CCDS; CCDS58052.1; -. [P82279-5] DR RefSeq; NP_001180569.1; NM_001193640.1. [P82279-3] DR RefSeq; NP_001244894.1; NM_001257965.1. DR RefSeq; NP_001244895.1; NM_001257966.1. [P82279-5] DR RefSeq; NP_957705.1; NM_201253.2. [P82279-1] DR UniGene; Hs.126135; -. DR PDB; 4UU5; X-ray; 1.23 A; B=1390-1406. DR PDBsum; 4UU5; -. DR ProteinModelPortal; P82279; -. DR SMR; P82279; -. DR BioGrid; 116990; 3. DR CORUM; P82279; -. DR IntAct; P82279; 3. DR MINT; MINT-1774304; -. DR STRING; 9606.ENSP00000356370; -. DR iPTMnet; P82279; -. DR PhosphoSitePlus; P82279; -. DR BioMuta; CRB1; -. DR DMDM; 71153499; -. DR MaxQB; P82279; -. DR PaxDb; P82279; -. DR PeptideAtlas; P82279; -. DR PRIDE; P82279; -. DR Ensembl; ENST00000367399; ENSP00000356369; ENSG00000134376. [P82279-3] DR Ensembl; ENST00000367400; ENSP00000356370; ENSG00000134376. [P82279-1] DR Ensembl; ENST00000484075; ENSP00000433932; ENSG00000134376. [P82279-2] DR Ensembl; ENST00000538660; ENSP00000438091; ENSG00000134376. [P82279-5] DR Ensembl; ENST00000638467; ENSP00000491102; ENSG00000134376. [P82279-2] DR GeneID; 23418; -. DR KEGG; hsa:23418; -. DR UCSC; uc001gtz.4; human. [P82279-1] DR CTD; 23418; -. DR DisGeNET; 23418; -. DR EuPathDB; HostDB:ENSG00000134376.14; -. DR GeneCards; CRB1; -. DR GeneReviews; CRB1; -. DR HGNC; HGNC:2343; CRB1. DR HPA; HPA061250; -. DR HPA; HPA063127; -. DR MalaCards; CRB1; -. DR MIM; 172870; phenotype. DR MIM; 268000; phenotype. DR MIM; 600105; phenotype. DR MIM; 604210; gene. DR MIM; 613835; phenotype. DR neXtProt; NX_P82279; -. DR OpenTargets; ENSG00000134376; -. DR Orphanet; 65; Leber congenital amaurosis. DR Orphanet; 251295; Pigmented paravenous retinochoroidal atrophy. DR Orphanet; 791; Retinitis pigmentosa. DR PharmGKB; PA26863; -. DR eggNOG; ENOG410IR70; Eukaryota. DR eggNOG; ENOG411193Y; LUCA. DR GeneTree; ENSGT00810000125346; -. DR HOVERGEN; HBG080001; -. DR InParanoid; P82279; -. DR KO; K16681; -. DR OMA; WDDFSCS; -. DR OrthoDB; EOG091G00H8; -. DR PhylomeDB; P82279; -. DR TreeFam; TF316224; -. DR GeneWiki; CRB1; -. DR GenomeRNAi; 23418; -. DR PRO; PR:P82279; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000134376; -. DR CleanEx; HS_CRB1; -. DR ExpressionAtlas; P82279; baseline and differential. DR Genevisible; P82279; HS. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005902; C:microvillus; IEA:Ensembl. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc. DR GO; GO:0007163; P:establishment or maintenance of cell polarity; TAS:ProtInc. DR GO; GO:0042462; P:eye photoreceptor cell development; IEA:Ensembl. DR GO; GO:0007009; P:plasma membrane organization; IEA:Ensembl. DR GO; GO:0006611; P:protein export from nucleus; IC:ParkinsonsUK-UCL. DR InterPro; IPR013320; ConA-like_dom. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site. DR InterPro; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR009030; Growth_fac_rcpt_. DR InterPro; IPR001791; Laminin_G. DR Pfam; PF00008; EGF; 13. DR Pfam; PF12661; hEGF; 3. DR Pfam; PF02210; Laminin_G_2; 3. DR SMART; SM00181; EGF; 18. DR SMART; SM00179; EGF_CA; 16. DR SMART; SM00282; LamG; 3. DR SUPFAM; SSF49899; SSF49899; 3. DR SUPFAM; SSF57184; SSF57184; 2. DR PROSITE; PS00010; ASX_HYDROXYL; 10. DR PROSITE; PS00022; EGF_1; 15. DR PROSITE; PS01186; EGF_2; 11. DR PROSITE; PS50026; EGF_3; 19. DR PROSITE; PS01187; EGF_CA; 7. DR PROSITE; PS50025; LAM_G_DOMAIN; 3. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Cell membrane; KW Complete proteome; Disease mutation; Disulfide bond; EGF-like domain; KW Glycoprotein; Leber congenital amaurosis; Membrane; Polymorphism; KW Reference proteome; Repeat; Retinitis pigmentosa; Secreted; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 25 {ECO:0000255}. FT CHAIN 26 1406 Protein crumbs homolog 1. FT /FTId=PRO_0000007500. FT TOPO_DOM 26 1347 Extracellular. {ECO:0000255}. FT TRANSMEM 1348 1368 Helical. {ECO:0000255}. FT TOPO_DOM 1369 1406 Cytoplasmic. {ECO:0000255}. FT DOMAIN 30 68 EGF-like 1. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 70 108 EGF-like 2. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 110 146 EGF-like 3. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 148 184 EGF-like 4; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 186 222 EGF-like 5; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 224 260 EGF-like 6; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 262 299 EGF-like 7; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 301 337 EGF-like 8. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 339 395 EGF-like 9. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 397 439 EGF-like 10; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 441 481 EGF-like 11. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 485 670 Laminin G-like 1. {ECO:0000255|PROSITE- FT ProRule:PRU00122}. FT DOMAIN 672 708 EGF-like 12. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 714 885 Laminin G-like 2. {ECO:0000255|PROSITE- FT ProRule:PRU00122}. FT DOMAIN 887 923 EGF-like 13. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 924 960 EGF-like 14. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 950 1137 Laminin G-like 3. {ECO:0000255|PROSITE- FT ProRule:PRU00122}. FT DOMAIN 1139 1175 EGF-like 15. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 1177 1212 EGF-like 16; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 1214 1250 EGF-like 17. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 1255 1295 EGF-like 18. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 1297 1333 EGF-like 19; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT CARBOHYD 30 30 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 41 41 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 42 42 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 215 215 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 287 287 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 313 313 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 322 322 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 418 418 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 427 427 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 453 453 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 550 550 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 561 561 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 657 657 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 757 757 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 871 871 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 880 880 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 968 968 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 975 975 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1000 1000 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1190 1190 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1243 1243 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1265 1265 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1273 1273 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 34 45 {ECO:0000250}. FT DISULFID 39 54 {ECO:0000250}. FT DISULFID 56 67 {ECO:0000250}. FT DISULFID 74 85 {ECO:0000250}. FT DISULFID 79 96 {ECO:0000250}. FT DISULFID 98 107 {ECO:0000250}. FT DISULFID 114 125 {ECO:0000250}. FT DISULFID 119 134 {ECO:0000250}. FT DISULFID 136 145 {ECO:0000250}. FT DISULFID 152 163 {ECO:0000250}. FT DISULFID 157 172 {ECO:0000250}. FT DISULFID 174 183 {ECO:0000250}. FT DISULFID 190 201 {ECO:0000250}. FT DISULFID 195 210 {ECO:0000250}. FT DISULFID 212 221 {ECO:0000250}. FT DISULFID 228 239 {ECO:0000250}. FT DISULFID 233 248 {ECO:0000250}. FT DISULFID 250 259 {ECO:0000250}. FT DISULFID 266 277 {ECO:0000250}. FT DISULFID 271 286 {ECO:0000250}. FT DISULFID 288 298 {ECO:0000250}. FT DISULFID 305 316 {ECO:0000250}. FT DISULFID 310 325 {ECO:0000250}. FT DISULFID 327 336 {ECO:0000250}. FT DISULFID 343 354 {ECO:0000250}. FT DISULFID 348 383 {ECO:0000250}. FT DISULFID 385 394 {ECO:0000250}. FT DISULFID 401 412 {ECO:0000250}. FT DISULFID 406 421 {ECO:0000250}. FT DISULFID 423 438 {ECO:0000250}. FT DISULFID 445 456 {ECO:0000250}. FT DISULFID 450 469 {ECO:0000250}. FT DISULFID 471 480 {ECO:0000250}. FT DISULFID 642 670 {ECO:0000250}. FT DISULFID 676 687 {ECO:0000250}. FT DISULFID 681 696 {ECO:0000250}. FT DISULFID 698 707 {ECO:0000250}. FT DISULFID 851 885 {ECO:0000250}. FT DISULFID 891 902 {ECO:0000250}. FT DISULFID 896 911 {ECO:0000250}. FT DISULFID 913 922 {ECO:0000250}. FT DISULFID 928 939 {ECO:0000250}. FT DISULFID 933 948 {ECO:0000250}. FT DISULFID 1096 1137 {ECO:0000250}. FT DISULFID 1143 1154 {ECO:0000250}. FT DISULFID 1148 1163 {ECO:0000250}. FT DISULFID 1165 1174 {ECO:0000250}. FT DISULFID 1181 1191 {ECO:0000250}. FT DISULFID 1186 1200 {ECO:0000250}. FT DISULFID 1202 1211 {ECO:0000250}. FT DISULFID 1218 1229 {ECO:0000250}. FT DISULFID 1223 1238 {ECO:0000250}. FT DISULFID 1240 1249 {ECO:0000250}. FT DISULFID 1259 1274 {ECO:0000250}. FT DISULFID 1268 1283 {ECO:0000250}. FT DISULFID 1285 1294 {ECO:0000250}. FT DISULFID 1301 1312 {ECO:0000250}. FT DISULFID 1306 1321 {ECO:0000250}. FT DISULFID 1323 1332 {ECO:0000250}. FT VAR_SEQ 1 351 Missing (in isoform 4). FT {ECO:0000303|PubMed:17974005}. FT /FTId=VSP_014724. FT VAR_SEQ 218 329 Missing (in isoform 3). FT {ECO:0000303|PubMed:15914641}. FT /FTId=VSP_014725. FT VAR_SEQ 352 390 GECVELSSEKQYGRITGLPSSFSYHEASGYVCICQPGFT FT -> MIRNSLCQPSRCLDEYLFFNRKMFGARTHGFHILMAML FT I (in isoform 4). FT {ECO:0000303|PubMed:17974005}. FT /FTId=VSP_014726. FT VAR_SEQ 710 1245 Missing (in isoform 5). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_045332. FT VAR_SEQ 1294 1406 Missing (in isoform 4). FT {ECO:0000303|PubMed:17974005}. FT /FTId=VSP_014727. FT VAR_SEQ 1336 1376 LADDLISDIFTTIGSVTVALLLILLLAIVASVVTSNKRATQ FT -> VSSLSFYVSLLFWQNLFQLLSYLILRMNDEPVVEWGEQ FT EDY (in isoform 2). FT {ECO:0000303|PubMed:10508521, FT ECO:0000303|PubMed:11734541}. FT /FTId=VSP_014728. FT VAR_SEQ 1377 1406 Missing (in isoform 2). FT {ECO:0000303|PubMed:10508521, FT ECO:0000303|PubMed:11734541}. FT /FTId=VSP_014729. FT VARIANT 27 27 C -> F (in RP12). FT {ECO:0000269|PubMed:19956407}. FT /FTId=VAR_064180. FT VARIANT 45 45 C -> W (in RP12; dbSNP:rs145141811). FT {ECO:0000269|PubMed:20591486}. FT /FTId=VAR_067125. FT VARIANT 144 144 F -> V (in LCA8; dbSNP:rs62636262). FT {ECO:0000269|PubMed:11231775}. FT /FTId=VAR_022941. FT VARIANT 157 157 C -> S (in RP12). FT {ECO:0000269|PubMed:20956273}. FT /FTId=VAR_067126. FT VARIANT 161 161 A -> V (in RP12; dbSNP:rs62635651). FT {ECO:0000269|PubMed:10508521}. FT /FTId=VAR_011641. FT VARIANT 162 162 V -> M (in PPCRA; dbSNP:rs137853138). FT {ECO:0000269|PubMed:15623792}. FT /FTId=VAR_022942. FT VARIANT 165 167 Missing (in RP12). FT /FTId=VAR_067127. FT VARIANT 195 195 C -> F (in RP12; dbSNP:rs764256655). FT {ECO:0000269|PubMed:15459956}. FT /FTId=VAR_022943. FT VARIANT 205 205 I -> T (found in patients with Leber FT congenital amaurosis; unknown FT pathological significance; FT dbSNP:rs62645749). FT {ECO:0000269|PubMed:12843338, FT ECO:0000269|PubMed:15459956, FT ECO:0000269|PubMed:20956273}. FT /FTId=VAR_022944. FT VARIANT 222 222 E -> K (in dbSNP:rs114846212). FT {ECO:0000269|PubMed:21602930}. FT /FTId=VAR_067128. FT VARIANT 250 250 C -> W (in RP12; dbSNP:rs62635652). FT {ECO:0000269|PubMed:10508521, FT ECO:0000269|PubMed:20956273}. FT /FTId=VAR_011642. FT VARIANT 289 289 T -> M (rare variant found in patients FT with retinal dystrophy; does not FT segregate with the disease in a family; FT unlikely to be pathogenic; FT dbSNP:rs62636263). FT {ECO:0000269|PubMed:11231775, FT ECO:0000269|PubMed:11389483, FT ECO:0000269|PubMed:12843338, FT ECO:0000269|PubMed:17724218, FT ECO:0000269|PubMed:21602930}. FT /FTId=VAR_022945. FT VARIANT 310 310 C -> Y (probable disease-associated FT mutation found in patients with early- FT onset retinal dystrophy; FT dbSNP:rs779835125). FT {ECO:0000269|PubMed:20683928}. FT /FTId=VAR_067129. FT VARIANT 312 312 N -> K (in RP12). FT {ECO:0000269|PubMed:20956273}. FT /FTId=VAR_067130. FT VARIANT 333 333 G -> D (in LCA8; dbSNP:rs587783015). FT {ECO:0000269|PubMed:18682808}. FT /FTId=VAR_067131. FT VARIANT 383 383 C -> Y (in LCA8; dbSNP:rs62645754). FT {ECO:0000269|PubMed:11231775}. FT /FTId=VAR_022946. FT VARIANT 433 433 Y -> C (in RP12; dbSNP:rs62636288). FT {ECO:0000269|PubMed:11389483}. FT /FTId=VAR_022947. FT VARIANT 438 438 C -> Y (in LCA8). FT {ECO:0000269|PubMed:17724218}. FT /FTId=VAR_067132. FT VARIANT 454 454 G -> R (in LCA8). FT {ECO:0000269|PubMed:16936081}. FT /FTId=VAR_067133. FT VARIANT 480 480 C -> G (in LCA8). FT {ECO:0000269|PubMed:11231775}. FT /FTId=VAR_022948. FT VARIANT 480 480 C -> R (in LCA8; dbSNP:rs62636264). FT {ECO:0000269|PubMed:11231775, FT ECO:0000269|PubMed:16205573}. FT /FTId=VAR_022949. FT VARIANT 488 488 F -> S (in dbSNP:rs777377174). FT {ECO:0000269|PubMed:16205573}. FT /FTId=VAR_067134. FT VARIANT 491 491 D -> V (found in a patient with early- FT onset retinal dystrophy; unknown FT pathological significance). FT {ECO:0000269|PubMed:20683928}. FT /FTId=VAR_067135. FT VARIANT 534 534 K -> N (in RP12). FT {ECO:0000269|PubMed:22334370}. FT /FTId=VAR_068363. FT VARIANT 535 535 L -> P (in LCA8; dbSNP:rs113082791). FT {ECO:0000269|PubMed:17438615}. FT /FTId=VAR_067136. FT VARIANT 564 564 D -> Y (in LCA8). FT {ECO:0000269|PubMed:17128490}. FT /FTId=VAR_067137. FT VARIANT 578 578 V -> E (in RP12). FT {ECO:0000269|PubMed:15459956}. FT /FTId=VAR_022950. FT VARIANT 584 584 D -> Y (in LCA8). FT {ECO:0000269|PubMed:15024725, FT ECO:0000269|PubMed:22065545}. FT /FTId=VAR_022951. FT VARIANT 587 587 C -> Y (in RP12). FT {ECO:0000269|PubMed:15459956}. FT /FTId=VAR_022952. FT VARIANT 635 635 S -> P (found in a patient with Leber FT congenital amaurosis; unknown FT pathological significance). FT {ECO:0000269|PubMed:21602930}. FT /FTId=VAR_067138. FT VARIANT 675 675 W -> C (in RP12). FT {ECO:0000269|PubMed:20956273}. FT /FTId=VAR_067139. FT VARIANT 679 679 Q -> E (in dbSNP:rs62636286). FT {ECO:0000269|PubMed:12843338}. FT /FTId=VAR_022953. FT VARIANT 681 681 C -> Y (in LCA8; dbSNP:rs62636266). FT {ECO:0000269|PubMed:11231775, FT ECO:0000269|PubMed:16205573}. FT /FTId=VAR_022954. FT VARIANT 710 710 E -> Q (in LCA8; dbSNP:rs62645755). FT {ECO:0000269|PubMed:15024725}. FT /FTId=VAR_022955. FT VARIANT 710 710 E -> V (in RP12; dbSNP:rs145282040). FT {ECO:0000269|PubMed:20591486, FT ECO:0000269|PubMed:20956273}. FT /FTId=VAR_067140. FT VARIANT 740 740 S -> F (in RP12). FT {ECO:0000269|PubMed:22065545}. FT /FTId=VAR_067141. FT VARIANT 741 741 M -> T (in LCA8; also found in patients FT with early-onset rod-cone retinal FT dystrophy; dbSNP:rs62636267). FT {ECO:0000269|PubMed:15024725, FT ECO:0000269|PubMed:20956273, FT ECO:0000269|PubMed:21602930, FT ECO:0000269|PubMed:22065545}. FT /FTId=VAR_022956. FT VARIANT 745 745 T -> M (in RP12 and LCA8; FT dbSNP:rs28939720). FT {ECO:0000269|PubMed:10508521, FT ECO:0000269|PubMed:15024725, FT ECO:0000269|PubMed:15459956, FT ECO:0000269|PubMed:16959974, FT ECO:0000269|PubMed:17724218, FT ECO:0000269|PubMed:20591486, FT ECO:0000269|PubMed:20956273, FT ECO:0000269|PubMed:22334370}. FT /FTId=VAR_011643. FT VARIANT 749 749 Missing (in RP12 and LCA8). FT {ECO:0000269|PubMed:12700176, FT ECO:0000269|PubMed:12843338}. FT /FTId=VAR_022957. FT VARIANT 753 753 L -> P (in LCA8). FT {ECO:0000269|PubMed:15691574, FT ECO:0000269|PubMed:16205573}. FT /FTId=VAR_067142. FT VARIANT 764 764 R -> C (in RP12 and LCA8; FT dbSNP:rs62635654). FT {ECO:0000269|PubMed:10508521, FT ECO:0000269|PubMed:11231775, FT ECO:0000269|PubMed:11389483, FT ECO:0000269|PubMed:12700176, FT ECO:0000269|PubMed:15024725, FT ECO:0000269|PubMed:15459956, FT ECO:0000269|PubMed:15691574, FT ECO:0000269|PubMed:16205573, FT ECO:0000269|PubMed:20683928, FT ECO:0000269|PubMed:20956273}. FT /FTId=VAR_011644. FT VARIANT 769 769 R -> H (in dbSNP:rs62636287). FT {ECO:0000269|PubMed:12843338, FT ECO:0000269|PubMed:18682808, FT ECO:0000269|PubMed:20591486}. FT /FTId=VAR_022958. FT VARIANT 769 769 R -> Q. {ECO:0000269|PubMed:11231775}. FT /FTId=VAR_022959. FT VARIANT 789 789 Missing (in early-onset retinal FT dystrophy; probable disease-associated FT mutation). {ECO:0000269|PubMed:22065545}. FT /FTId=VAR_067143. FT VARIANT 821 821 T -> M (in dbSNP:rs142857810). FT {ECO:0000269|PubMed:11389483}. FT /FTId=VAR_067144. FT VARIANT 836 836 P -> T (in RP12; dbSNP:rs116471343). FT {ECO:0000269|PubMed:15459956, FT ECO:0000269|PubMed:20956273, FT ECO:0000269|PubMed:22065545}. FT /FTId=VAR_022960. FT VARIANT 837 837 D -> H (in RP12; located on the same FT allele as T-1354; dbSNP:rs62636289). FT {ECO:0000269|PubMed:11389483}. FT /FTId=VAR_022961. FT VARIANT 846 846 G -> R (in RP12; dbSNP:rs539189291). FT {ECO:0000269|PubMed:12573663, FT ECO:0000269|PubMed:20956273}. FT /FTId=VAR_022962. FT VARIANT 850 850 G -> S (in RP12 and LCA8; FT dbSNP:rs776591659). FT {ECO:0000269|PubMed:15459956, FT ECO:0000269|PubMed:20591486, FT ECO:0000269|PubMed:20956273}. FT /FTId=VAR_022963. FT VARIANT 852 852 I -> T (in LCA8; dbSNP:rs62636271). FT {ECO:0000269|PubMed:15024725, FT ECO:0000269|PubMed:17724218}. FT /FTId=VAR_022964. FT VARIANT 891 891 C -> G (in RP12; without preservation of FT the paraarteriolar retinal pigment FT epithelium; dbSNP:rs62635658). FT {ECO:0000269|PubMed:12843338}. FT /FTId=VAR_022965. FT VARIANT 894 894 N -> S (in RP12; dbSNP:rs62636290). FT {ECO:0000269|PubMed:11389483}. FT /FTId=VAR_022966. FT VARIANT 901 901 V -> I (found in a patient with RP12; FT unknown pathological significance). FT {ECO:0000269|PubMed:20591486}. FT /FTId=VAR_067145. FT VARIANT 905 905 R -> Q (in dbSNP:rs114052315). FT {ECO:0000269|PubMed:15459956}. FT /FTId=VAR_022967. FT VARIANT 937 937 A -> T (found in a patient with Leber FT congenital amaurosis; unknown FT pathological significance; FT dbSNP:rs114630940). FT {ECO:0000269|PubMed:18682808}. FT /FTId=VAR_067146. FT VARIANT 939 939 C -> Y (in LCA8). FT {ECO:0000269|PubMed:18055821}. FT /FTId=VAR_067147. FT VARIANT 948 948 C -> Y (in RP12 and LCA8; without FT preservation of the paraarteriolar FT retinal pigment epithelium; FT dbSNP:rs62645748). FT {ECO:0000269|PubMed:10508521, FT ECO:0000269|PubMed:11231775, FT ECO:0000269|PubMed:11389483, FT ECO:0000269|PubMed:12700176, FT ECO:0000269|PubMed:12843338, FT ECO:0000269|PubMed:15024725, FT ECO:0000269|PubMed:15459956, FT ECO:0000269|PubMed:15691574, FT ECO:0000269|PubMed:16205573, FT ECO:0000269|PubMed:18055821, FT ECO:0000269|PubMed:20591486, FT ECO:0000269|PubMed:20683928, FT ECO:0000269|PubMed:20956273, FT ECO:0000269|PubMed:22065545}. FT /FTId=VAR_011645. FT VARIANT 959 959 G -> S (found in a patient with RP12; FT unknown pathological significance; FT dbSNP:rs557111131). FT {ECO:0000269|PubMed:15459956}. FT /FTId=VAR_022968. FT VARIANT 962 962 Missing (in RP12; without preservation of FT the paraarteriolar retinal pigment FT epithelium). FT {ECO:0000269|PubMed:12843338}. FT /FTId=VAR_022969. FT VARIANT 986 986 N -> I (in RP12). FT {ECO:0000269|PubMed:15459956}. FT /FTId=VAR_022970. FT VARIANT 989 989 I -> T (in LCA8). FT {ECO:0000269|PubMed:12573663}. FT /FTId=VAR_022971. FT VARIANT 1003 1003 I -> T (in LCA8). FT {ECO:0000269|PubMed:20956273}. FT /FTId=VAR_067148. FT VARIANT 1012 1012 L -> S (in RP12). FT {ECO:0000269|PubMed:20956273}. FT /FTId=VAR_067149. FT VARIANT 1025 1025 S -> I (in LCA8; dbSNP:rs62636274). FT {ECO:0000269|PubMed:15024725}. FT /FTId=VAR_022972. FT VARIANT 1025 1025 S -> N (in RP12). FT {ECO:0000269|PubMed:20956273}. FT /FTId=VAR_067150. FT VARIANT 1041 1041 M -> T (in RP12; dbSNP:rs62635656). FT {ECO:0000269|PubMed:10508521}. FT /FTId=VAR_011646. FT VARIANT 1071 1071 L -> P (in RP12; dbSNP:rs62635657). FT {ECO:0000269|PubMed:10508521, FT ECO:0000269|PubMed:12573663}. FT /FTId=VAR_011647. FT VARIANT 1099 1099 T -> K (in RP12). FT {ECO:0000269|PubMed:21987686}. FT /FTId=VAR_067151. FT VARIANT 1100 1100 I -> R (in LCA8; dbSNP:rs62635659). FT {ECO:0000269|PubMed:11389483}. FT /FTId=VAR_011648. FT VARIANT 1100 1100 I -> T (in RP12; dbSNP:rs62635659). FT {ECO:0000269|PubMed:12843338, FT ECO:0000269|PubMed:15459956}. FT /FTId=VAR_022973. FT VARIANT 1103 1103 G -> R (in LCA8 and RP12; FT dbSNP:rs62636275). FT {ECO:0000269|PubMed:15024725, FT ECO:0000269|PubMed:17724218, FT ECO:0000269|PubMed:19140180, FT ECO:0000269|PubMed:20956273, FT ECO:0000269|PubMed:22065545}. FT /FTId=VAR_022974. FT VARIANT 1107 1107 L -> P (in LCA8; dbSNP:rs62636276). FT {ECO:0000269|PubMed:15024725, FT ECO:0000269|PubMed:20956273}. FT /FTId=VAR_022975. FT VARIANT 1107 1107 L -> R (in LCA8; dbSNP:rs62636276). FT {ECO:0000269|PubMed:15024725}. FT /FTId=VAR_022976. FT VARIANT 1161 1161 Y -> C (in LCA8). FT {ECO:0000269|PubMed:20108431}. FT /FTId=VAR_067152. FT VARIANT 1165 1165 C -> W (in RP12). FT {ECO:0000269|PubMed:19956407}. FT /FTId=VAR_064181. FT VARIANT 1174 1174 C -> G (in LCA8 and RP12). FT {ECO:0000269|PubMed:20956273}. FT /FTId=VAR_067153. FT VARIANT 1181 1181 C -> R (in RP12; dbSNP:rs62636291). FT {ECO:0000269|PubMed:11389483}. FT /FTId=VAR_011649. FT VARIANT 1198 1198 Y -> C (probable disease-associated FT mutation found in patients with early- FT onset retinal dystrophy). FT {ECO:0000269|PubMed:22065545}. FT /FTId=VAR_067154. FT VARIANT 1205 1205 G -> R (in LCA8; dbSNP:rs574742644). FT {ECO:0000269|PubMed:11231775}. FT /FTId=VAR_022977. FT VARIANT 1218 1218 C -> F (in LCA8). FT {ECO:0000269|PubMed:12700176}. FT /FTId=VAR_022978. FT VARIANT 1223 1223 C -> S (probable disease-associated FT mutation found in patients with early- FT onset retinal dystrophy). FT {ECO:0000269|PubMed:22065545}. FT /FTId=VAR_067155. FT VARIANT 1305 1305 P -> L (in RP12). FT {ECO:0000269|PubMed:22128245}. FT /FTId=VAR_067156. FT VARIANT 1317 1317 N -> H (in LCA8; dbSNP:rs62636281). FT {ECO:0000269|PubMed:11231775}. FT /FTId=VAR_022979. FT VARIANT 1321 1321 C -> S (in LCA8; also early onset RP FT without preservation of the FT paraarteriolar retinal pigment FT epithelium; dbSNP:rs62635649). FT {ECO:0000269|PubMed:11559858, FT ECO:0000269|PubMed:15024725}. FT /FTId=VAR_022980. FT VARIANT 1331 1331 R -> H (in dbSNP:rs62636285). FT {ECO:0000269|PubMed:11231775, FT ECO:0000269|PubMed:11389483, FT ECO:0000269|PubMed:12843338}. FT /FTId=VAR_022981. FT VARIANT 1332 1332 C -> F (in LCA8; dbSNP:rs377543137). FT {ECO:0000269|PubMed:18055821}. FT /FTId=VAR_067157. FT VARIANT 1354 1354 A -> T (found in a patient with RP12; FT located on the same allele as H-837; FT dbSNP:rs200469148). FT {ECO:0000269|PubMed:11389483}. FT /FTId=VAR_022982. FT VARIANT 1365 1365 A -> D (probable disease-associated FT mutation found in patients with early- FT onset retinal dystrophy). FT {ECO:0000269|PubMed:20956273}. FT /FTId=VAR_067158. FT VARIANT 1381 1381 P -> L (in LCA8). FT {ECO:0000269|PubMed:20956273}. FT /FTId=VAR_067159. FT VARIANT 1383 1383 R -> H (in RP12; dbSNP:rs200573274). FT {ECO:0000269|PubMed:15459956, FT ECO:0000269|PubMed:20591486}. FT /FTId=VAR_022983. FT TURN 1394 1396 {ECO:0000244|PDB:4UU5}. FT STRAND 1403 1406 {ECO:0000244|PDB:4UU5}. SQ SEQUENCE 1406 AA; 154183 MW; F2D04D20FAA6E37D CRC64; MALKNINYLL IFYLSFSLLI YIKNSFCNKN NTRCLSNSCQ NNSTCKDFSK DNDCSCSDTA NNLDKDCDNM KDPCFSNPCQ GSATCVNTPG ERSFLCKCPP GYSGTICETT IGSCGKNSCQ HGGICHQDPI YPVCICPAGY AGRFCEIDHD ECASSPCQNG AVCQDGIDGY SCFCVPGYQG RHCDLEVDEC ASDPCKNEAT CLNEIGRYTC ICPHNYSGVN CELEIDECWS QPCLNGATCQ DALGAYFCDC APGFLGDHCE LNTDECASQP CLHGGLCVDG ENRYSCNCTG SGFTGTHCET LMPLCWSKPC HNNATCEDSV DNYTCHCWPG YTGAQCEIDL NECNSNPCQS NGECVELSSE KQYGRITGLP SSFSYHEASG YVCICQPGFT GIHCEEDVNE CSSNPCQNGG TCENLPGNYT CHCPFDNLSR TFYGGRDCSD ILLGCTHQQC LNNGTCIPHF QDGQHGFSCL CPSGYTGSLC EIATTLSFEG DGFLWVKSGS VTTKGSVCNI ALRFQTVQPM ALLLFRSNRD VFVKLELLSG YIHLSIQVNN QSKVLLFISH NTSDGEWHFV EVIFAEAVTL TLIDDSCKEK CIAKAPTPLE SDQSICAFQN SFLGGLPVGM TSNGVALLNF YNMPSTPSFV GCLQDIKIDW NHITLENISS GSSLNVKAGC VRKDWCESQP CQSRGRCINL WLSYQCDCHR PYEGPNCLRE YVAGRFGQDD STGYVIFTLD ESYGDTISLS MFVRTLQPSG LLLALENSTY QYIRVWLERG RLAMLTPNSP KLVVKFVLND GNVHLISLKI KPYKIELYQS SQNLGFISAS TWKIEKGDVI YIGGLPDKQE TELNGGFFKG CIQDVRLNNQ NLEFFPNPTN NASLNPVLVN VTQGCAGDNS CKSNPCHNGG VCHSRWDDFS CSCPALTSGK ACEEVQWCGF SPCPHGAQCQ PVLQGFECIA NAVFNGQSGQ ILFRSNGNIT RELTNITFGF RTRDANVIIL HAEKEPEFLN ISIQDSRLFF QLQSGNSFYM LSLTSLQSVN DGTWHEVTLS MTDPLSQTSR WQMEVDNETP FVTSTIATGS LNFLKDNTDI YVGDRAIDNI KGLQGCLSTI EIGGIYLSYF ENVHGFINKP QEEQFLKIST NSVVTGCLQL NVCNSNPCLH GGNCEDIYSS YHCSCPLGWS GKHCELNIDE CFSNPCIHGN CSDRVAAYHC TCEPGYTGVN CEVDIDNCQS HQCANGATCI SHTNGYSCLC FGNFTGKFCR QSRLPSTVCG NEKTNLTCYN GGNCTEFQTE LKCMCRPGFT GEWCEKDIDE CASDPCVNGG LCQDLLNKFQ CLCDVAFAGE RCEVDLADDL ISDIFTTIGS VTVALLLILL LAIVASVVTS NKRATQGTYS PSRQEKEGSR VEMWNLMPPP AMERLI //