ID SNF8_HUMAN Reviewed; 258 AA. AC Q96H20; Q8IXY3; Q9UN50; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 10-JUN-2026, entry version 186. DE RecName: Full=Vacuolar-sorting protein SNF8; DE AltName: Full=ELL-associated protein of 30 kDa; DE AltName: Full=ESCRT-II complex subunit VPS22; DE Short=hVps22; GN Name=SNF8; Synonyms=EAP30; 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]. RX PubMed=10419521; DOI=10.1074/jbc.274.31.21981; RA Schmidt A.E., Miller T., Schmidt S.L., Shiekhattar R., Shilatifard A.; RT "Cloning and characterization of the EAP30 subunit of the ELL complex that RT confers derepression of transcription by RNA polymerase II."; RL J. Biol. Chem. 274:21981-21985(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Pancreas, and Placenta; 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 [3] RP SELF-ASSOCIATION, AND INTERACTION WITH VPS25; VPS36 AND TSG101. RX PubMed=14505570; DOI=10.1016/s0092-8674(03)00714-1; RA von Schwedler U.K., Stuchell M., Mueller B., Ward D.M., Chung H.-Y., RA Morita E., Wang H.E., Davis T., He G.P., Cimbora D.M., Scott A., RA Kraeusslich H.-G., Kaplan J., Morham S.G., Sundquist W.I.; RT "The protein network of HIV budding."; RL Cell 114:701-713(2003). RN [4] RP IDENTIFICATION IN THE ESCRT-II COMPLEX, AND INTERACTION WITH VPS36 AND RP VPS25. RX PubMed=14519844; DOI=10.1073/pnas.2133846100; RA Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.; RT "Divergent retroviral late-budding domains recruit vacuolar protein sorting RT factors by using alternative adaptor proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003). RN [5] RP ERRATUM OF PUBMED:14519844. RA Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.; RL Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003). RN [6] RP INTERACTION WITH RILPL1, AND SUBCELLULAR LOCATION. RX PubMed=16857164; DOI=10.1016/j.bbrc.2006.07.007; RA Progida C., Spinosa M.R., De Luca A., Bucci C.; RT "RILP interacts with the VPS22 component of the ESCRT-II complex."; RL Biochem. Biophys. Res. Commun. 347:1074-1079(2006). RN [7] RP INTERACTION WITH VPS25; VPS36 AND RILPL1, AND SUBCELLULAR LOCATION. RX PubMed=17010938; DOI=10.1016/j.bbrc.2006.09.064; RA Wang T., Hong W.; RT "RILP interacts with VPS22 and VPS36 of ESCRT-II and regulates their RT membrane recruitment."; RL Biochem. Biophys. Res. Commun. 350:413-423(2006). RN [8] RP INTERACTION WITH 14-3-3 PROTEINS. RX PubMed=16260042; DOI=10.1016/j.jneumeth.2005.09.015; RA Satoh J., Nanri Y., Yamamura T.; RT "Rapid identification of 14-3-3-binding proteins by protein microarray RT analysis."; RL J. Neurosci. Methods 152:278-288(2006). RN [9] RP INTERACTION WITH VPS25; VPS36 AND TSG101, AND SUBCELLULAR LOCATION. RX PubMed=16973552; DOI=10.1128/jvi.01049-06; RA Langelier C., von Schwedler U.K., Fisher R.D., De Domenico I., White P.L., RA Hill C.P., Kaplan J., Ward D., Sundquist W.I.; RT "Human ESCRT-II complex and its role in human immunodeficiency virus type 1 RT release."; RL J. Virol. 80:9465-9480(2006). RN [10] RP FUNCTION. RX PubMed=17959629; DOI=10.1242/jcs.017301; RA Progida C., Malerod L., Stuffers S., Brech A., Bucci C., Stenmark H.; RT "RILP is required for the proper morphology and function of late RT endosomes."; RL J. Cell Sci. 120:3729-3737(2007). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=17714434; DOI=10.1111/j.1600-0854.2007.00630.x; RA Maleroed L., Stuffers S., Brech A., Stenmark H.; RT "Vps22/EAP30 in ESCRT-II mediates endosomal sorting of growth factor and RT chemokine receptors destined for lysosomal degradation."; RL Traffic 8:1617-1629(2007). RN [12] RP FUNCTION. RX PubMed=18031739; DOI=10.1016/j.yexcr.2007.10.014; RA Raiborg C., Malerod L., Pedersen N.M., Stenmark H.; RT "Differential functions of Hrs and ESCRT proteins in endocytic membrane RT trafficking."; RL Exp. Cell Res. 314:801-813(2008). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP FUNCTION. RX PubMed=22660413; DOI=10.1038/ncb2502; RA Baietti M.F., Zhang Z., Mortier E., Melchior A., Degeest G., Geeraerts A., RA Ivarsson Y., Depoortere F., Coomans C., Vermeiren E., Zimmermann P., RA David G.; RT "Syndecan-syntenin-ALIX regulates the biogenesis of exosomes."; RL Nat. Cell Biol. 14:677-685(2012). RN [15] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-4, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 25-258 IN COMPLEX WITH VPS25 AND RP VPS36. RX PubMed=18539118; DOI=10.1016/j.devcel.2008.04.004; RA Im Y.J., Hurley J.H.; RT "Integrated structural model and membrane targeting mechanism of the human RT ESCRT-II complex."; RL Dev. Cell 14:902-913(2008). RN [17] RP VARIANTS DEE115 LEU-79; 167-TYR--PRO-258 DEL; ASP-191 AND LEU-208, VARIANTS RP NEDOA LEU-79 AND ILE-102, CHARACTERIZATION OF VARIANT DEE115 RP 167-TYR--PRO-258 DEL, CHARACTERIZATION OF VARIANT NEDOA ILE-102, RP INVOLVEMENT IN DEE115, INVOLVEMENT IN NEDOA, AND FUNCTION. RX PubMed=38423010; DOI=10.1016/j.ajhg.2024.02.005; RA Brugger M., Lauri A., Zhen Y., Gramegna L.L., Zott B., Sekulic N., RA Fasano G., Kopajtich R., Cordeddu V., Radio F.C., Mancini C., Pizzi S., RA Paradisi G., Zanni G., Vasco G., Carrozzo R., Palombo F., Tonon C., RA Lodi R., La Morgia C., Arelin M., Blechschmidt C., Finck T., Soerensen V., RA Kreiser K., Strobl-Wildemann G., Daum H., Michaelson-Cohen R., Ziccardi L., RA Zampino G., Prokisch H., Abou Jamra R., Fiorini C., Arzberger T., RA Winkelmann J., Caporali L., Carelli V., Stenmark H., Tartaglia M., RA Wagner M.; RT "Bi-allelic variants in SNF8 cause a disease spectrum ranging from severe RT developmental and epileptic encephalopathy to syndromic optic atrophy."; RL Am. J. Hum. Genet. 111:594-613(2024). CC -!- FUNCTION: Component of the endosomal sorting complex required for CC transport II (ESCRT-II), which is required for multivesicular body CC (MVB) formation and sorting of endosomal cargo proteins into MVBs, and CC plays a role in autophagy (PubMed:38423010). The MVB pathway mediates CC delivery of transmembrane proteins into the lumen of the lysosome for CC degradation. The ESCRT-II complex is probably involved in the CC recruitment of the ESCRT-III complex. The ESCRT-II complex may also CC play a role in transcription regulation by participating in CC derepression of transcription by RNA polymerase II, possibly via its CC interaction with ELL. Required for degradation of both endocytosed EGF CC and EGFR, but not for the EGFR ligand-mediated internalization. It is CC also required for the degradation of CXCR4. Required for the exosomal CC release of SDCBP, CD63 and syndecan (PubMed:22660413). CC {ECO:0000269|PubMed:17714434, ECO:0000269|PubMed:17959629, CC ECO:0000269|PubMed:18031739, ECO:0000269|PubMed:22660413, CC ECO:0000269|PubMed:38423010}. CC -!- SUBUNIT: Component of the endosomal sorting complex required for CC transport II (ESCRT-II), composed of SNF8, VPS25 and VPS36. SNF8 is CC essential for the stability of the ESCRT-II complex. ESCRT-II interacts CC with ELL. Interacts with TSG101 (via the C-terminal domain). Interacts CC with RILPL1 (via the N-terminal domain); which recruits ESCRT-II to the CC endosome membranes. Interacts with 14-3-3 proteins. CC {ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844, CC ECO:0000269|PubMed:16260042, ECO:0000269|PubMed:16857164, CC ECO:0000269|PubMed:16973552, ECO:0000269|PubMed:17010938, CC ECO:0000269|PubMed:17714434, ECO:0000269|PubMed:18539118}. CC -!- INTERACTION: CC Q96H20; Q6PJH3: AKAP9; NbExp=3; IntAct=EBI-747719, EBI-11745576; CC Q96H20; P55212: CASP6; NbExp=3; IntAct=EBI-747719, EBI-718729; CC Q96H20; Q92989: CLP1; NbExp=3; IntAct=EBI-747719, EBI-2559831; CC Q96H20; Q8WUE5: CT55; NbExp=3; IntAct=EBI-747719, EBI-6873363; CC Q96H20; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-747719, EBI-12593112; CC Q96H20; P55199: ELL; NbExp=3; IntAct=EBI-747719, EBI-1245868; CC Q96H20; Q9NW38: FANCL; NbExp=3; IntAct=EBI-747719, EBI-2339898; CC Q96H20; Q8IVS8: GLYCTK; NbExp=5; IntAct=EBI-747719, EBI-748515; CC Q96H20; Q08379: GOLGA2; NbExp=3; IntAct=EBI-747719, EBI-618309; CC Q96H20; O60341: KDM1A; NbExp=2; IntAct=EBI-747719, EBI-710124; CC Q96H20; O14901: KLF11; NbExp=3; IntAct=EBI-747719, EBI-948266; CC Q96H20; P13473-2: LAMP2; NbExp=3; IntAct=EBI-747719, EBI-21591415; CC Q96H20; P49736: MCM2; NbExp=8; IntAct=EBI-747719, EBI-374819; CC Q96H20; P24928: POLR2A; NbExp=2; IntAct=EBI-747719, EBI-295301; CC Q96H20; Q96LA8: PRMT6; NbExp=2; IntAct=EBI-747719, EBI-912440; CC Q96H20; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-747719, EBI-5280197; CC Q96H20; P62826: RAN; NbExp=3; IntAct=EBI-747719, EBI-286642; CC Q96H20; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-747719, EBI-358489; CC Q96H20; O95793-2: STAU1; NbExp=3; IntAct=EBI-747719, EBI-358189; CC Q96H20; P51687: SUOX; NbExp=5; IntAct=EBI-747719, EBI-3921347; CC Q96H20; Q9BYV2: TRIM54; NbExp=6; IntAct=EBI-747719, EBI-2130429; CC Q96H20; P40222: TXLNA; NbExp=3; IntAct=EBI-747719, EBI-359793; CC Q96H20; Q08AM6: VAC14; NbExp=4; IntAct=EBI-747719, EBI-2107455; CC Q96H20; Q9BRG1: VPS25; NbExp=20; IntAct=EBI-747719, EBI-741945; CC Q96H20; Q86VN1: VPS36; NbExp=9; IntAct=EBI-747719, EBI-4401822; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane. Nucleus CC {ECO:0000305}. Late endosome membrane. Note=Recruited to the endosome CC membrane to participate in vesicle formation. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96H20-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96H20-2; Sequence=VSP_015340; CC -!- DISEASE: Developmental and epileptic encephalopathy 115 (DEE115) CC [MIM:620783]: A form of epileptic encephalopathy, a heterogeneous group CC of early-onset epilepsies characterized by refractory seizures, CC neurodevelopmental impairment, and poor prognosis. Development is CC normal prior to seizure onset, after which cognitive and motor delays CC become apparent. DEE115 is an autosomal recessive, severe form CC characterized by onset soon after birth. Affected individuals show CC massive reduction of white matter, hypo- or aplasia of the corpus CC callosum, and neurodevelopmental arrest. Death in the first year of CC life may occur. {ECO:0000269|PubMed:38423010}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- DISEASE: Neurodevelopmental disorder plus optic atrophy (NEDOA) CC [MIM:620784]: An autosomal recessive disorder characterized by mild CC developmental delay, intellectual disability and childhood-onset optic CC atrophy or ataxia. {ECO:0000269|PubMed:38423010}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the SNF8 family. {ECO:0000305}. 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; AF156102; AAD46560.1; -; mRNA. DR EMBL; BC008976; AAH08976.1; -; mRNA. DR EMBL; BC038830; AAH38830.1; -; mRNA. DR CCDS; CCDS11541.1; -. [Q96H20-1] DR CCDS; CCDS82156.1; -. [Q96H20-2] DR RefSeq; NP_001304121.1; NM_001317192.2. [Q96H20-2] DR RefSeq; NP_001304122.1; NM_001317193.1. DR RefSeq; NP_001304123.1; NM_001317194.1. DR RefSeq; NP_009172.2; NM_007241.3. [Q96H20-1] DR PDB; 2ZME; X-ray; 2.90 A; A=1-258. DR PDB; 3CUQ; X-ray; 2.61 A; A=25-258. DR PDBsum; 2ZME; -. DR PDBsum; 3CUQ; -. DR AlphaFoldDB; Q96H20; -. DR SMR; Q96H20; -. DR BioGRID; 116425; 92. DR ComplexPortal; CPX-2506; ESCRT-II complex. DR CORUM; Q96H20; -. DR FunCoup; Q96H20; 2596. DR IntAct; Q96H20; 48. DR MINT; Q96H20; -. DR NDEx; MUSIC2-C5180-SNF8; Osteosarcoma (U2OS) cell map - C5180 (62 proteins). DR STRING; 9606.ENSP00000421380; -. DR iPTMnet; Q96H20; -. DR MetOSite; Q96H20; -. DR PhosphoSitePlus; Q96H20; -. DR BioMuta; SNF8; -. DR DMDM; 73919323; -. DR jPOST; Q96H20; -. DR MassIVE; Q96H20; -. DR PaxDb; 9606-ENSP00000421380; -. DR PeptideAtlas; Q96H20; -. DR ProteomicsDB; 76695; -. [Q96H20-1] DR ProteomicsDB; 76696; -. [Q96H20-2] DR Pumba; Q96H20; -. DR Antibodypedia; 30335; 203 antibodies from 22 providers. DR DNASU; 11267; -. DR Ensembl; ENST00000290330.7; ENSP00000290330.3; ENSG00000159210.11. [Q96H20-2] DR Ensembl; ENST00000502492.6; ENSP00000421380.1; ENSG00000159210.11. [Q96H20-1] DR GeneID; 11267; -. DR KEGG; hsa:11267; -. DR MANE-Select; ENST00000502492.6; ENSP00000421380.1; NM_007241.4; NP_009172.2. DR UCSC; uc002ioj.5; human. [Q96H20-1] DR AGR; HGNC:17028; -. DR ClinPGx; PA142670892; -. DR CTD; 11267; -. DR DisGeNET; 11267; -. DR GeneCards; SNF8; -. DR HGNC; HGNC:17028; SNF8. DR HPA; ENSG00000159210; Low tissue specificity. DR MalaCards; SNF8; -. DR MIM; 610904; gene. DR MIM; 620783; phenotype. DR MIM; 620784; phenotype. DR OpenTargets; ENSG00000159210; -. DR VEuPathDB; HostDB:ENSG00000159210; -. DR eggNOG; KOG3341; Eukaryota. DR GeneTree; ENSGT00390000007843; -. DR HOGENOM; CLU_070147_2_0_1; -. DR InParanoid; Q96H20; -. DR OMA; QIVEVCM; -. DR OrthoDB; 283883at2759; -. DR PAN-GO; Q96H20; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q96H20; -. DR PathwayCommons; Q96H20; -. DR Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT). DR Reactome; R-HSA-9610379; HCMV Late Events. DR SignaLink; Q96H20; -. DR Agora; ENSG00000159210; -. DR BioGRID-ORCS; 11267; 688 hits in 1178 CRISPR screens. DR ChiTaRS; SNF8; human. DR EvolutionaryTrace; Q96H20; -. DR GeneWiki; SNF8; -. DR GenomeRNAi; 11267; -. DR Pharos; Q96H20; Tbio. DR PRO; PR:Q96H20; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q96H20; protein. DR Bgee; ENSG00000159210; Expressed in apex of heart and 204 other cell types or tissues. DR ExpressionAtlas; Q96H20; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB. DR GO; GO:0000814; C:ESCRT II complex; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB. DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI. DR GO; GO:0016247; F:channel regulator activity; IDA:UniProtKB. DR GO; GO:0008289; F:lipid binding; IPI:DisProt. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-KW. DR GO; GO:0045022; P:early endosome to late endosome transport; IMP:UniProtKB. DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB. DR GO; GO:0016236; P:macroautophagy; IMP:UniProtKB. DR GO; GO:0090148; P:membrane fission; NAS:ComplexPortal. DR GO; GO:0036258; P:multivesicular body assembly; IMP:UniProtKB. DR GO; GO:0071985; P:multivesicular body sorting pathway; IMP:UniProtKB. DR GO; GO:1903543; P:positive regulation of exosomal secretion; IMP:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB. DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:UniProtKB. DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central. DR GO; GO:0042176; P:regulation of protein catabolic process; IMP:UniProtKB. DR GO; GO:0061635; P:regulation of protein complex stability; IMP:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI. DR DisProt; DP02598; -. DR FunFam; 1.10.10.10:FF:000085; Vacuolar-sorting protein SNF8; 1. DR FunFam; 1.10.10.10:FF:000234; Vacuolar-sorting protein SNF8; 1. DR Gene3D; 6.10.140.180; -; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2. DR IDEAL; IID00864; -. DR InterPro; IPR016689; ESCRT-2_cplx_Snf8. DR InterPro; IPR040608; Snf8/Vps36. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR12806; EAP30 SUBUNIT OF ELL COMPLEX; 1. DR PANTHER; PTHR12806:SF0; VACUOLAR-SORTING PROTEIN SNF8; 1. DR Pfam; PF04157; EAP30; 1. DR PIRSF; PIRSF017215; ESCRT2_Vps22; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; KW Disease variant; Endosome; Epilepsy; Intellectual disability; Membrane; KW Methylation; Nucleus; Protein transport; Proteomics identification; KW Reference proteome; Transcription; Transcription regulation; Transport. FT CHAIN 1..258 FT /note="Vacuolar-sorting protein SNF8" FT /id="PRO_0000215209" FT COILED 27..53 FT /evidence="ECO:0000255" FT MOD_RES 4 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT VAR_SEQ 189 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_015340" FT VARIANT 79 FT /note="P -> L (in DEE115 and NEDOA; likely pathogenic; FT dbSNP:rs2041013413)" FT /evidence="ECO:0000269|PubMed:38423010" FT /id="VAR_089579" FT VARIANT 102 FT /note="V -> I (in NEDOA; likely pathogenic; fails to rescue FT defective embryo development in a zebrafish disease model; FT dbSNP:rs200399045)" FT /evidence="ECO:0000269|PubMed:38423010" FT /id="VAR_089580" FT VARIANT 167..258 FT /note="Missing (in DEE115; pathogenic; fails to rescue FT defective embryo development in a zebrafish disease model)" FT /evidence="ECO:0000269|PubMed:38423010" FT /id="VAR_089581" FT VARIANT 191 FT /note="G -> D (in DEE115; likely pathogenic; FT dbSNP:rs2040862241)" FT /evidence="ECO:0000269|PubMed:38423010" FT /id="VAR_089582" FT VARIANT 208 FT /note="R -> L (in DEE115; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:38423010" FT /id="VAR_089583" FT CONFLICT 250 FT /note="A -> P (in Ref. 1; AAD46560)" FT /evidence="ECO:0000305" FT HELIX 37..60 FT /evidence="ECO:0007829|PDB:3CUQ" FT HELIX 62..75 FT /evidence="ECO:0007829|PDB:3CUQ" FT HELIX 86..91 FT /evidence="ECO:0007829|PDB:3CUQ" FT HELIX 93..115 FT /evidence="ECO:0007829|PDB:3CUQ" FT STRAND 116..120 FT /evidence="ECO:0007829|PDB:3CUQ" FT HELIX 121..130 FT /evidence="ECO:0007829|PDB:3CUQ" FT TURN 131..134 FT /evidence="ECO:0007829|PDB:3CUQ" FT HELIX 141..151 FT /evidence="ECO:0007829|PDB:3CUQ" FT HELIX 152..154 FT /evidence="ECO:0007829|PDB:3CUQ" FT STRAND 159..163 FT /evidence="ECO:0007829|PDB:3CUQ" FT STRAND 166..170 FT /evidence="ECO:0007829|PDB:3CUQ" FT HELIX 178..187 FT /evidence="ECO:0007829|PDB:3CUQ" FT TURN 188..190 FT /evidence="ECO:0007829|PDB:3CUQ" FT STRAND 191..193 FT /evidence="ECO:0007829|PDB:3CUQ" FT HELIX 195..202 FT /evidence="ECO:0007829|PDB:3CUQ" FT HELIX 206..219 FT /evidence="ECO:0007829|PDB:3CUQ" FT STRAND 223..231 FT /evidence="ECO:0007829|PDB:3CUQ" FT STRAND 233..235 FT /evidence="ECO:0007829|PDB:3CUQ" FT HELIX 249..251 FT /evidence="ECO:0007829|PDB:3CUQ" SQ SEQUENCE 258 AA; 28864 MW; FD6CBA6BC0A4485E CRC64; MHRRGVGAGA IAKKKLAEAK YKERGTVLAE DQLAQMSKQL DMFKTNLEEF ASKHKQEIRK NPEFRVQFQD MCATIGVDPL ASGKGFWSEM LGVGDFYYEL GVQIIEVCLA LKHRNGGLIT LEELHQQVLK GRGKFAQDVS QDDLIRAIKK LKALGTGFGI IPVGGTYLIQ SVPAELNMDH TVVLQLAEKN GYVTVSEIKA SLKWETERAR QVLEHLLKEG LAWLDLQAPG EAHYWLPALF TDLYSQEITA EEAREALP //