AIPL1_HUMAN
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 03-AUG-2022, entry version 191.
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; P52954: LBX1; NbExp=3; IntAct=EBI-6557414, EBI-20141748;
CC Q9NZN9; Q9Y5A7: NUB1; NbExp=2; IntAct=EBI-6557414, EBI-3936907;
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 -!- WEB RESOURCE: Name=Mutations of the AIPL1 gene; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/aipl1mut.htm";
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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_001033054.2. [Q9NZN9-3]
DR RefSeq; NP_001028227.1; NM_001033055.2. [Q9NZN9-2]
DR RefSeq; NP_001272328.1; NM_001285399.2.
DR RefSeq; NP_001272329.1; NM_001285400.2. [Q9NZN9-4]
DR RefSeq; NP_001272330.1; NM_001285401.2. [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; 94.
DR IntAct; Q9NZN9; 20.
DR STRING; 9606.ENSP00000370521; -.
DR iPTMnet; Q9NZN9; -.
DR PhosphoSitePlus; Q9NZN9; -.
DR BioMuta; AIPL1; -.
DR DMDM; 23503042; -.
DR MassIVE; Q9NZN9; -.
DR PaxDb; Q9NZN9; -.
DR PeptideAtlas; Q9NZN9; -.
DR PRIDE; 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; 370 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 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 neXtProt; NX_Q9NZN9; -.
DR OpenTargets; ENSG00000129221; -.
DR Orphanet; 1872; Cone rod dystrophy.
DR Orphanet; 65; Leber congenital amaurosis.
DR PharmGKB; PA24653; -.
DR VEuPathDB; HostDB:ENSG00000129221; -.
DR eggNOG; KOG0545; Eukaryota.
DR GeneTree; ENSGT00390000001289; -.
DR InParanoid; Q9NZN9; -.
DR OMA; RTTKCDE; -.
DR PhylomeDB; Q9NZN9; -.
DR TreeFam; TF314507; -.
DR PathwayCommons; Q9NZN9; -.
DR SignaLink; Q9NZN9; -.
DR BioGRID-ORCS; 23746; 9 hits in 1073 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 tissues.
DR ExpressionAtlas; Q9NZN9; baseline and differential.
DR Genevisible; Q9NZN9; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; 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 rhodopsin mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0001895; P:retina homeostasis; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR039663; AIP/AIPL1.
DR InterPro; IPR031209; AIPL1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR11242; PTHR11242; 1.
DR PANTHER; PTHR11242:SF2; PTHR11242:SF2; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF48452; SSF48452; 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; Reference proteome; Repeat;
KW 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 335..361
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
