ID GEMI4_HUMAN Reviewed; 1058 AA. AC P57678; Q9NZS7; Q9UG32; Q9Y4Q2; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 08-FEB-2011, sequence version 2. DT 27-MAR-2024, entry version 186. DE RecName: Full=Gem-associated protein 4; DE Short=Gemin-4; DE AltName: Full=Component of gems 4; DE AltName: Full=p97; GN Name=GEMIN4; 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], AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=10725331; DOI=10.1083/jcb.148.6.1177; RA Charroux B., Pellizzoni L., Perkinson R.A., Yong J., Shevchenko A., RA Mann M., Dreyfuss G.; RT "Gemin4: a novel component of the SMN complex that is found in both gems RT and nucleoli."; RL J. Cell Biol. 148:1177-1186(2000). RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 186-1058. RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [4] RP INTERACTION WITH PPP4R2. RX PubMed=12668731; DOI=10.1242/jcs.00409; RA Carnegie G.K., Sleeman J.E., Morrice N., Hastie C.J., Peggie M.W., RA Philp A., Lamond A.I., Cohen P.T.W.; RT "Protein phosphatase 4 interacts with the survival of motor neurons complex RT and enhances the temporal localisation of snRNPs."; RL J. Cell Sci. 116:1905-1913(2003). RN [5] RP IDENTIFICATION IN THE SMN COMPLEX, AND IDENTIFICATION IN SMN-SM COMPLEX. RX PubMed=16314521; DOI=10.1128/mcb.25.24.10989-11004.2005; RA Golembe T.J., Yong J., Dreyfuss G.; RT "Specific sequence features, recognized by the SMN complex, identify snRNAs RT and determine their fate as snRNPs."; RL Mol. Cell. Biol. 25:10989-11004(2005). RN [6] RP IDENTIFICATION IN THE SMN COMPLEX, AND INTERACTION WITH GEMIN3 AND GEMIN8. RX PubMed=17178713; DOI=10.1074/jbc.m608528200; RA Otter S., Grimmler M., Neuenkirchen N., Chari A., Sickmann A., Fischer U.; RT "A comprehensive interaction map of the human survival of motor neuron RT (SMN) complex."; RL J. Biol. Chem. 282:5825-5833(2007). RN [7] RP FUNCTION IN SNRNP BIOGENESIS, AND IDENTIFICATION IN SMN-SM COMPLEX. RX PubMed=18984161; DOI=10.1016/j.cell.2008.09.020; RA Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., RA Englbrecht C., Sickmann A., Stark H., Fischer U.; RT "An assembly chaperone collaborates with the SMN complex to generate RT spliceosomal SnRNPs."; RL Cell 135:497-509(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [10] 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-84 AND SER-86, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [12] RP INTERACTION WITH GEMIN5. RX PubMed=33963192; DOI=10.1038/s41467-021-22627-w; RA Kour S., Rajan D.S., Fortuna T.R., Anderson E.N., Ward C., Lee Y., Lee S., RA Shin Y.B., Chae J.H., Choi M., Siquier K., Cantagrel V., Amiel J., RA Stolerman E.S., Barnett S.S., Cousin M.A., Castro D., McDonald K., RA Kirmse B., Nemeth A.H., Rajasundaram D., Innes A.M., Lynch D., Frosk P., RA Collins A., Gibbons M., Yang M., Desguerre I., Boddaert N., Gitiaux C., RA Rydning S.L., Selmer K.K., Urreizti R., Garcia-Oguiza A., Osorio A.N., RA Verdura E., Pujol A., McCurry H.R., Landers J.E., Agnihotri S., RA Andriescu E.C., Moody S.B., Phornphutkul C., Sacoto M.J.G., Begtrup A., RA Houlden H., Kirschner J., Schorling D., Rudnik-Schoeneborn S., Strom T.M., RA Leiz S., Juliette K., Richardson R., Yang Y., Zhang Y., Wang M., Wang J., RA Wang X., Platzer K., Donkervoort S., Boennemann C.G., Wagner M., Issa M.Y., RA Elbendary H.M., Stanley V., Maroofian R., Gleeson J.G., Zaki M.S., RA Senderek J., Pandey U.B.; RT "Loss of function mutations in GEMIN5 cause a neurodevelopmental RT disorder."; RL Nat. Commun. 12:2558-2558(2021). RN [13] RP VARIANT NEDMCR ARG-818, AND INVOLVEMENT IN NEDMCR. RX PubMed=25558065; DOI=10.1016/j.celrep.2014.12.015; RA Alazami A.M., Patel N., Shamseldin H.E., Anazi S., Al-Dosari M.S., RA Alzahrani F., Hijazi H., Alshammari M., Aldahmesh M.A., Salih M.A., RA Faqeih E., Alhashem A., Bashiri F.A., Al-Owain M., Kentab A.Y., Sogaty S., RA Al Tala S., Temsah M.H., Tulbah M., Aljelaify R.F., Alshahwan S.A., RA Seidahmed M.Z., Alhadid A.A., Aldhalaan H., Alqallaf F., Kurdi W., RA Alfadhel M., Babay Z., Alsogheer M., Kaya N., Al-Hassnan Z.N., RA Abdel-Salam G.M., Al-Sannaa N., Al Mutairi F., El Khashab H.Y., Bohlega S., RA Jia X., Nguyen H.C., Hammami R., Adly N., Mohamed J.Y., Abdulwahab F., RA Ibrahim N., Naim E.A., Al-Younes B., Meyer B.F., Hashem M., Shaheen R., RA Xiong Y., Abouelhoda M., Aldeeri A.A., Monies D.M., Alkuraya F.S.; RT "Accelerating novel candidate gene discovery in neurogenetic disorders via RT whole-exome sequencing of prescreened multiplex consanguineous families."; RL Cell Rep. 10:148-161(2015). RN [14] RP VARIANT NEDMCR LEU-105. RX PubMed=30237576; DOI=10.1038/s41436-018-0138-x; RA Maddirevula S., Alzahrani F., Al-Owain M., Al Muhaizea M.A., Kayyali H.R., RA AlHashem A., Rahbeeni Z., Al-Otaibi M., Alzaidan H.I., Balobaid A., RA El Khashab H.Y., Bubshait D.K., Faden M., Yamani S.A., Dabbagh O., RA Al-Mureikhi M., Jasser A.A., Alsaif H.S., Alluhaydan I., Seidahmed M.Z., RA Alabbasi B.H., Almogarri I., Kurdi W., Akleh H., Qari A., Al Tala S.M., RA Alhomaidi S., Kentab A.Y., Salih M.A., Chedrawi A., Alameer S., Tabarki B., RA Shamseldin H.E., Patel N., Ibrahim N., Abdulwahab F., Samira M., Goljan E., RA Abouelhoda M., Meyer B.F., Hashem M., Shaheen R., AlShahwan S., RA Alfadhel M., Ben-Omran T., Al-Qattan M.M., Monies D., Alkuraya F.S.; RT "Autozygome and high throughput confirmation of disease genes candidacy."; RL Genet. Med. 21:736-742(2019). CC -!- FUNCTION: The SMN complex catalyzes the assembly of small nuclear CC ribonucleoproteins (snRNPs), the building blocks of the spliceosome, CC and thereby plays an important role in the splicing of cellular pre- CC mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins CC SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in CC a heptameric protein ring on the Sm site of the small nuclear RNA to CC form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, CC SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm CC complex by the chaperone CLNS1A that controls the assembly of the core CC snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm CC proteins from CLNS1A forming an intermediate. Binding of snRNA inside CC 5Sm triggers eviction of the SMN complex, thereby allowing binding of CC SNRPD3 and SNRPB to complete assembly of the core snRNP. CC {ECO:0000269|PubMed:18984161}. CC -!- SUBUNIT: Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, CC DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP CC (PubMed:18984161, PubMed:16314521, PubMed:17178713). Part of the SMN-Sm CC complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, CC GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, CC SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG (PubMed:18984161, CC PubMed:16314521). Interacts with GEMIN3; the interaction is direct CC (PubMed:18984161, PubMed:17178713). Interacts with GEMIN5 CC (PubMed:33963192). Interacts with GEMIN8; the interaction is direct CC (PubMed:17178713). Interacts with several snRNP SM core proteins, CC including SNRPB, SNRPD1, SNRPD2, SNRPD3 and SNRPE (PubMed:18984161). CC Interacts with PPP4R2 (PubMed:12668731). {ECO:0000269|PubMed:12668731, CC ECO:0000269|PubMed:16314521, ECO:0000269|PubMed:17178713, CC ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:33963192}. CC -!- INTERACTION: CC P57678; P05187: ALPP; NbExp=3; IntAct=EBI-356700, EBI-1211484; CC P57678; Q8N715: CCDC185; NbExp=3; IntAct=EBI-356700, EBI-740814; CC P57678; P49368: CCT3; NbExp=3; IntAct=EBI-356700, EBI-356673; CC P57678; Q86Y33-5: CDC20B; NbExp=3; IntAct=EBI-356700, EBI-11983537; CC P57678; Q5T4B2: CERCAM; NbExp=3; IntAct=EBI-356700, EBI-12261896; CC P57678; P27918: CFP; NbExp=3; IntAct=EBI-356700, EBI-9038570; CC P57678; Q9UHI6: DDX20; NbExp=7; IntAct=EBI-356700, EBI-347658; CC P57678; Q9NXK8: FBXL12; NbExp=3; IntAct=EBI-356700, EBI-719790; CC P57678; O43593: HR; NbExp=3; IntAct=EBI-356700, EBI-2880706; CC P57678; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-356700, EBI-2556193; CC P57678; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-356700, EBI-11953846; CC P57678; Q3LI77: KRTAP13-4; NbExp=3; IntAct=EBI-356700, EBI-11953996; CC P57678; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-356700, EBI-11992140; CC P57678; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-356700, EBI-14065470; CC P57678; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-356700, EBI-1044640; CC P57678; O95711: LY86; NbExp=3; IntAct=EBI-356700, EBI-12203791; CC P57678; P16860: NPPB; NbExp=3; IntAct=EBI-356700, EBI-747044; CC P57678; P20618: PSMB1; NbExp=3; IntAct=EBI-356700, EBI-372273; CC P57678; O75127: PTCD1; NbExp=3; IntAct=EBI-356700, EBI-2560233; CC P57678; O75771: RAD51D; NbExp=3; IntAct=EBI-356700, EBI-1055693; CC P57678; O95977: S1PR4; NbExp=3; IntAct=EBI-356700, EBI-12194739; CC P57678; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-356700, EBI-742688; CC P57678; O43609: SPRY1; NbExp=4; IntAct=EBI-356700, EBI-3866665; CC P57678; Q03518: TAP1; NbExp=3; IntAct=EBI-356700, EBI-747259; CC P57678; Q9Y3C8: UFC1; NbExp=3; IntAct=EBI-356700, EBI-1045733; CC P57678; Q9Y4E8-2: USP15; NbExp=3; IntAct=EBI-356700, EBI-12041225; CC P57678; O75604: USP2; NbExp=3; IntAct=EBI-356700, EBI-743272; CC P57678; Q5BKZ1: ZNF326; NbExp=3; IntAct=EBI-356700, EBI-2560158; CC P57678; P13682: ZNF35; NbExp=3; IntAct=EBI-356700, EBI-11041653; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleolus. Nucleus, CC gem. Note=Localized in subnuclear structures next to coiled bodies, CC called gems, which are highly enriched in spliceosomal snRNPs and in CC the nucleolus. CC -!- DISEASE: Neurodevelopmental disorder with microcephaly, cataracts, and CC renal abnormalities (NEDMCR) [MIM:617913]: An autosomal recessive, CC severe neurodevelopmental disorder characterized by global CC developmental delay since infancy, microcephaly, poor or absent speech, CC and inability to walk or spasticity. Additional features include renal CC abnormalities, congenital cataracts, gastroesophageal reflux disease, CC seizures with onset in infancy or childhood, hyporeflexia, and non- CC specific white matter abnormalities on brain imaging. CC {ECO:0000269|PubMed:25558065, ECO:0000269|PubMed:30237576}. 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; AF173856; AAF35283.1; -; mRNA. DR EMBL; AC087392; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL080150; CAB45743.3; -; mRNA. DR EMBL; AL080167; CAB45755.1; -; mRNA. DR CCDS; CCDS45559.1; -. DR PIR; T12535; T12535. DR RefSeq; NP_056536.2; NM_015721.2. DR AlphaFoldDB; P57678; -. DR BioGRID; 119102; 282. DR ComplexPortal; CPX-6031; Survival motor neuron complex. DR CORUM; P57678; -. DR IntAct; P57678; 93. DR MINT; P57678; -. DR STRING; 9606.ENSP00000321706; -. DR BindingDB; P57678; -. DR ChEMBL; CHEMBL5169137; -. DR GlyGen; P57678; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P57678; -. DR PhosphoSitePlus; P57678; -. DR SwissPalm; P57678; -. DR BioMuta; GEMIN4; -. DR DMDM; 322510030; -. DR EPD; P57678; -. DR jPOST; P57678; -. DR MassIVE; P57678; -. DR MaxQB; P57678; -. DR PaxDb; 9606-ENSP00000321706; -. DR PeptideAtlas; P57678; -. DR ProteomicsDB; 57005; -. DR Pumba; P57678; -. DR Antibodypedia; 22646; 235 antibodies from 27 providers. DR DNASU; 50628; -. DR Ensembl; ENST00000319004.6; ENSP00000321706.5; ENSG00000179409.11. DR GeneID; 50628; -. DR KEGG; hsa:50628; -. DR MANE-Select; ENST00000319004.6; ENSP00000321706.5; NM_015721.3; NP_056536.2. DR UCSC; uc002frs.2; human. DR AGR; HGNC:15717; -. DR CTD; 50628; -. DR DisGeNET; 50628; -. DR GeneCards; GEMIN4; -. DR HGNC; HGNC:15717; GEMIN4. DR HPA; ENSG00000179409; Low tissue specificity. DR MalaCards; GEMIN4; -. DR MIM; 606969; gene. DR MIM; 617913; phenotype. DR neXtProt; NX_P57678; -. DR OpenTargets; ENSG00000179409; -. DR VEuPathDB; HostDB:ENSG00000179409; -. DR eggNOG; ENOG502QRX9; Eukaryota. DR GeneTree; ENSGT00390000012296; -. DR InParanoid; P57678; -. DR OMA; SCHNWLP; -. DR OrthoDB; 5401549at2759; -. DR PhylomeDB; P57678; -. DR TreeFam; TF329445; -. DR PathwayCommons; P57678; -. DR Reactome; R-HSA-191859; snRNP Assembly. DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery. DR SignaLink; P57678; -. DR SIGNOR; P57678; -. DR BioGRID-ORCS; 50628; 646 hits in 1161 CRISPR screens. DR ChiTaRS; GEMIN4; human. DR GeneWiki; GEMIN4; -. DR GenomeRNAi; 50628; -. DR Pharos; P57678; Tbio. DR PRO; PR:P57678; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P57678; Protein. DR Bgee; ENSG00000179409; Expressed in sperm and 179 other cell types or tissues. DR ExpressionAtlas; P57678; baseline and differential. DR GO; GO:0015030; C:Cajal body; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0097504; C:Gemini of coiled bodies; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; TAS:ProtInc. DR GO; GO:0032797; C:SMN complex; IDA:UniProtKB. DR GO; GO:0034719; C:SMN-Sm protein complex; IDA:UniProtKB. DR GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:MGI. DR GO; GO:0006364; P:rRNA processing; TAS:ProtInc. DR GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB. DR InterPro; IPR033265; GEMIN4. DR PANTHER; PTHR15571; GEM-ASSOCIATED PROTEIN 4; 1. DR PANTHER; PTHR15571:SF2; GEM-ASSOCIATED PROTEIN 4; 1. DR Genevisible; P57678; HS. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; Disease variant; mRNA processing; mRNA splicing; KW Nucleus; Phosphoprotein; Reference proteome. FT CHAIN 1..1058 FT /note="Gem-associated protein 4" FT /id="PRO_0000087459" FT REGION 714..735 FT /note="Leucine-zipper" FT /evidence="ECO:0000255" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 84 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 86 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 205 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VARIANT 105 FT /note="P -> L (in NEDMCR; uncertain significance)" FT /evidence="ECO:0000269|PubMed:30237576" FT /id="VAR_082144" FT VARIANT 182 FT /note="F -> L (in dbSNP:rs34604548)" FT /id="VAR_056891" FT VARIANT 502 FT /note="I -> V (in dbSNP:rs34616851)" FT /id="VAR_056892" FT VARIANT 579 FT /note="A -> G (in dbSNP:rs910925)" FT /id="VAR_024317" FT VARIANT 684 FT /note="R -> Q (in dbSNP:rs3744741)" FT /id="VAR_021971" FT VARIANT 739 FT /note="I -> T (in dbSNP:rs1062923)" FT /id="VAR_056893" FT VARIANT 749 FT /note="P -> L (in dbSNP:rs8078660)" FT /id="VAR_056894" FT VARIANT 782 FT /note="F -> L (in dbSNP:rs34452716)" FT /id="VAR_056895" FT VARIANT 818 FT /note="W -> R (in NEDMCR; uncertain significance; FT dbSNP:rs730882219)" FT /evidence="ECO:0000269|PubMed:25558065" FT /id="VAR_080610" FT VARIANT 824 FT /note="V -> F (in dbSNP:rs34936176)" FT /id="VAR_056896" FT VARIANT 913 FT /note="V -> I (in dbSNP:rs34610323)" FT /id="VAR_056897" FT VARIANT 1033 FT /note="R -> C (in dbSNP:rs7813)" FT /id="VAR_020390" FT CONFLICT 163 FT /note="V -> I (in Ref. 1; AAF35283)" FT /evidence="ECO:0000305" FT CONFLICT 450 FT /note="Q -> E (in Ref. 1; AAF35283 and 3; CAB45743)" FT /evidence="ECO:0000305" FT CONFLICT 593 FT /note="E -> V (in Ref. 1; AAF35283 and 3; CAB45743)" FT /evidence="ECO:0000305" FT CONFLICT 713 FT /note="Q -> P (in Ref. 1; AAF35283)" FT /evidence="ECO:0000305" FT CONFLICT 929 FT /note="D -> N (in Ref. 1; AAF35283 and 3; FT CAB45755/CAB45743)" FT /evidence="ECO:0000305" SQ SEQUENCE 1058 AA; 120037 MW; ACEC60EC19EF5081 CRC64; MDLGPLNICE EMTILHGGFL LAEQLFHPKA LAELTKSDWE RVGRPIVEAL REISSAAAHS QPFAWKKKAL IIIWAKVLQP HPVTPSDTET RWQEDLFFSV GNMIPTINHT ILFELLKSLE ASGLFIQLLM ALPTTICHAE LERFLEHVTV DTSAEDVAFF LDVWWEVMKH KGHPQDPLLS QFSAMAHKYL PALDEFPHPP KRLRSDPDAC PTMPLLAMLL RGLTQIQSRI LGPGRKCCAL ANLADMLTVF ALTEDDPQEV SATVYLDKLA TVISVWNSDT QNPYHQQALA EKVKEAERDV SLTSLAKLPS ETIFVGCEFL HHLLREWGEE LQAVLRSSQG TSYDSYRLCD SLTSFSQNAT LYLNRTSLSK EDRQVVSELA ECVRDFLRKT STVLKNRALE DITASIAMAV IQQKMDRHME VCYIFASEKK WAFSDEWVAC LGSNRALFRQ PDLVLRLLET VIDVSTADRA IPESQIRQVI HLILECYADL SLPGKNKVLA GILRSWGRKG LSEKLLAYVE GFQEDLNTTF NQLTQSASEQ GLAKAVASVA RLVIVHPEVT VKKMCSLAVV NLGTHKFLAQ ILTAFPALRF VEEQGPNSSA TFMVSCLKET VWMKFSTPKE EKQFLELLNC LMSPVKPQGI PVAALLEPDE VLKEFVLPFL RLDVEEVDLS LRIFIQTLEA NACREEYWLQ TCSPFPLLFS LCQLLDRFSK YWQLPKEKRC LSLDRKDLAI HILELLCEIV SANAETFSPD VWIKSLSWLH RKLEQLDWTV GLRLKSFFEG HFKCEVPATL FEICKLSEDE WTSQAHPGYG AGTGLLAWME CCCVSSGISE RMLSLLVVDV GNPEEVRLFS KGFLVALVQV MPWCSPQEWQ RLHQLTRRLL EKQLLHVPYS LEYIQFVPLL NLKPFAQELQ LSVLFLRTFQ FLCSHSCRDW LPLEGWNHVV KLLCGSLTRL LDSVRAIQAA GPWVQGPEQD LTQEALFVYT QVFCHALHIM AMLHPEVCEP LYVLALETLT CYETLSKTNP SVSSLLQRAH EQRFLKSIAE GIGPEERRQT LLQKMSSF //