ID AIPL1_HUMAN Reviewed; 384 AA. AC Q9NZN9; D3DTM4; Q659W3; Q659W4; Q6ZZB6; Q8N6A0; Q9H873; Q9NS10; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 19-SEP-2002, sequence version 2. DT 28-JAN-2026, entry version 207. DE RecName: Full=Aryl-hydrocarbon-interacting protein-like 1; GN Name=AIPL1; Synonyms=AIPL2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC DNA] RP (ISOFORM 1), VARIANT HIS-90, AND VARIANT LCA4 ARG-239. RX PubMed=10615133; DOI=10.1038/71732; RA Sohocki M.M., Bowne S.J., Sullivan L.S., Blackshaw S., Cepko C.L., RA Payne A.M., Bhattacharya S.S., Khaliq S., Mehdi Q., Birch D.G., RA Harrison W.R., Elder F.F.B., Heckenlively J.R., Daiger S.P.; RT "Mutations in a novel photoreceptor-pineal gene on 17p cause Leber RT congenital amaurosis."; RL Nat. Genet. 24:79-83(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Retinoblastoma; RA Guo J.H., Zhou G.J., Yu L.; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4 AND 5). RC TISSUE=Retina; RA Janke B., Preising M., Lorenz B.; RT "Alternative splicing in AIPL1: Implications on function and the mutational RT spectrum."; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RC TISSUE=Retinoblastoma; RA Kato S.; RT "Full-length cDNA derived from human retinoblastoma cell line Y79."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Eye; 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP INTERACTION WITH NUB1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP MUTAGENESIS OF ARG-53; MET-79; VAL-96; ALA-197; ILE-206 AND GLY-262, RP CHARACTERIZATION OF VARIANT LEU-302, AND CHARACTERIZATION OF VARIANT LCA4 RP ARG-239. RC TISSUE=Retina; RX PubMed=12374762; DOI=10.1093/hmg/11.22.2723; RA Akey D.T., Zhu X., Dyer M., Li A., Sorensen A., Blackshaw S., RA Fukuda-Kamitani T., Daiger S.P., Craft C.M., Kamitani T., Sohocki M.M.; RT "The inherited blindness associated protein AIPL1 interacts with the cell RT cycle regulator protein NUB1."; RL Hum. Mol. Genet. 11:2723-2733(2002). RN [10] RP VARIANT LCA4 HIS-270, AND VARIANT LEU-302. 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 [11] RP VARIANTS HIS-90 AND GLU-309 DELINS ASP-LEU-ASN-ARG-ARG-GLU-LEU. 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 with RT Leber congenital amaurosis."; RL PLoS ONE 6:E19458-E19458(2011). CC -!- FUNCTION: May be important in protein trafficking and/or protein CC folding and stabilization. CC -!- SUBUNIT: Interacts with NUB1. {ECO:0000269|PubMed:12374762}. CC -!- INTERACTION: CC Q9NZN9; P54132: BLM; NbExp=3; IntAct=EBI-6557414, EBI-621372; CC Q9NZN9; P52954: LBX1; NbExp=3; IntAct=EBI-6557414, EBI-20141748; CC Q9NZN9; Q9Y5A7: NUB1; NbExp=2; IntAct=EBI-6557414, EBI-3936907; CC Q9NZN9; O76074: PDE5A; NbExp=3; IntAct=EBI-6557414, EBI-9023531; CC Q9NZN9; Q9NRY6: PLSCR3; NbExp=3; IntAct=EBI-6557414, EBI-750734; CC Q9NZN9; Q8IYB5-2: SMAP1; NbExp=3; IntAct=EBI-6557414, EBI-12061577; CC Q9NZN9; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-6557414, EBI-717399; CC Q9NZN9; Q9NX01: TXNL4B; NbExp=3; IntAct=EBI-6557414, EBI-10309345; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12374762}. Nucleus CC {ECO:0000269|PubMed:12374762}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q9NZN9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NZN9-2; Sequence=VSP_041507; CC Name=3; Synonyms=AIPL2; CC IsoId=Q9NZN9-3; Sequence=VSP_041508; CC Name=4; CC IsoId=Q9NZN9-4; Sequence=VSP_047708; CC Name=5; CC IsoId=Q9NZN9-5; Sequence=VSP_047709; CC -!- TISSUE SPECIFICITY: Highly expressed in retina. Specifically localized CC to the developing photoreceptor layer and within the photoreceptors of CC the adult retina. {ECO:0000269|PubMed:12374762}. CC -!- DISEASE: Leber congenital amaurosis 4 (LCA4) [MIM:604393]: A severe CC dystrophy of the retina, typically becoming evident in the first years CC of life. Visual function is usually poor and often accompanied by CC nystagmus, sluggish or near-absent pupillary responses, photophobia, CC high hyperopia and keratoconus. {ECO:0000269|PubMed:10615133, CC ECO:0000269|PubMed:12374762, ECO:0000269|PubMed:17724218}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. 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; AF180472; AAF26708.1; -; Genomic_DNA. DR EMBL; AF148864; AAF74023.1; -; mRNA. DR EMBL; AF525970; AAM88405.1; -; mRNA. DR EMBL; AK023970; BAB14744.1; -; mRNA. DR EMBL; AJ633677; CAG17882.1; -; mRNA. DR EMBL; AJ830742; CAH25995.1; -; mRNA. DR EMBL; AJ830743; CAH25996.1; -; mRNA. DR EMBL; AB593053; BAJ84000.1; -; mRNA. DR EMBL; AB593054; BAJ84001.1; -; mRNA. DR EMBL; AC055872; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471108; EAW90310.1; -; Genomic_DNA. DR EMBL; CH471108; EAW90312.1; -; Genomic_DNA. DR EMBL; CH471108; EAW90313.1; -; Genomic_DNA. DR EMBL; CH471108; EAW90314.1; -; Genomic_DNA. DR EMBL; BC012055; AAH12055.1; -; mRNA. DR CCDS; CCDS11075.1; -. [Q9NZN9-1] DR CCDS; CCDS32539.1; -. [Q9NZN9-2] DR CCDS; CCDS32540.1; -. [Q9NZN9-3] DR CCDS; CCDS67130.1; -. [Q9NZN9-4] DR CCDS; CCDS67133.1; -. [Q9NZN9-5] DR RefSeq; NP_001028226.1; NM_001033054.3. [Q9NZN9-3] DR RefSeq; NP_001028227.1; NM_001033055.3. [Q9NZN9-2] DR RefSeq; NP_001272328.1; NM_001285399.2. DR RefSeq; NP_001272329.1; NM_001285400.3. [Q9NZN9-4] DR RefSeq; NP_001272330.1; NM_001285401.3. [Q9NZN9-5] DR RefSeq; NP_001272332.1; NM_001285403.2. DR RefSeq; NP_055151.3; NM_014336.4. [Q9NZN9-1] DR PDB; 5U9A; X-ray; 2.70 A; A=2-161. DR PDB; 5U9I; X-ray; 2.30 A; A=2-161. DR PDB; 5U9J; X-ray; 2.10 A; A/B=2-161. DR PDB; 5U9K; X-ray; 2.70 A; A=2-161. DR PDB; 5V35; X-ray; 2.50 A; A=2-161. DR PDB; 6PX0; X-ray; 1.55 A; A=171-316. DR PDBsum; 5U9A; -. DR PDBsum; 5U9I; -. DR PDBsum; 5U9J; -. DR PDBsum; 5U9K; -. DR PDBsum; 5V35; -. DR PDBsum; 6PX0; -. DR AlphaFoldDB; Q9NZN9; -. DR SASBDB; Q9NZN9; -. DR SMR; Q9NZN9; -. DR BioGRID; 117248; 95. DR CORUM; Q9NZN9; -. DR FunCoup; Q9NZN9; 1375. DR IntAct; Q9NZN9; 28. DR STRING; 9606.ENSP00000370521; -. DR GlyGen; Q9NZN9; 2 sites. DR iPTMnet; Q9NZN9; -. DR PhosphoSitePlus; Q9NZN9; -. DR BioMuta; AIPL1; -. DR DMDM; 23503042; -. DR jPOST; Q9NZN9; -. DR MassIVE; Q9NZN9; -. DR PaxDb; 9606-ENSP00000370521; -. DR PeptideAtlas; Q9NZN9; -. DR ProteomicsDB; 65946; -. DR ProteomicsDB; 65947; -. DR ProteomicsDB; 83467; -. [Q9NZN9-1] DR ProteomicsDB; 83468; -. [Q9NZN9-2] DR ProteomicsDB; 83469; -. [Q9NZN9-3] DR TopDownProteomics; Q9NZN9-1; -. [Q9NZN9-1] DR TopDownProteomics; Q9NZN9-2; -. [Q9NZN9-2] DR TopDownProteomics; Q9NZN9-3; -. [Q9NZN9-3] DR Antibodypedia; 23762; 372 antibodies from 33 providers. DR DNASU; 23746; -. DR Ensembl; ENST00000250087.9; ENSP00000250087.5; ENSG00000129221.16. [Q9NZN9-3] DR Ensembl; ENST00000381129.8; ENSP00000370521.3; ENSG00000129221.16. [Q9NZN9-1] DR Ensembl; ENST00000570466.5; ENSP00000461287.1; ENSG00000129221.16. [Q9NZN9-4] DR Ensembl; ENST00000576307.5; ENSP00000459522.1; ENSG00000129221.16. [Q9NZN9-2] DR Ensembl; ENST00000576776.5; ENSP00000460827.1; ENSG00000129221.16. [Q9NZN9-5] DR GeneID; 23746; -. DR KEGG; hsa:23746; -. DR MANE-Select; ENST00000381129.8; ENSP00000370521.3; NM_014336.5; NP_055151.3. DR UCSC; uc002gcp.5; human. [Q9NZN9-1] DR AGR; HGNC:359; -. DR ClinPGx; PA24653; -. DR CTD; 23746; -. DR DisGeNET; 23746; -. DR GeneCards; AIPL1; -. DR GeneReviews; AIPL1; -. DR HGNC; HGNC:359; AIPL1. DR HPA; ENSG00000129221; Tissue enriched (retina). DR MalaCards; AIPL1; -. DR MIM; 604392; gene. DR MIM; 604393; phenotype. DR OpenTargets; ENSG00000129221; -. DR Orphanet; 1872; Cone rod dystrophy. DR Orphanet; 65; Leber congenital amaurosis. DR VEuPathDB; HostDB:ENSG00000129221; -. DR eggNOG; KOG0545; Eukaryota. DR GeneTree; ENSGT00390000001289; -. DR InParanoid; Q9NZN9; -. DR OMA; EYDRETW; -. DR OrthoDB; 5829758at2759; -. DR PAN-GO; Q9NZN9; 0 GO annotations based on evolutionary models. DR PhylomeDB; Q9NZN9; -. DR PathwayCommons; Q9NZN9; -. DR SignaLink; Q9NZN9; -. DR Agora; ENSG00000129221; -. DR BioGRID-ORCS; 23746; 9 hits in 1153 CRISPR screens. DR ChiTaRS; AIPL1; human. DR GeneWiki; AIPL1; -. DR GenomeRNAi; 23746; -. DR Pharos; Q9NZN9; Tbio. DR PRO; PR:Q9NZN9; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q9NZN9; protein. DR Bgee; ENSG00000129221; Expressed in pancreatic ductal cell and 46 other cell types or tissues. DR ExpressionAtlas; Q9NZN9; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl. DR GO; GO:0001918; F:farnesylated protein binding; IDA:MGI. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro. DR GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc. DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl. DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0007603; P:phototransduction, visible light; IEA:Ensembl. DR GO; GO:0018343; P:protein farnesylation; IDA:MGI. DR GO; GO:0022400; P:regulation of opsin-mediated signaling pathway; IEA:Ensembl. DR GO; GO:0001895; P:retina homeostasis; IEA:Ensembl. DR GO; GO:0007601; P:visual perception; TAS:ProtInc. DR FunFam; 1.25.40.10:FF:000052; Aryl-hydrocarbon-interacting protein-like 1; 1. DR FunFam; 3.10.50.40:FF:000018; Aryl-hydrocarbon-interacting protein-like 1; 1. DR Gene3D; 3.10.50.40; -; 1. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1. DR InterPro; IPR039663; AIP/AIPL1/TTC9. DR InterPro; IPR056277; PPIase_AIP. DR InterPro; IPR046357; PPIase_dom_sf. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_rpt. DR PANTHER; PTHR11242; ARYL HYDROCARBON RECEPTOR INTERACTING PROTEIN RELATED; 1. DR PANTHER; PTHR11242:SF2; ARYL-HYDROCARBON-INTERACTING PROTEIN-LIKE 1; 1. DR Pfam; PF23322; PPIase_AIP; 1. DR SMART; SM00028; TPR; 2. DR SUPFAM; SSF54534; FKBP-like; 1. DR SUPFAM; SSF48452; TPR-like; 1. DR PROSITE; PS50293; TPR_REGION; 2. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant; KW Leber congenital amaurosis; Nucleus; Proteomics identification; KW Reference proteome; Repeat; Sensory transduction; TPR repeat; Vision. FT CHAIN 1..384 FT /note="Aryl-hydrocarbon-interacting protein-like 1" FT /id="PRO_0000075342" FT DOMAIN 53..145 FT /note="PPIase FKBP-type" FT REPEAT 178..211 FT /note="TPR 1" FT REPEAT 230..263 FT /note="TPR 2" FT REPEAT 264..297 FT /note="TPR 3" FT REGION 328..384 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 367..378 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 33..92 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_041507" FT VAR_SEQ 33..54 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_047708" FT VAR_SEQ 93..155 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|Ref.2, ECO:0000303|Ref.5" FT /id="VSP_041508" FT VAR_SEQ 215..238 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_047709" FT VARIANT 33 FT /note="V -> A (in dbSNP:rs16955859)" FT /id="VAR_050626" FT VARIANT 90 FT /note="D -> H (in dbSNP:rs12449580)" FT /evidence="ECO:0000269|PubMed:10615133, FT ECO:0000269|PubMed:21602930" FT /id="VAR_010140" FT VARIANT 134 FT /note="Y -> F (in dbSNP:rs16955851)" FT /id="VAR_050627" FT VARIANT 239 FT /note="C -> R (in LCA4; no significant effect on FT interaction with NUB1; dbSNP:rs62637012)" FT /evidence="ECO:0000269|PubMed:10615133, FT ECO:0000269|PubMed:12374762" FT /id="VAR_010139" FT VARIANT 270 FT /note="R -> H (in LCA4)" FT /evidence="ECO:0000269|PubMed:17724218" FT /id="VAR_067165" FT VARIANT 302 FT /note="R -> L (found in a patient with LCA4; there is no FT interaction with NUB1; dbSNP:rs62637015)" FT /evidence="ECO:0000269|PubMed:12374762, FT ECO:0000269|PubMed:17724218" FT /id="VAR_067166" FT VARIANT 309 FT /note="E -> DLNRREL (found in a patient with LCA4)" FT /evidence="ECO:0000269|PubMed:21602930" FT /id="VAR_067167" FT MUTAGEN 53 FT /note="R->W: No interaction with NUB1." FT /evidence="ECO:0000269|PubMed:12374762" FT MUTAGEN 79 FT /note="M->T: No interaction with NUB1." FT /evidence="ECO:0000269|PubMed:12374762" FT MUTAGEN 96 FT /note="V->I: No interaction with NUB1." FT /evidence="ECO:0000269|PubMed:12374762" FT MUTAGEN 197 FT /note="A->P: No significant effect on interaction with FT NUB1." FT /evidence="ECO:0000269|PubMed:12374762" FT MUTAGEN 206 FT /note="I->N: No significant effect on interaction with FT NUB1." FT /evidence="ECO:0000269|PubMed:12374762" FT MUTAGEN 262 FT /note="G->S: No interaction with NUB1." FT /evidence="ECO:0000269|PubMed:12374762" FT CONFLICT 244 FT /note="E -> K (in Ref. 3; CAG17882)" FT /evidence="ECO:0000305" FT CONFLICT 306..315 FT /note="RLLENRMAEK -> EAAGEPHGGE (in Ref. 1; AAF26708)" FT /evidence="ECO:0000305" FT STRAND 12..18 FT /evidence="ECO:0007829|PDB:5U9J" FT STRAND 21..23 FT /evidence="ECO:0007829|PDB:5U9I" FT STRAND 32..40 FT /evidence="ECO:0007829|PDB:5U9J" FT STRAND 42..45 FT /evidence="ECO:0007829|PDB:5U9J" FT STRAND 48..51 FT /evidence="ECO:0007829|PDB:5U9J" FT HELIX 52..55 FT /evidence="ECO:0007829|PDB:5U9J" FT STRAND 59..62 FT /evidence="ECO:0007829|PDB:5U9J" FT STRAND 66..68 FT /evidence="ECO:0007829|PDB:5U9A" FT HELIX 71..76 FT /evidence="ECO:0007829|PDB:5U9J" FT STRAND 84..89 FT /evidence="ECO:0007829|PDB:5U9J" FT HELIX 91..94 FT /evidence="ECO:0007829|PDB:5U9J" FT HELIX 97..108 FT /evidence="ECO:0007829|PDB:5U9J" FT HELIX 116..129 FT /evidence="ECO:0007829|PDB:5U9J" FT HELIX 135..142 FT /evidence="ECO:0007829|PDB:5U9J" FT STRAND 147..157 FT /evidence="ECO:0007829|PDB:5U9J" FT HELIX 181..190 FT /evidence="ECO:0007829|PDB:6PX0" FT HELIX 194..212 FT /evidence="ECO:0007829|PDB:6PX0" FT HELIX 220..242 FT /evidence="ECO:0007829|PDB:6PX0" FT HELIX 246..259 FT /evidence="ECO:0007829|PDB:6PX0" FT HELIX 264..276 FT /evidence="ECO:0007829|PDB:6PX0" FT HELIX 280..293 FT /evidence="ECO:0007829|PDB:6PX0" FT HELIX 295..297 FT /evidence="ECO:0007829|PDB:6PX0" FT HELIX 298..312 FT /evidence="ECO:0007829|PDB:6PX0" SQ SEQUENCE 384 AA; 43903 MW; 47F681A1DC91A82D CRC64; MDAALLLNVE GVKKTILHGG TGELPNFITG SRVIFHFRTM KCDEERTVID DSRQVGQPMH IIIGNMFKLE VWEILLTSMR VHEVAEFWCD TIHTGVYPIL SRSLRQMAQG KDPTEWHVHT CGLANMFAYH TLGYEDLDEL QKEPQPLVFV IELLQVDAPS DYQRETWNLS NHEKMKAVPV LHGEGNRLFK LGRYEEASSK YQEAIICLRN LQTKEKPWEV QWLKLEKMIN TLILNYCQCL LKKEEYYEVL EHTSDILRHH PGIVKAYYVR ARAHAEVWNE AEAKADLQKV LELEPSMQKA VRRELRLLEN RMAEKQEEER LRCRNMLSQG ATQPPAEPPT EPPAQSSTEP PAEPPTAPSA ELSAGPPAEP ATEPPPSPGH SLQH //