ID DYHC1_HUMAN Reviewed; 4646 AA. AC Q14204; B0I1R0; Q6DKQ7; Q8WU28; Q92814; Q9Y4G5; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 04-JAN-2005, sequence version 5. DT 27-MAR-2024, entry version 226. DE RecName: Full=Cytoplasmic dynein 1 heavy chain 1; DE AltName: Full=Cytoplasmic dynein heavy chain 1; DE AltName: Full=Dynein heavy chain, cytosolic; GN Name=DYNC1H1 {ECO:0000312|HGNC:HGNC:2961}; GN Synonyms=DHC1, DNCH1, DNCL, DNECL, DYHC, KIAA0325; 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 [LARGE SCALE MRNA], AND VARIANT GLN-4029. RC TISSUE=Brain; RX PubMed=9205841; DOI=10.1093/dnares/4.2.141; RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. VII. The RT complete sequences of 100 new cDNA clones from brain which can code for RT large proteins in vitro."; RL DNA Res. 4:141-150(1997). RN [2] RP SEQUENCE REVISION. RA Ohara O., Nagase T., Kikuno R., Yamakawa H., Nomura N.; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Yamakawa H., Kikuno R.F., Nagase T., Ohara O.; RT "Multiplex amplification and cloning of 5'-ends of cDNA by ligase-free RT recombination: preparation of full-length cDNA clones encoding motor RT proteins."; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-3902 AND GLN-4029. RG NIEHS SNPs program; RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1130-2026. RX PubMed=8666668; DOI=10.1083/jcb.133.4.831; RA Vaisberg E.A., Grissom P.M., McIntosh J.R.; RT "Mammalian cells express three distinct dynein heavy chains that are RT localized to different cytoplasmic organelles."; RL J. Cell Biol. 133:831-842(1996). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1884-2024. RX PubMed=8227145; DOI=10.1083/jcb.123.4.849; RA Vaisberg E.A., Koonce M.P., McIntosh J.R.; RT "Cytoplasmic dynein plays a role in mammalian mitotic spindle formation."; RL J. Cell Biol. 123:849-858(1993). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3658-4646. RC TISSUE=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 [8] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4368, 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 [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1125; LYS-3480 AND LYS-4283, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] 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 [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-4162; THR-4366 AND RP SER-4368, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [19] RP FUNCTION. RX PubMed=27462074; DOI=10.1074/jbc.m116.724831; RA Chu X., Chen X., Wan Q., Zheng Z., Du Q.; RT "Nuclear mitotic apparatus (NuMA) interacts with and regulates astrin at RT the mitotic spindle."; RL J. Biol. Chem. 291:20055-20067(2016). RN [20] RP INTERACTION WITH CRACR2A. RX PubMed=31092558; DOI=10.1083/jcb.201810118; RA Miteva K.T., Pedicini L., Wilson L.A., Jayasinghe I., Slip R.G., RA Marszalek K., Gaunt H.J., Bartoli F., Deivasigamani S., Sobradillo D., RA Beech D.J., McKeown L.; RT "Rab46 integrates Ca2+ and histamine signaling to regulate selective cargo RT release from Weibel-Palade bodies."; RL J. Cell Biol. 218:2232-2246(2019). RN [21] {ECO:0007744|PDB:5OWO, ECO:0007744|PDB:6F1T, ECO:0007744|PDB:6F1U, ECO:0007744|PDB:6F1V, ECO:0007744|PDB:6F1Y, ECO:0007744|PDB:6F38, ECO:0007744|PDB:6F3A} RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 1-201, AND SUBUNIT. RX PubMed=29420470; DOI=10.1038/nature25462; RA Urnavicius L., Lau C.K., Elshenawy M.M., Morales-Rios E., Motz C., RA Yildiz A., Carter A.P.; RT "Cryo-EM shows how dynactin recruits two dyneins for faster movement."; RL Nature 554:202-206(2018). RN [22] {ECO:0007744|PDB:7Z8F, ECO:0007744|PDB:7Z8G, ECO:0007744|PDB:7Z8H, ECO:0007744|PDB:7Z8I, ECO:0007744|PDB:7Z8J, ECO:0007744|PDB:7Z8K, ECO:0007744|PDB:7Z8L} RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS), AND SUBUNIT. RX PubMed=36071160; DOI=10.1038/s41586-022-05186-y; RA Chaaban S., Carter A.P.; RT "Structure of dynein-dynactin on microtubules shows tandem adaptor RT binding."; RL Nature 610:212-216(2022). RN [23] RP VARIANT CDCBM13 PRO-3822. RX PubMed=21076407; DOI=10.1038/ng.712; RA Vissers L.E., de Ligt J., Gilissen C., Janssen I., Steehouwer M., RA de Vries P., van Lier B., Arts P., Wieskamp N., del Rosario M., RA van Bon B.W., Hoischen A., de Vries B.B., Brunner H.G., Veltman J.A.; RT "A de novo paradigm for mental retardation."; RL Nat. Genet. 42:1109-1112(2010). RN [24] RP VARIANT CMT2O ARG-306. RX PubMed=21820100; DOI=10.1016/j.ajhg.2011.07.002; RA Weedon M.N., Hastings R., Caswell R., Xie W., Paszkiewicz K., Antoniadi T., RA Williams M., King C., Greenhalgh L., Newbury-Ecob R., Ellard S.; RT "Exome sequencing identifies a DYNC1H1 mutation in a large pedigree with RT dominant axonal Charcot-Marie-Tooth disease."; RL Am. J. Hum. Genet. 89:308-312(2011). RN [25] RP VARIANT CDCBM13 LYS-1518. RX PubMed=22368300; DOI=10.1136/jmedgenet-2011-100542; RA Willemsen M.H., Vissers L.E., Willemsen M.A., van Bon B.W., Kroes T., RA de Ligt J., de Vries B.B., Schoots J., Lugtenberg D., Hamel B.C., RA van Bokhoven H., Brunner H.G., Veltman J.A., Kleefstra T.; RT "Mutations in DYNC1H1 cause severe intellectual disability with neuronal RT migration defects."; RL J. Med. Genet. 49:179-183(2012). RN [26] RP VARIANT SMALED1 ARG-306. RX PubMed=22847149; DOI=10.1007/s10048-012-0337-6; RA Tsurusaki Y., Saitoh S., Tomizawa K., Sudo A., Asahina N., Shiraishi H., RA Ito J.I., Tanaka H., Doi H., Saitsu H., Miyake N., Matsumoto N.; RT "A DYNC1H1 mutation causes a dominant spinal muscular atrophy with lower RT extremity predominance."; RL Neurogenetics 13:327-332(2012). RN [27] RP VARIANTS SMALED1 LEU-584; GLU-671 AND CYS-970, AND CHARACTERIZATION OF RP VARIANT SMALED1 LEU-584. RX PubMed=22459677; DOI=10.1212/wnl.0b013e3182556c05; RA Harms M.B., Ori-McKenney K.M., Scoto M., Tuck E.P., Bell S., Ma D., RA Masi S., Allred P., Al-Lozi M., Reilly M.M., Miller L.J., Jani-Acsadi A., RA Pestronk A., Shy M.E., Muntoni F., Vallee R.B., Baloh R.H.; RT "Mutations in the tail domain of DYNC1H1 cause dominant spinal muscular RT atrophy."; RL Neurology 78:1714-1720(2012). RN [28] RP VARIANT CDCBM13 LYS-1518, AND VARIANTS ALA-142; LEU-1250; MET-2247; RP CYS-4143; SER-4285; THR-4421; SER-4507 AND GLY-4603. RX PubMed=23033978; DOI=10.1056/nejmoa1206524; RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., RA Veltman J.A., Vissers L.E.; RT "Diagnostic exome sequencing in persons with severe intellectual RT disability."; RL N. Engl. J. Med. 367:1921-1929(2012). RN [29] RP VARIANTS CDCBM13 ILE-129; 659-THR--MET-662 DEL; GLN-1567; CYS-1962; RP THR-3241; ASN-3336; GLN-3344 AND GLN-3384, AND CHARACTERIZATION OF VARIANTS RP CDCBM13 ASN-3336 AND GLN-3384. RX PubMed=23603762; DOI=10.1038/ng.2613; RA Poirier K., Lebrun N., Broix L., Tian G., Saillour Y., Boscheron C., RA Parrini E., Valence S., Pierre B.S., Oger M., Lacombe D., Genevieve D., RA Fontana E., Darra F., Cances C., Barth M., Bonneau D., Bernadina B.D., RA N'guyen S., Gitiaux C., Parent P., des Portes V., Pedespan J.M., Legrez V., RA Castelnau-Ptakine L., Nitschke P., Hieu T., Masson C., Zelenika D., RA Andrieux A., Francis F., Guerrini R., Cowan N.J., Bahi-Buisson N., RA Chelly J.; RT "Mutations in TUBG1, DYNC1H1, KIF5C and KIF2A cause malformations of RT cortical development and microcephaly."; RL Nat. Genet. 45:639-647(2013). RN [30] RP VARIANT LYS-94, VARIANT SMALED1 LEU-264, VARIANT CMT2O CYS-598, RP CHARACTERIZATION OF VARIANT SMALED1 LEU-264, CHARACTERIZATION OF VARIANT RP CMT2O CYS-598, AND INTERACTION WITH BICD2. RX PubMed=25512093; DOI=10.1002/humu.22744; RA Peeters K., Bervoets S., Chamova T., Litvinenko I., De Vriendt E., RA Bichev S., Kancheva D., Mitev V., Kennerson M., Timmerman V., De Jonghe P., RA Tournev I., MacMillan J., Jordanova A.; RT "Novel mutations in the DYNC1H1 tail domain refine the genetic and clinical RT spectrum of dyneinopathies."; RL Hum. Mutat. 36:287-291(2015). RN [31] RP VARIANTS CMT2O ARG-1194 AND LYS-3048, AND CHARACTERIZATION OF VARIANTS RP CMT2O ARG-1194 AND LYS-3048. RX PubMed=24307404; DOI=10.1002/humu.22491; RA Fiorillo C., Moro F., Yi J., Weil S., Brisca G., Astrea G., Severino M., RA Romano A., Battini R., Rossi A., Minetti C., Bruno C., Santorelli F.M., RA Vallee R.; RT "Novel dynein DYNC1H1 neck and motor domain mutations link distal spinal RT muscular atrophy and abnormal cortical development."; RL Hum. Mutat. 35:298-302(2014). RN [32] RP VARIANT SMALED1 CYS-598. RX PubMed=25484024; DOI=10.1016/j.pediatrneurol.2014.09.003; RA Punetha J., Monges S., Franchi M.E., Hoffman E.P., Cirak S., Tesi-Rocha C.; RT "Exome Sequencing Identifies DYNC1H1 Variant Associated With Vertebral RT Abnormality and Spinal Muscular Atrophy With Lower Extremity RT Predominance."; RL Pediatr. Neurol. 52:239-244(2015). RN [33] RP VARIANT SMALED1 LEU-776. RX PubMed=26846447; DOI=10.1038/srep20423; RA Ding D., Chen Z., Li K., Long Z., Ye W., Tang Z., Xia K., Qiu R., Tang B., RA Jiang H.; RT "Identification of a de novo DYNC1H1 mutation via WES according to RT published guidelines."; RL Sci. Rep. 6:20423-20423(2016). RN [34] RP VARIANT SMALED1 GLU-1132, AND VARIANT CDCBM13 GLN-3384. RX PubMed=28193117; DOI=10.1177/0883073816683083; RA Chen Y., Xu Y., Li G., Li N., Yu T., Yao R.E., Wang X., Shen Y., Wang J.; RT "Exome Sequencing Identifies De Novo DYNC1H1 Mutations Associated With RT Distal Spinal Muscular Atrophy and Malformations of Cortical Development."; RL J. Child Neurol. 32:379-386(2017). CC -!- FUNCTION: Cytoplasmic dynein 1 acts as a motor for the intracellular CC retrograde motility of vesicles and organelles along microtubules. CC Dynein has ATPase activity; the force-producing power stroke is thought CC to occur on release of ADP. Plays a role in mitotic spindle assembly CC and metaphase plate congression (PubMed:27462074). CC {ECO:0000269|PubMed:27462074}. CC -!- SUBUNIT: Homodimer. The cytoplasmic dynein 1 complex consists of two CC catalytic heavy chains (HCs) and a number of non-catalytic subunits CC presented by intermediate chains (ICs), light intermediate chains CC (LICs) and light chains (LCs); the composition seems to vary in respect CC to the IC, LIC and LC composition. The heavy chain homodimer serves as CC a scaffold for the probable homodimeric assembly of the respective non- CC catalytic subunits. The ICs and LICs bind directly to the HC dimer and CC dynein LCs assemble on the IC dimer (PubMed:29420470, PubMed:36071160). CC Interacts with DYNC1LI1; DYNC1LI1 and DYNC1LI2 bind mutually exclusive CC to DYNC1H1. Interacts with DYNC1LI2; DYNC1LI1 and DYNC1LI2 bind CC mutually exclusive to DYNC1H1. Interacts with DYNC1I2 (By similarity). CC Interacts with BICD2 (PubMed:25512093). Interacts with isoform 2 of CC CRACR2A (PubMed:31092558). Interacts with DNALI1 (By similarity). CC {ECO:0000250|UniProtKB:P38650, ECO:0000250|UniProtKB:Q9JHU4, CC ECO:0000269|PubMed:25512093, ECO:0000269|PubMed:29420470, CC ECO:0000269|PubMed:31092558, ECO:0000269|PubMed:36071160}. CC -!- INTERACTION: CC Q14204; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-356015, EBI-2875816; CC Q14204; Q12797-6: ASPH; NbExp=3; IntAct=EBI-356015, EBI-12092171; CC Q14204; Q9Y6H3: ATP23; NbExp=3; IntAct=EBI-356015, EBI-12811889; CC Q14204; O95817: BAG3; NbExp=3; IntAct=EBI-356015, EBI-747185; CC Q14204; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-356015, EBI-745073; CC Q14204; Q7L1Q6-2: BZW1; NbExp=3; IntAct=EBI-356015, EBI-21557060; CC Q14204; P49336-2: CDK8; NbExp=3; IntAct=EBI-356015, EBI-11039720; CC Q14204; Q9Y281: CFL2; NbExp=3; IntAct=EBI-356015, EBI-351218; CC Q14204; Q86WV2: COX4I1; NbExp=3; IntAct=EBI-356015, EBI-10260134; CC Q14204; P26998: CRYBB3; NbExp=3; IntAct=EBI-356015, EBI-1965681; CC Q14204; P09668: CTSH; NbExp=3; IntAct=EBI-356015, EBI-6189940; CC Q14204; Q9BTE7: DCUN1D5; NbExp=3; IntAct=EBI-356015, EBI-3924013; CC Q14204; Q9NRI5: DISC1; NbExp=4; IntAct=EBI-356015, EBI-529989; CC Q14204; Q9Y6W6: DUSP10; NbExp=3; IntAct=EBI-356015, EBI-3443946; CC Q14204; Q13144: EIF2B5; NbExp=3; IntAct=EBI-356015, EBI-4401110; CC Q14204; Q7L5A8: FA2H; NbExp=3; IntAct=EBI-356015, EBI-11337888; CC Q14204; P24522: GADD45A; NbExp=3; IntAct=EBI-356015, EBI-448167; CC Q14204; B2RAF7: hCG_1818547; NbExp=3; IntAct=EBI-356015, EBI-25844370; CC Q14204; P42858: HTT; NbExp=8; IntAct=EBI-356015, EBI-466029; CC Q14204; Q14005-2: IL16; NbExp=3; IntAct=EBI-356015, EBI-17178971; CC Q14204; Q6DKI2: LGALS9C; NbExp=3; IntAct=EBI-356015, EBI-9088829; CC Q14204; Q99683: MAP3K5; NbExp=3; IntAct=EBI-356015, EBI-476263; CC Q14204; Q15759: MAPK11; NbExp=3; IntAct=EBI-356015, EBI-298304; CC Q14204; Q92886: NEUROG1; NbExp=3; IntAct=EBI-356015, EBI-10279647; CC Q14204; P20783-2: NTF3; NbExp=3; IntAct=EBI-356015, EBI-25844111; CC Q14204; P32243-2: OTX2; NbExp=3; IntAct=EBI-356015, EBI-9087860; CC Q14204; Q6P4D5-2: PABIR3; NbExp=3; IntAct=EBI-356015, EBI-9091052; CC Q14204; P19388: POLR2E; NbExp=3; IntAct=EBI-356015, EBI-395189; CC Q14204; O60237-2: PPP1R12B; NbExp=3; IntAct=EBI-356015, EBI-10700351; CC Q14204; Q96QH2: PRAM1; NbExp=3; IntAct=EBI-356015, EBI-2860740; CC Q14204; P49810: PSEN2; NbExp=3; IntAct=EBI-356015, EBI-2010251; CC Q14204; Q96DX8: RTP4; NbExp=3; IntAct=EBI-356015, EBI-12275482; CC Q14204; P48443: RXRG; NbExp=3; IntAct=EBI-356015, EBI-712405; CC Q14204; Q9BY12-3: SCAPER; NbExp=3; IntAct=EBI-356015, EBI-25837959; CC Q14204; Q5T0L3: SPATA46; NbExp=3; IntAct=EBI-356015, EBI-750105; CC Q14204; O60506-4: SYNCRIP; NbExp=3; IntAct=EBI-356015, EBI-11123832; CC Q14204; O15273: TCAP; NbExp=3; IntAct=EBI-356015, EBI-954089; CC Q14204; Q9BXU0: TEX12; NbExp=3; IntAct=EBI-356015, EBI-12090309; CC Q14204; O60830: TIMM17B; NbExp=3; IntAct=EBI-356015, EBI-2372529; CC Q14204; Q8IU80-2: TMPRSS6; NbExp=3; IntAct=EBI-356015, EBI-25839648; CC Q14204; Q8IUR5-4: TMTC1; NbExp=3; IntAct=EBI-356015, EBI-9089156; CC Q14204; Q9NX94: WBP1L; NbExp=3; IntAct=EBI-356015, EBI-10316321; CC Q14204; P61964: WDR5; NbExp=3; IntAct=EBI-356015, EBI-540834; CC Q14204; O00308: WWP2; NbExp=3; IntAct=EBI-356015, EBI-743923; CC Q14204; Q96EF9: ZHX1-C8orf76; NbExp=3; IntAct=EBI-356015, EBI-25830993; CC Q14204; Q96EJ4; NbExp=3; IntAct=EBI-356015, EBI-750454; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000305|PubMed:36071160}. CC -!- DOMAIN: Dynein heavy chains probably consist of an N-terminal stem CC (which binds cargo and interacts with other dynein components), and the CC head or motor domain. The motor contains six tandemly-linked AAA CC domains in the head, which form a ring. A stalk-like structure (formed CC by two of the coiled coil domains) protrudes between AAA 4 and AAA 5 CC and terminates in a microtubule-binding site. A seventh domain may also CC contribute to this ring; it is not clear whether the N-terminus or the CC C-terminus forms this extra domain. There are four well-conserved and CC two non-conserved ATPase sites, one per AAA domain. Probably only one CC of these (within AAA 1) actually hydrolyzes ATP, the others may serve a CC regulatory function. CC -!- DISEASE: Charcot-Marie-Tooth disease, axonal, 2O (CMT2O) [MIM:614228]: CC An axonal form of Charcot-Marie-Tooth disease, a disorder of the CC peripheral nervous system, characterized by progressive weakness and CC atrophy, initially of the peroneal muscles and later of the distal CC muscles of the arms. Charcot-Marie-Tooth disease is classified in two CC main groups on the basis of electrophysiologic properties and CC histopathology: primary peripheral demyelinating neuropathies CC (designated CMT1 when they are dominantly inherited) and primary CC peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group CC are characterized by signs of axonal degeneration in the absence of CC obvious myelin alterations, normal or slightly reduced nerve conduction CC velocities, and progressive distal muscle weakness and atrophy. CC {ECO:0000269|PubMed:21820100, ECO:0000269|PubMed:24307404, CC ECO:0000269|PubMed:25512093}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Cortical dysplasia, complex, with other brain malformations 13 CC (CDCBM13) [MIM:614563]: An autosomal dominant disorder characterized by CC global developmental delay with impaired intellectual development. Some CC patients show signs of peripheral neuropathy, such as abnormal gait and CC hyporeflexia. CDCBM13 is associated with variable neuronal migration CC defects resulting in cortical malformations. CC {ECO:0000269|PubMed:21076407, ECO:0000269|PubMed:22368300, CC ECO:0000269|PubMed:23033978, ECO:0000269|PubMed:23603762, CC ECO:0000269|PubMed:28193117}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Spinal muscular atrophy, lower extremity-predominant 1, CC autosomal dominant (SMALED1) [MIM:158600]: A form of spinal muscular CC atrophy, a neuromuscular disorder characterized by degeneration of the CC anterior horn cells of the spinal cord, leading to symmetrical muscle CC weakness and atrophy. SMALED1 is characterized by muscle weakness CC predominantly affecting the proximal lower extremities. CC {ECO:0000269|PubMed:22459677, ECO:0000269|PubMed:22847149, CC ECO:0000269|PubMed:25484024, ECO:0000269|PubMed:25512093, CC ECO:0000269|PubMed:26846447, ECO:0000269|PubMed:28193117}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA20783.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/dnch1/"; 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; AB002323; BAA20783.3; ALT_INIT; mRNA. DR EMBL; AB290157; BAG06711.1; -; mRNA. DR EMBL; AY682080; AAT74625.1; -; Genomic_DNA. DR EMBL; U53530; AAB09727.1; -; mRNA. DR EMBL; L23958; AAA16065.1; -; mRNA. DR EMBL; BC021297; AAH21297.2; -; mRNA. DR CCDS; CCDS9966.1; -. DR PIR; A49019; A49019. DR PIR; G02529; G02529. DR RefSeq; NP_001367.2; NM_001376.4. DR PDB; 5NUG; EM; 3.80 A; A/B=1-4646. DR PDB; 5OWO; X-ray; 1.79 A; A/B/C/D=1-201. DR PDB; 6F1T; EM; 3.50 A; e/f/m/n=1-1053. DR PDB; 6F1U; EM; 3.40 A; f/m/n=1-1186. DR PDB; 6F1V; EM; 3.40 A; f/m=1-1186. DR PDB; 6F1Y; EM; 3.40 A; f=780-927. DR PDB; 6F38; EM; 6.70 A; e/f/m/n=1-1455. DR PDB; 6F3A; EM; 8.20 A; e/f=1-1455. DR PDB; 7Z8F; EM; 20.00 A; e/f/m/n=1-4646. DR PDB; 7Z8G; EM; 3.52 A; A=1-4646. DR PDB; 7Z8H; EM; 3.41 A; A=1-4646. DR PDB; 7Z8I; EM; 3.30 A; f/m/n=1-4646. DR PDB; 7Z8J; EM; 3.93 A; f/m/n=1-4646. DR PDB; 7Z8K; EM; 4.37 A; e/f=1-4646. DR PDB; 7Z8L; EM; 4.90 A; f=1-4646. DR PDB; 8DYU; EM; 4.00 A; A=1320-4646. DR PDB; 8DYV; EM; 3.97 A; A=1320-4646. DR PDB; 8FCY; EM; 3.40 A; A=1458-3277, A=3412-4646. DR PDB; 8FD6; EM; 2.90 A; A=1458-3277, A=3412-4646. DR PDB; 8FDT; EM; 3.20 A; A=1458-3277, A=3412-4646. DR PDB; 8FDU; EM; 3.30 A; A=1458-3277, A=3412-4646. DR PDBsum; 5NUG; -. DR PDBsum; 5OWO; -. DR PDBsum; 6F1T; -. DR PDBsum; 6F1U; -. DR PDBsum; 6F1V; -. DR PDBsum; 6F1Y; -. DR PDBsum; 6F38; -. DR PDBsum; 6F3A; -. DR PDBsum; 7Z8F; -. DR PDBsum; 7Z8G; -. DR PDBsum; 7Z8H; -. DR PDBsum; 7Z8I; -. DR PDBsum; 7Z8J; -. DR PDBsum; 7Z8K; -. DR PDBsum; 7Z8L; -. DR PDBsum; 8DYU; -. DR PDBsum; 8DYV; -. DR PDBsum; 8FCY; -. DR PDBsum; 8FD6; -. DR PDBsum; 8FDT; -. DR PDBsum; 8FDU; -. DR BMRB; Q14204; -. DR EMDB; EMD-14549; -. DR EMDB; EMD-14550; -. DR EMDB; EMD-14551; -. DR EMDB; EMD-14552; -. DR EMDB; EMD-14553; -. DR EMDB; EMD-14555; -. DR EMDB; EMD-14556; -. DR EMDB; EMD-27782; -. DR EMDB; EMD-27783; -. DR EMDB; EMD-28999; -. DR EMDB; EMD-29003; -. DR EMDB; EMD-29012; -. DR EMDB; EMD-29014; -. DR EMDB; EMD-3698; -. DR EMDB; EMD-4168; -. DR EMDB; EMD-4169; -. DR EMDB; EMD-4170; -. DR EMDB; EMD-4171; -. DR EMDB; EMD-4177; -. DR SMR; Q14204; -. DR BioGRID; 108117; 453. DR ComplexPortal; CPX-5025; Cytoplasmic dynein complex, variant 1. DR CORUM; Q14204; -. DR DIP; DIP-37544N; -. DR IntAct; Q14204; 196. DR MINT; Q14204; -. DR STRING; 9606.ENSP00000348965; -. DR CarbonylDB; Q14204; -. DR GlyCosmos; Q14204; 5 sites, 2 glycans. DR GlyGen; Q14204; 6 sites, 2 O-linked glycans (6 sites). DR iPTMnet; Q14204; -. DR MetOSite; Q14204; -. DR PhosphoSitePlus; Q14204; -. DR SwissPalm; Q14204; -. DR BioMuta; DYNC1H1; -. DR DMDM; 57015308; -. DR EPD; Q14204; -. DR jPOST; Q14204; -. DR MassIVE; Q14204; -. DR MaxQB; Q14204; -. DR PaxDb; 9606-ENSP00000348965; -. DR PeptideAtlas; Q14204; -. DR PRIDE; Q14204; -. DR ProteomicsDB; 59927; -. DR Pumba; Q14204; -. DR Antibodypedia; 122; 168 antibodies from 28 providers. DR DNASU; 1778; -. DR Ensembl; ENST00000360184.10; ENSP00000348965.4; ENSG00000197102.14. DR GeneID; 1778; -. DR KEGG; hsa:1778; -. DR MANE-Select; ENST00000360184.10; ENSP00000348965.4; NM_001376.5; NP_001367.2. DR UCSC; uc001yks.3; human. DR AGR; HGNC:2961; -. DR CTD; 1778; -. DR DisGeNET; 1778; -. DR GeneCards; DYNC1H1; -. DR GeneReviews; DYNC1H1; -. DR HGNC; HGNC:2961; DYNC1H1. DR HPA; ENSG00000197102; Low tissue specificity. DR MalaCards; DYNC1H1; -. DR MIM; 158600; phenotype. DR MIM; 600112; gene. DR MIM; 614228; phenotype. DR MIM; 614563; phenotype. DR neXtProt; NX_Q14204; -. DR OpenTargets; ENSG00000197102; -. DR Orphanet; 284232; Autosomal dominant Charcot-Marie-Tooth disease type 2O. DR Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability. DR Orphanet; 209341; DYNC1H1-related autosomal dominant childhood-onset proximal spinal muscular atrophy. DR PharmGKB; PA27432; -. DR VEuPathDB; HostDB:ENSG00000197102; -. DR eggNOG; KOG3595; Eukaryota. DR GeneTree; ENSGT00940000156103; -. DR HOGENOM; CLU_000038_7_0_1; -. DR InParanoid; Q14204; -. DR OMA; NERQMTR; -. DR OrthoDB; 312195at2759; -. DR PhylomeDB; Q14204; -. DR TreeFam; TF101165; -. DR PathwayCommons; Q14204; -. DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-2467813; Separation of Sister Chromatids. DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion. DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition. DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand. DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes. DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes. DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome. DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes. DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane. DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport. DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic. DR Reactome; R-HSA-68877; Mitotic Prometaphase. DR Reactome; R-HSA-8854518; AURKA Activation by TPX2. DR Reactome; R-HSA-9609690; HCMV Early Events. DR Reactome; R-HSA-9646399; Aggrephagy. DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation. DR SignaLink; Q14204; -. DR SIGNOR; Q14204; -. DR BioGRID-ORCS; 1778; 817 hits in 1172 CRISPR screens. DR ChiTaRS; DYNC1H1; human. DR GeneWiki; DYNC1H1; -. DR GenomeRNAi; 1778; -. DR Pharos; Q14204; Tbio. DR PRO; PR:Q14204; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q14204; Protein. DR Bgee; ENSG00000197102; Expressed in cortical plate and 203 other cell types or tissues. DR ExpressionAtlas; Q14204; baseline and differential. DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC. DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome. DR GO; GO:0005938; C:cell cortex; IBA:GO_Central. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:GO_Central. DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0030286; C:dynein complex; IPI:ComplexPortal. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0030175; C:filopodium; IEA:Ensembl. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005874; C:microtubule; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0045505; F:dynein intermediate chain binding; IEA:InterPro. DR GO; GO:0051959; F:dynein light intermediate chain binding; IPI:FlyBase. DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central. DR GO; GO:0051293; P:establishment of spindle localization; IMP:CACAO. DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central. DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central. DR GO; GO:0033962; P:P-body assembly; ISS:BHF-UCL. DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab. DR GO; GO:0032388; P:positive regulation of intracellular transport; IMP:UniProtKB. DR GO; GO:1905832; P:positive regulation of spindle assembly; IMP:UniProtKB. DR GO; GO:0090235; P:regulation of metaphase plate congression; IMP:UniProtKB. DR GO; GO:0060236; P:regulation of mitotic spindle organization; IMP:UniProtKB. DR GO; GO:0008090; P:retrograde axonal transport; IBA:GO_Central. DR GO; GO:0034063; P:stress granule assembly; ISS:BHF-UCL. DR CDD; cd00009; AAA; 2. DR Gene3D; 1.10.287.2620; -; 1. DR Gene3D; 1.10.472.130; -; 1. DR Gene3D; 1.10.8.1220; -; 1. DR Gene3D; 1.10.8.710; -; 1. DR Gene3D; 1.20.1270.280; -; 1. DR Gene3D; 1.20.58.1120; -; 1. DR Gene3D; 1.20.920.20; -; 2. DR Gene3D; 1.20.920.30; -; 1. DR Gene3D; 1.20.920.60; -; 1. DR Gene3D; 3.10.490.20; -; 1. DR Gene3D; 6.10.140.1060; -; 1. DR Gene3D; 1.20.140.100; Dynein heavy chain, N-terminal domain 2; 1. DR Gene3D; 3.20.180.20; Dynein heavy chain, N-terminal domain 2; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 5. DR Gene3D; 1.10.8.720; Region D6 of dynein motor; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR035699; AAA_6. DR InterPro; IPR035706; AAA_9. DR InterPro; IPR041658; AAA_lid_11. DR InterPro; IPR042219; AAA_lid_11_sf. DR InterPro; IPR026983; DHC_fam. DR InterPro; IPR042222; Dynein_2_N. DR InterPro; IPR043157; Dynein_AAA1S. DR InterPro; IPR041466; Dynein_AAA5_ext. DR InterPro; IPR041228; Dynein_C. DR InterPro; IPR043160; Dynein_C_barrel. DR InterPro; IPR024743; Dynein_HC_stalk. DR InterPro; IPR024317; Dynein_heavy_chain_D4_dom. DR InterPro; IPR004273; Dynein_heavy_D6_P-loop. DR InterPro; IPR013602; Dynein_heavy_linker. DR InterPro; IPR013594; Dynein_heavy_tail. DR InterPro; IPR042228; Dynein_linker_3. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR46532:SF13; DYNEIN CYTOPLASMIC 1 HEAVY CHAIN 1; 1. DR PANTHER; PTHR46532; MALE FERTILITY FACTOR KL5; 1. DR Pfam; PF12774; AAA_6; 1. DR Pfam; PF12775; AAA_7; 1. DR Pfam; PF12780; AAA_8; 1. DR Pfam; PF12781; AAA_9; 1. DR Pfam; PF18198; AAA_lid_11; 1. DR Pfam; PF08385; DHC_N1; 1. DR Pfam; PF08393; DHC_N2; 1. DR Pfam; PF17852; Dynein_AAA_lid; 1. DR Pfam; PF18199; Dynein_C; 1. DR Pfam; PF03028; Dynein_heavy; 1. DR Pfam; PF12777; MT; 1. DR SMART; SM00382; AAA; 4. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4. DR Genevisible; Q14204; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division; KW Charcot-Marie-Tooth disease; Coiled coil; Cytoplasm; Cytoskeleton; KW Disease variant; Dynein; Intellectual disability; Microtubule; Mitosis; KW Motor protein; Neurodegeneration; Neuropathy; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Repeat; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22223895" FT CHAIN 2..4646 FT /note="Cytoplasmic dynein 1 heavy chain 1" FT /id="PRO_0000114627" FT REGION 53..1867 FT /note="Stem" FT /evidence="ECO:0000250" FT REGION 448..703 FT /note="Interaction with DYNC1I2" FT /evidence="ECO:0000250" FT REGION 651..802 FT /note="Interaction with DYNC1LI2" FT /evidence="ECO:0000250" FT REGION 1868..2099 FT /note="AAA 1" FT /evidence="ECO:0000250" FT REGION 2180..2452 FT /note="AAA 2" FT /evidence="ECO:0000250" FT REGION 2390..2411 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2556..2805 FT /note="AAA 3" FT /evidence="ECO:0000250" FT REGION 2899..3168 FT /note="AAA 4" FT /evidence="ECO:0000250" FT REGION 3189..3500 FT /note="Stalk" FT /evidence="ECO:0000250" FT REGION 3553..3782 FT /note="AAA 5" FT /evidence="ECO:0000250" FT REGION 4005..4221 FT /note="AAA 6" FT /evidence="ECO:0000250" FT COILED 181..202 FT /evidence="ECO:0000255" FT COILED 455..478 FT /evidence="ECO:0000255" FT COILED 543..566 FT /evidence="ECO:0000255" FT COILED 1171..1252 FT /evidence="ECO:0000255" FT COILED 1357..1373 FT /evidence="ECO:0000255" FT COILED 3189..3275 FT /evidence="ECO:0000255" FT COILED 3396..3500 FT /evidence="ECO:0000255" FT COILED 3737..3800 FT /evidence="ECO:0000255" FT COMPBIAS 2390..2408 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1906..1913 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT BINDING 2224..2231 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT BINDING 2595..2602 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT BINDING 2937..2944 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22223895" FT MOD_RES 70 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1125 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 1230 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JHU4" FT MOD_RES 3480 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 4162 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 4283 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 4366 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 4368 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT VARIANT 94 FT /note="E -> K (found in a patient with spinal muscular FT atrophy; uncertain significance)" FT /evidence="ECO:0000269|PubMed:25512093" FT /id="VAR_073155" FT VARIANT 129 FT /note="K -> I (in CDCBM13; dbSNP:rs1555407885)" FT /evidence="ECO:0000269|PubMed:23603762" FT /id="VAR_070580" FT VARIANT 142 FT /note="E -> A" FT /evidence="ECO:0000269|PubMed:23033978" FT /id="VAR_069437" FT VARIANT 264 FT /note="R -> L (in SMALED1; slight increased BICD2-binding; FT dbSNP:rs713993043)" FT /evidence="ECO:0000269|PubMed:25512093" FT /id="VAR_073156" FT VARIANT 306 FT /note="H -> R (in CMT2O and SMALED1; dbSNP:rs387906738)" FT /evidence="ECO:0000269|PubMed:21820100, FT ECO:0000269|PubMed:22847149" FT /id="VAR_066651" FT VARIANT 584 FT /note="I -> L (in SMALED1; disrupts dynein complex FT stability and function; dbSNP:rs387906741)" FT /evidence="ECO:0000269|PubMed:22459677" FT /id="VAR_067820" FT VARIANT 598 FT /note="R -> C (in CMT2O and SMALED1; slight increased FT BICD2-binding; dbSNP:rs587780564)" FT /evidence="ECO:0000269|PubMed:25484024, FT ECO:0000269|PubMed:25512093" FT /id="VAR_073157" FT VARIANT 659..662 FT /note="Missing (in CDCBM13)" FT /evidence="ECO:0000269|PubMed:23603762" FT /id="VAR_070581" FT VARIANT 671 FT /note="K -> E (in SMALED1; dbSNP:rs387906742)" FT /evidence="ECO:0000269|PubMed:22459677" FT /id="VAR_067821" FT VARIANT 776 FT /note="P -> L (in SMALED1; dbSNP:rs1057518083)" FT /evidence="ECO:0000269|PubMed:26846447" FT /id="VAR_078241" FT VARIANT 970 FT /note="Y -> C (in SMALED1; dbSNP:rs387906743)" FT /evidence="ECO:0000269|PubMed:22459677" FT /id="VAR_067822" FT VARIANT 1132 FT /note="G -> E (in SMALED1)" FT /evidence="ECO:0000269|PubMed:28193117" FT /id="VAR_078242" FT VARIANT 1194 FT /note="Q -> R (in CMT2O; impairs function; FT dbSNP:rs1555408964)" FT /evidence="ECO:0000269|PubMed:24307404" FT /id="VAR_072092" FT VARIANT 1250 FT /note="V -> L (in dbSNP:rs369914512)" FT /evidence="ECO:0000269|PubMed:23033978" FT /id="VAR_069438" FT VARIANT 1518 FT /note="E -> K (in CDCBM13; dbSNP:rs387906740)" FT /evidence="ECO:0000269|PubMed:22368300, FT ECO:0000269|PubMed:23033978" FT /id="VAR_067823" FT VARIANT 1567 FT /note="R -> Q (in CDCBM13; dbSNP:rs797044901)" FT /evidence="ECO:0000269|PubMed:23603762" FT /id="VAR_070582" FT VARIANT 1962 FT /note="R -> C (in CDCBM13; dbSNP:rs879253881)" FT /evidence="ECO:0000269|PubMed:23603762" FT /id="VAR_070583" FT VARIANT 2247 FT /note="V -> M (in dbSNP:rs1064796963)" FT /evidence="ECO:0000269|PubMed:23033978" FT /id="VAR_069439" FT VARIANT 3048 FT /note="E -> K (in CMT2O; impairs function; FT dbSNP:rs1555410941)" FT /evidence="ECO:0000269|PubMed:24307404" FT /id="VAR_072093" FT VARIANT 3241 FT /note="K -> T (in CDCBM13; dbSNP:rs1555411145)" FT /evidence="ECO:0000269|PubMed:23603762" FT /id="VAR_070584" FT VARIANT 3336 FT /note="K -> N (in CDCBM13; shows a substantial reduction in FT the microtubule binding affinity compared to the wild-type FT control protein; dbSNP:rs397509410)" FT /evidence="ECO:0000269|PubMed:23603762" FT /id="VAR_070585" FT VARIANT 3344 FT /note="R -> Q (in CDCBM13; dbSNP:rs397509412)" FT /evidence="ECO:0000269|PubMed:23603762" FT /id="VAR_070586" FT VARIANT 3384 FT /note="R -> Q (in CDCBM13; shows a substantial reduction in FT the microtubule binding affinity compared to the wild-type FT control protein; dbSNP:rs397509411)" FT /evidence="ECO:0000269|PubMed:23603762, FT ECO:0000269|PubMed:28193117" FT /id="VAR_070587" FT VARIANT 3822 FT /note="H -> P (in CDCBM13; dbSNP:rs387906739)" FT /evidence="ECO:0000269|PubMed:21076407" FT /id="VAR_065085" FT VARIANT 3902 FT /note="D -> N (in dbSNP:rs17512818)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_020889" FT VARIANT 4029 FT /note="H -> Q (in dbSNP:rs10129889)" FT /evidence="ECO:0000269|PubMed:9205841, ECO:0000269|Ref.4" FT /id="VAR_020890" FT VARIANT 4143 FT /note="R -> C (in dbSNP:rs1316357429)" FT /evidence="ECO:0000269|PubMed:23033978" FT /id="VAR_069440" FT VARIANT 4285 FT /note="A -> S (in dbSNP:rs749486351)" FT /evidence="ECO:0000269|PubMed:23033978" FT /id="VAR_069441" FT VARIANT 4421 FT /note="A -> T (in dbSNP:rs376492799)" FT /evidence="ECO:0000269|PubMed:23033978" FT /id="VAR_069442" FT VARIANT 4507 FT /note="I -> S" FT /evidence="ECO:0000269|PubMed:23033978" FT /id="VAR_069443" FT VARIANT 4603 FT /note="S -> G" FT /evidence="ECO:0000269|PubMed:23033978" FT /id="VAR_069444" FT CONFLICT 1778..1779 FT /note="LH -> SD (in Ref. 5; AAB09727)" FT /evidence="ECO:0000305" FT CONFLICT 1941 FT /note="M -> R (in Ref. 5; AAB09727)" FT /evidence="ECO:0000305" FT CONFLICT 2025 FT /note="R -> N (in Ref. 5; AAB09727)" FT /evidence="ECO:0000305" FT HELIX 27..41 FT /evidence="ECO:0007829|PDB:5OWO" FT STRAND 42..47 FT /evidence="ECO:0007829|PDB:5OWO" FT HELIX 50..57 FT /evidence="ECO:0007829|PDB:5OWO" FT HELIX 59..70 FT /evidence="ECO:0007829|PDB:5OWO" FT STRAND 71..73 FT /evidence="ECO:0007829|PDB:6F1T" FT STRAND 76..85 FT /evidence="ECO:0007829|PDB:5OWO" FT STRAND 97..105 FT /evidence="ECO:0007829|PDB:5OWO" FT STRAND 113..124 FT /evidence="ECO:0007829|PDB:5OWO" FT HELIX 132..134 FT /evidence="ECO:0007829|PDB:5OWO" FT STRAND 135..140 FT /evidence="ECO:0007829|PDB:5OWO" FT HELIX 145..155 FT /evidence="ECO:0007829|PDB:5OWO" FT HELIX 157..165 FT /evidence="ECO:0007829|PDB:5OWO" FT HELIX 178..199 FT /evidence="ECO:0007829|PDB:5OWO" FT HELIX 211..222 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 229..237 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 239..260 FT /evidence="ECO:0007829|PDB:7Z8I" FT STRAND 266..269 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 271..292 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 295..306 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 310..318 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 322..332 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 333..335 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 341..345 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 350..364 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 365..368 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 374..399 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 401..403 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 406..440 FT /evidence="ECO:0007829|PDB:7Z8I" FT TURN 442..444 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 456..484 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 514..532 FT /evidence="ECO:0007829|PDB:7Z8I" FT TURN 534..537 FT /evidence="ECO:0007829|PDB:6F1U" FT HELIX 540..574 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 578..587 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 590..592 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 597..603 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 605..624 FT /evidence="ECO:0007829|PDB:7Z8I" FT TURN 627..629 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 631..638 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 643..669 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 673..675 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 677..692 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 696..709 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 711..714 FT /evidence="ECO:0007829|PDB:6F1T" FT STRAND 715..723 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 729..731 FT /evidence="ECO:0007829|PDB:6F1T" FT STRAND 732..738 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 741..753 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 754..756 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 762..797 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 799..805 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 806..820 FT /evidence="ECO:0007829|PDB:7Z8I" FT STRAND 826..828 FT /evidence="ECO:0007829|PDB:6F1V" FT HELIX 829..865 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 871..890 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 896..913 FT /evidence="ECO:0007829|PDB:7Z8I" FT TURN 992..995 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 999..1002 FT /evidence="ECO:0007829|PDB:6F1T" FT TURN 1009..1011 FT /evidence="ECO:0007829|PDB:6F1T" FT HELIX 1014..1017 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 1020..1024 FT /evidence="ECO:0007829|PDB:7Z8I" FT HELIX 1033..1050 FT /evidence="ECO:0007829|PDB:6F1T" FT HELIX 1464..1470 FT /evidence="ECO:0007829|PDB:8FCY" FT STRAND 1477..1479 FT /evidence="ECO:0007829|PDB:8FCY" FT STRAND 1485..1487 FT /evidence="ECO:0007829|PDB:8FCY" FT TURN 1492..1494 FT /evidence="ECO:0007829|PDB:8FCY" FT HELIX 1495..1509 FT /evidence="ECO:0007829|PDB:8FCY" FT STRAND 1514..1516 FT /evidence="ECO:0007829|PDB:8FCY" FT HELIX 1544..1551 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 1556..1559 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 1563..1568 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 1590..1592 FT /evidence="ECO:0007829|PDB:8FCY" FT HELIX 1608..1625 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 1627..1631 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 1634..1642 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 1647..1652 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 1654..1657 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 1658..1666 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 1672..1678 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 1679..1681 FT /evidence="ECO:0007829|PDB:8FCY" FT STRAND 1683..1691 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 1692..1694 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 1698..1728 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 1735..1744 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 1747..1768 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 1771..1773 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 1778..1797 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 1802..1828 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 1836..1839 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 1843..1846 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 1852..1854 FT /evidence="ECO:0007829|PDB:8FDT" FT STRAND 1856..1860 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 1865..1867 FT /evidence="ECO:0007829|PDB:8FCY" FT HELIX 1883..1896 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 1897..1899 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 1901..1905 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 1907..1911 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 1912..1922 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 1927..1931 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 1933..1935 FT /evidence="ECO:0007829|PDB:8FCY" FT HELIX 1938..1951 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 1954..1959 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 1960..1962 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 1965..1982 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 1983..1986 FT /evidence="ECO:0007829|PDB:8FCY" FT STRAND 1988..1990 FT /evidence="ECO:0007829|PDB:7Z8H" FT HELIX 1992..1994 FT /evidence="ECO:0007829|PDB:7Z8H" FT STRAND 1998..2007 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2013..2018 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2030..2033 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2036..2040 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2046..2057 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2062..2079 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2090..2113 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2124..2129 FT /evidence="ECO:0007829|PDB:7Z8H" FT HELIX 2133..2144 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2146..2148 FT /evidence="ECO:0007829|PDB:8FDT" FT HELIX 2151..2153 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2154..2164 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2176..2188 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2195..2198 FT /evidence="ECO:0007829|PDB:8FCY" FT HELIX 2201..2216 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2218..2223 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2226..2229 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2230..2245 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2249..2254 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 2256..2258 FT /evidence="ECO:0007829|PDB:8FDT" FT HELIX 2261..2265 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2266..2268 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 2270..2272 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2275..2277 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2279..2288 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 2290..2292 FT /evidence="ECO:0007829|PDB:7Z8H" FT HELIX 2294..2296 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2297..2305 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 2309..2311 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2313..2315 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 2316..2318 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2324..2326 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 2328..2330 FT /evidence="ECO:0007829|PDB:8FCY" FT STRAND 2332..2334 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2339..2346 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2353..2358 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2359..2363 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 2366..2368 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2371..2383 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 2387..2395 FT /evidence="ECO:0007829|PDB:7Z8H" FT HELIX 2396..2399 FT /evidence="ECO:0007829|PDB:7Z8H" FT HELIX 2411..2423 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2424..2426 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2428..2430 FT /evidence="ECO:0007829|PDB:8FCY" FT HELIX 2432..2440 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2451..2475 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2477..2479 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2483..2503 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2508..2521 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2530..2532 FT /evidence="ECO:0007829|PDB:8FDT" FT HELIX 2534..2536 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2537..2539 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 2541..2543 FT /evidence="ECO:0007829|PDB:8FCY" FT STRAND 2545..2547 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2548..2551 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2559..2561 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2572..2586 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2591..2594 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2601..2611 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2612..2614 FT /evidence="ECO:0007829|PDB:7Z8H" FT STRAND 2615..2621 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2628..2638 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2641..2643 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2645..2651 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2658..2665 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 2673..2675 FT /evidence="ECO:0007829|PDB:8FDU" FT HELIX 2678..2688 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2689..2693 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 2695..2697 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2700..2712 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2725..2728 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2733..2735 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2741..2755 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2756..2758 FT /evidence="ECO:0007829|PDB:8FDT" FT TURN 2760..2762 FT /evidence="ECO:0007829|PDB:8FCY" FT HELIX 2763..2765 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2766..2783 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 2786..2788 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2796..2810 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2818..2833 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2834..2836 FT /evidence="ECO:0007829|PDB:8FDT" FT HELIX 2840..2857 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2859..2861 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2863..2866 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 2868..2870 FT /evidence="ECO:0007829|PDB:8FCY" FT STRAND 2873..2880 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2886..2903 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2913..2927 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2932..2937 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2943..2954 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 2957..2960 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2969..2984 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 2985..2987 FT /evidence="ECO:0007829|PDB:8FCY" FT STRAND 2990..2995 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 2996..2998 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3002..3014 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3024..3040 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3047..3060 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 3063..3068 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 3072..3074 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3075..3081 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3083..3085 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 3088..3096 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3099..3110 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3139..3163 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3173..3219 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3473..3501 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3503..3516 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 3517..3520 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3522..3538 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3549..3552 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3556..3564 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3571..3581 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 3587..3590 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 3592..3594 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3595..3603 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 3604..3608 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 3610..3616 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3619..3629 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 3633..3636 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3638..3640 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3643..3645 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3646..3650 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 3654..3656 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 3659..3664 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 3667..3670 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 3677..3682 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3690..3693 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 3696..3700 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3705..3720 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3722..3755 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 3759..3761 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3763..3786 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3789..3798 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3802..3817 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 3818..3821 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3829..3841 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3844..3846 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3852..3872 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3877..3879 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3880..3893 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 3895..3898 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3902..3910 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3911..3913 FT /evidence="ECO:0007829|PDB:8FCY" FT HELIX 3929..3938 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 3943..3946 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3947..3952 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3956..3961 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3966..3968 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3982..3996 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 3998..4000 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 4001..4012 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 4018..4022 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 4027..4033 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4037..4039 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4041..4045 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 4052..4061 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4066..4070 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 4073..4075 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 4076..4088 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4093..4097 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 4098..4100 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 4103..4113 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4123..4129 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 4136..4141 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4142..4147 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 4152..4163 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 4166..4170 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4171..4173 FT /evidence="ECO:0007829|PDB:8FDT" FT HELIX 4175..4192 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 4194..4196 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 4197..4199 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4200..4203 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 4209..4226 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4227..4229 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 4235..4237 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 4240..4244 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 4246..4249 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4252..4255 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 4259..4272 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 4275..4277 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4278..4281 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4283..4287 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4288..4291 FT /evidence="ECO:0007829|PDB:8FDT" FT HELIX 4302..4310 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 4318..4321 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 4325..4327 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 4329..4346 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 4376..4390 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 4402..4406 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 4408..4438 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 4446..4456 FT /evidence="ECO:0007829|PDB:8FD6" FT TURN 4462..4464 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 4475..4498 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4500..4507 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4509..4511 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 4517..4531 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4536..4538 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4540..4545 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4557..4561 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4563..4568 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4571..4575 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4579..4581 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4583..4585 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4588..4593 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4604..4614 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4618..4626 FT /evidence="ECO:0007829|PDB:8FD6" FT HELIX 4632..4637 FT /evidence="ECO:0007829|PDB:8FD6" FT STRAND 4641..4643 FT /evidence="ECO:0007829|PDB:8FCY" SQ SEQUENCE 4646 AA; 532408 MW; D4D4E15DFBDE4797 CRC64; MSEPGGGGGE DGSAGLEVSA VQNVADVSVL QKHLRKLVPL LLEDGGEAPA ALEAALEEKS ALEQMRKFLS DPQVHTVLVE RSTLKEDVGD EGEEEKEFIS YNINIDIHYG VKSNSLAFIK RTPVIDADKP VSSQLRVLTL SEDSPYETLH SFISNAVAPF FKSYIRESGK ADRDGDKMAP SVEKKIAELE MGLLHLQQNI EIPEISLPIH PMITNVAKQC YERGEKPKVT DFGDKVEDPT FLNQLQSGVN RWIREIQKVT KLDRDPASGT ALQEISFWLN LERALYRIQE KRESPEVLLT LDILKHGKRF HATVSFDTDT GLKQALETVN DYNPLMKDFP LNDLLSATEL DKIRQALVAI FTHLRKIRNT KYPIQRALRL VEAISRDLSS QLLKVLGTRK LMHVAYEEFE KVMVACFEVF QTWDDEYEKL QVLLRDIVKR KREENLKMVW RINPAHRKLQ ARLDQMRKFR RQHEQLRAVI VRVLRPQVTA VAQQNQGEVP EPQDMKVAEV LFDAADANAI EEVNLAYENV KEVDGLDVSK EGTEAWEAAM KRYDERIDRV ETRITARLRD QLGTAKNANE MFRIFSRFNA LFVRPHIRGA IREYQTQLIQ RVKDDIESLH DKFKVQYPQS QACKMSHVRD LPPVSGSIIW AKQIDRQLTA YMKRVEDVLG KGWENHVEGQ KLKQDGDSFR MKLNTQEIFD DWARKVQQRN LGVSGRIFTI ESTRVRGRTG NVLKLKVNFL PEIITLSKEV RNLKWLGFRV PLAIVNKAHQ ANQLYPFAIS LIESVRTYER TCEKVEERNT ISLLVAGLKK EVQALIAEGI ALVWESYKLD PYVQRLAETV FNFQEKVDDL LIIEEKIDLE VRSLETCMYD HKTFSEILNR VQKAVDDLNL HSYSNLPIWV NKLDMEIERI LGVRLQAGLR AWTQVLLGQA EDKAEVDMDT DAPQVSHKPG GEPKIKNVVH ELRITNQVIY LNPPIEECRY KLYQEMFAWK MVVLSLPRIQ SQRYQVGVHY ELTEEEKFYR NALTRMPDGP VALEESYSAV MGIVSEVEQY VKVWLQYQCL WDMQAENIYN RLGEDLNKWQ ALLVQIRKAR GTFDNAETKK EFGPVVIDYG KVQSKVNLKY DSWHKEVLSK FGQMLGSNMT EFHSQISKSR QELEQHSVDT ASTSDAVTFI TYVQSLKRKI KQFEKQVELY RNGQRLLEKQ RFQFPPSWLY IDNIEGEWGA FNDIMRRKDS AIQQQVANLQ MKIVQEDRAV ESRTTDLLTD WEKTKPVTGN LRPEEALQAL TIYEGKFGRL KDDREKCAKA KEALELTDTG LLSGSEERVQ VALEELQDLK GVWSELSKVW EQIDQMKEQP WVSVQPRKLR QNLDALLNQL KSFPARLRQY ASYEFVQRLL KGYMKINMLV IELKSEALKD RHWKQLMKRL HVNWVVSELT LGQIWDVDLQ KNEAIVKDVL LVAQGEMALE EFLKQIREVW NTYELDLVNY QNKCRLIRGW DDLFNKVKEH INSVSAMKLS PYYKVFEEDA LSWEDKLNRI MALFDVWIDV QRRWVYLEGI FTGSADIKHL LPVETQRFQS ISTEFLALMK KVSKSPLVMD VLNIQGVQRS LERLADLLGK IQKALGEYLE RERSSFPRFY FVGDEDLLEI IGNSKNVAKL QKHFKKMFAG VSSIILNEDN SVVLGISSRE GEEVMFKTPV SITEHPKINE WLTLVEKEMR VTLAKLLAES VTEVEIFGKA TSIDPNTYIT WIDKYQAQLV VLSAQIAWSE NVETALSSMG GGGDAAPLHS VLSNVEVTLN VLADSVLMEQ PPLRRRKLEH LITELVHQRD VTRSLIKSKI DNAKSFEWLS QMRFYFDPKQ TDVLQQLSIQ MANAKFNYGF EYLGVQDKLV QTPLTDRCYL TMTQALEARL GGSPFGPAGT GKTESVKALG HQLGRFVLVF NCDETFDFQA MGRIFVGLCQ VGAWGCFDEF NRLEERMLSA VSQQVQCIQE ALREHSNPNY DKTSAPITCE LLNKQVKVSP DMAIFITMNP GYAGRSNLPD NLKKLFRSLA MTKPDRQLIA QVMLYSQGFR TAEVLANKIV PFFKLCDEQL SSQSHYDFGL RALKSVLVSA GNVKRERIQK IKREKEERGE AVDEGEIAEN LPEQEILIQS VCETMVPKLV AEDIPLLFSL LSDVFPGVQY HRGEMTALRE ELKKVCQEMY LTYGDGEEVG GMWVEKVLQL YQITQINHGL MMVGPSGSGK SMAWRVLLKA LERLEGVEGV AHIIDPKAIS KDHLYGTLDP NTREWTDGLF THVLRKIIDS VRGELQKRQW IVFDGDVDPE WVENLNSVLD DNKLLTLPNG ERLSLPPNVR IMFEVQDLKY ATLATVSRCG MVWFSEDVLS TDMIFNNFLA RLRSIPLDEG EDEAQRRRKG KEDEGEEAAS PMLQIQRDAA TIMQPYFTSN GLVTKALEHA FQLEHIMDLT RLRCLGSLFS MLHQACRNVA QYNANHPDFP MQIEQLERYI QRYLVYAILW SLSGDSRLKM RAELGEYIRR ITTVPLPTAP NIPIIDYEVS ISGEWSPWQA KVPQIEVETH KVAAPDVVVP TLDTVRHEAL LYTWLAEHKP LVLCGPPGSG KTMTLFSALR ALPDMEVVGL NFSSATTPEL LLKTFDHYCE YRRTPNGVVL APVQLGKWLV LFCDEINLPD MDKYGTQRVI SFIRQMVEHG GFYRTSDQTW VKLERIQFVG ACNPPTDPGR KPLSHRFLRH VPVVYVDYPG PASLTQIYGT FNRAMLRLIP SLRTYAEPLT AAMVEFYTMS QERFTQDTQP HYIYSPREMT RWVRGIFEAL RPLETLPVEG LIRIWAHEAL RLFQDRLVED EERRWTDENI DTVALKHFPN IDREKAMSRP ILYSNWLSKD YIPVDQEELR DYVKARLKVF YEEELDVPLV LFNEVLDHVL RIDRIFRQPQ GHLLLIGVSG AGKTTLSRFV AWMNGLSVYQ IKVHRKYTGE DFDEDLRTVL RRSGCKNEKI AFIMDESNVL DSGFLERMNT LLANGEVPGL FEGDEYATLM TQCKEGAQKE GLMLDSHEEL YKWFTSQVIR NLHVVFTMNP SSEGLKDRAA TSPALFNRCV LNWFGDWSTE ALYQVGKEFT SKMDLEKPNY IVPDYMPVVY DKLPQPPSHR EAIVNSCVFV HQTLHQANAR LAKRGGRTMA ITPRHYLDFI NHYANLFHEK RSELEEQQMH LNVGLRKIKE TVDQVEELRR DLRIKSQELE VKNAAANDKL KKMVKDQQEA EKKKVMSQEI QEQLHKQQEV IADKQMSVKE DLDKVEPAVI EAQNAVKSIK KQHLVEVRSM ANPPAAVKLA LESICLLLGE STTDWKQIRS IIMRENFIPT IVNFSAEEIS DAIREKMKKN YMSNPSYNYE IVNRASLACG PMVKWAIAQL NYADMLKRVE PLRNELQKLE DDAKDNQQKA NEVEQMIRDL EASIARYKEE YAVLISEAQA IKADLAAVEA KVNRSTALLK SLSAERERWE KTSETFKNQM STIAGDCLLS AAFIAYAGYF DQQMRQNLFT TWSHHLQQAN IQFRTDIART EYLSNADERL RWQASSLPAD DLCTENAIML KRFNRYPLII DPSGQATEFI MNEYKDRKIT RTSFLDDAFR KNLESALRFG NPLLVQDVES YDPVLNPVLN REVRRTGGRV LITLGDQDID LSPSFVIFLS TRDPTVEFPP DLCSRVTFVN FTVTRSSLQS QCLNEVLKAE RPDVDEKRSD LLKLQGEFQL RLRQLEKSLL QALNEVKGRI LDDDTIITTL ENLKREAAEV TRKVEETDIV MQEVETVSQQ YLPLSTACSS IYFTMESLKQ IHFLYQYSLQ FFLDIYHNVL YENPNLKGVT DHTQRLSIIT KDLFQVAFNR VARGMLHQDH ITFAMLLARI KLKGTVGEPT YDAEFQHFLR GNEIVLSAGS TPRIQGLTVE QAEAVVRLSC LPAFKDLIAK VQADEQFGIW LDSSSPEQTV PYLWSEETPA TPIGQAIHRL LLIQAFRPDR LLAMAHMFVS TNLGESFMSI MEQPLDLTHI VGTEVKPNTP VLMCSVPGYD ASGHVEDLAA EQNTQITSIA IGSAEGFNQA DKAINTAVKS GRWVMLKNVH LAPGWLMQLE KKLHSLQPHA CFRLFLTMEI NPKVPVNLLR AGRIFVFEPP PGVKANMLRT FSSIPVSRIC KSPNERARLY FLLAWFHAII QERLRYAPLG WSKKYEFGES DLRSACDTVD TWLDDTAKGR QNISPDKIPW SALKTLMAQS IYGGRVDNEF DQRLLNTFLE RLFTTRSFDS EFKLACKVDG HKDIQMPDGI RREEFVQWVE LLPDTQTPSW LGLPNNAERV LLTTQGVDMI SKMLKMQMLE DEDDLAYAET EKKTRTDSTS DGRPAWMRTL HTTASNWLHL IPQTLSHLKR TVENIKDPLF RFFEREVKMG AKLLQDVRQD LADVVQVCEG KKKQTNYLRT LINELVKGIL PRSWSHYTVP AGMTVIQWVS DFSERIKQLQ NISLAAASGG AKELKNIHVC LGGLFVPEAY ITATRQYVAQ ANSWSLEELC LEVNVTTSQG ATLDACSFGV TGLKLQGATC NNNKLSLSNA ISTALPLTQL RWVKQTNTEK KASVVTLPVY LNFTRADLIF TVDFEIATKE DPRSFYERGV AVLCTE //