DYHC1_MOUSE
ID DYHC1_MOUSE Reviewed; 4644 AA.
AC Q9JHU4; E9QM71;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 189.
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; Synonyms=Dhc1, Dnch1, Dnchc1, Dyhc;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=FVB/NJ;
RA Sasaki S., Shionoya A., Hirotsune S.;
RT "Complete cDNA sequence of murine cytoplasmic dynein heavy chain.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP INVOLVEMENT IN MOTOR NEURON DEGENERATION, VARIANT LOA TYR-580, AND VARIANT
RP CRA1 CYS-1055.
RX PubMed=12730604; DOI=10.1126/science.1083129;
RA Hafezparast M., Klocke R., Ruhrberg C., Marquardt A., Ahmad-Annuar A.,
RA Bowen S., Lalli G., Witherden A.S., Hummerich H., Nicholson S.,
RA Morgan P.J., Oozageer R., Priestley J.V., Averill S., King V.R., Ball S.,
RA Peters J., Toda T., Yamamoto A., Hiraoka Y., Augustin M., Korthaus D.,
RA Wattler S., Wabnitz P., Dickneite C., Lampel S., Boehme F., Peraus G.,
RA Popp A., Rudelius M., Schlegel J., Fuchs H., de Angelis M.H., Schiavo G.,
RA Shima D.T., Russ A.P., Stumm G., Martin J.E., Fisher E.M.C.;
RT "Mutations in dynein link motor neuron degeneration to defects in
RT retrograde transport.";
RL Science 300:808-812(2003).
RN [4]
RP INTERACTION WITH DNALI1.
RX PubMed=16496424; DOI=10.1002/mrd.20475;
RA Rashid S., Breckle R., Hupe M., Geisler S., Doerwald N., Neesen J.;
RT "The murine Dnali1 gene encodes a flagellar protein that interacts with the
RT cytoplasmic dynein heavy chain 1.";
RL Mol. Reprod. Dev. 73:784-794(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1228, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP INTERACTION WITH BICD2.
RX PubMed=22956769; DOI=10.1091/mbc.e12-03-0210;
RA Splinter D., Razafsky D.S., Schlager M.A., Serra-Marques A., Grigoriev I.,
RA Demmers J., Keijzer N., Jiang K., Poser I., Hyman A.A., Hoogenraad C.C.,
RA King S.J., Akhmanova A.;
RT "BICD2, dynactin, and LIS1 cooperate in regulating dynein recruitment to
RT cellular structures.";
RL Mol. Biol. Cell 23:4226-4241(2012).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-4281, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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. {ECO:0000250|UniProtKB:Q14204}.
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. Interacts with DYNC1LI1; DYNC1LI1
CC and DYNC1LI2 bind mutually exclusive to DYNC1H1. Interacts with
CC DYNC1LI2; DYNC1LI1 and DYNC1LI2 bind mutually exclusive to DYNC1H1.
CC Interacts with DYNC1I2 (By similarity). Interacts with BICD2
CC (PubMed:22956769). Interacts with DNALI1 (PubMed:16496424).
CC {ECO:0000250|UniProtKB:P38650, ECO:0000269|PubMed:16496424,
CC ECO:0000269|PubMed:22956769}.
CC -!- INTERACTION:
CC Q9JHU4; P07141: Csf1; NbExp=2; IntAct=EBI-645061, EBI-777188;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
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: Note=Defects in Dync1h1 are the cause of the 'Legs at odd
CC angles' (LOA) phenotype, an autosomal dominant trait where affected
CC animals display unusual twisting of the body and clenching of the
CC hindlimbs when suspended by the tail. Heterozygotes suffer age-related
CC progressive loss of muscle tone and locomotor ability without major
CC reduction in life-span while homozygotes show a more severe phenotype
CC with an inability to move or feed, and die within 24 hours of birth.
CC LOA mutants display defects in migration of facial motor neuron cell
CC bodies and impaired retrograde transport in spinal cord motor neurons.
CC {ECO:0000269|PubMed:12730604}.
CC -!- DISEASE: Note=Defects in Dync1h1 are the cause of the Cramping 1 (Cra1)
CC phenotype, an autosomal dominant trait where affected animals display
CC unusual twisting of the body and clenching of the hindlimbs when
CC suspended by the tail. Heterozygotes suffer age-related progressive
CC loss of muscle tone and locomotor ability without major reduction in
CC life-span while homozygotes show a more severe phenotype with an
CC inability to move or feed, and die within 24 hours of birth.
CC {ECO:0000269|PubMed:12730604}.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
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DR EMBL; AY004877; AAF91078.1; -; mRNA.
DR EMBL; AC152827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS36559.1; -.
DR RefSeq; NP_084514.2; NM_030238.2.
DR PDB; 3ERR; X-ray; 2.27 A; A/B=3260-3427.
DR PDB; 3J1T; EM; 9.70 A; A=3264-3427.
DR PDB; 3J1U; EM; 9.70 A; A=3264-3427.
DR PDB; 3WUQ; X-ray; 3.50 A; A=3207-3483.
DR PDB; 5AYH; X-ray; 3.01 A; A=3207-3475.
DR PDB; 6RZA; EM; 5.40 A; X=3270-3285, X=3410-3418.
DR PDB; 6RZB; EM; 5.00 A; C=3270-3418.
DR PDBsum; 3ERR; -.
DR PDBsum; 3J1T; -.
DR PDBsum; 3J1U; -.
DR PDBsum; 3WUQ; -.
DR PDBsum; 5AYH; -.
DR PDBsum; 6RZA; -.
DR PDBsum; 6RZB; -.
DR BMRB; Q9JHU4; -.
DR SMR; Q9JHU4; -.
DR BioGRID; 199254; 73.
DR ComplexPortal; CPX-5699; Cytoplasmic dynein complex, variant 1.
DR IntAct; Q9JHU4; 39.
DR MINT; Q9JHU4; -.
DR STRING; 10090.ENSMUSP00000018851; -.
DR iPTMnet; Q9JHU4; -.
DR PhosphoSitePlus; Q9JHU4; -.
DR SwissPalm; Q9JHU4; -.
DR EPD; Q9JHU4; -.
DR jPOST; Q9JHU4; -.
DR MaxQB; Q9JHU4; -.
DR PaxDb; Q9JHU4; -.
DR PeptideAtlas; Q9JHU4; -.
DR PRIDE; Q9JHU4; -.
DR ProteomicsDB; 277422; -.
DR Antibodypedia; 122; 151 antibodies from 27 providers.
DR DNASU; 13424; -.
DR Ensembl; ENSMUST00000018851; ENSMUSP00000018851; ENSMUSG00000018707.
DR GeneID; 13424; -.
DR KEGG; mmu:13424; -.
DR UCSC; uc007pbo.1; mouse.
DR CTD; 1778; -.
DR MGI; MGI:103147; Dync1h1.
DR VEuPathDB; HostDB:ENSMUSG00000018707; -.
DR eggNOG; KOG3595; Eukaryota.
DR GeneTree; ENSGT00940000156103; -.
DR HOGENOM; CLU_000038_7_0_1; -.
DR InParanoid; Q9JHU4; -.
DR OMA; FIMDEAN; -.
DR OrthoDB; 26380at2759; -.
DR PhylomeDB; Q9JHU4; -.
DR TreeFam; TF101165; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR Reactome; R-MMU-9646399; Aggrephagy.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 13424; 26 hits in 72 CRISPR screens.
DR ChiTaRS; Dync1h1; mouse.
DR EvolutionaryTrace; Q9JHU4; -.
DR PRO; PR:Q9JHU4; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9JHU4; protein.
DR Bgee; ENSMUSG00000018707; Expressed in cortical plate and 265 other tissues.
DR ExpressionAtlas; Q9JHU4; baseline and differential.
DR Genevisible; Q9JHU4; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005868; C:cytoplasmic dynein complex; ISO:MGI.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0030286; C:dynein complex; ISO:MGI.
DR GO; GO:0030175; C:filopodium; IDA:MGI.
DR GO; GO:0002177; C:manchette; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IPI:MGI.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0003341; P:cilium movement; IC:MGI.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0051293; P:establishment of spindle localization; ISO:MGI.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0072382; P:minus-end-directed vesicle transport along microtubule; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR GO; GO:0033962; P:P-body assembly; IMP:BHF-UCL.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0032388; P:positive regulation of intracellular transport; ISS:UniProtKB.
DR GO; GO:1905832; P:positive regulation of spindle assembly; ISS:UniProtKB.
DR GO; GO:0090235; P:regulation of metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; ISS:UniProtKB.
DR GO; GO:0008090; P:retrograde axonal transport; IBA:GO_Central.
DR GO; GO:0034063; P:stress granule assembly; IMP:BHF-UCL.
DR Gene3D; 1.10.8.710; -; 1.
DR Gene3D; 1.10.8.720; -; 1.
DR Gene3D; 1.20.140.100; -; 1.
DR Gene3D; 3.10.490.20; -; 1.
DR Gene3D; 3.20.180.20; -; 1.
DR Gene3D; 3.40.50.300; -; 5.
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; 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 Pfam; PF12774; AAA_6; 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; SSF52540; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division;
KW Coiled coil; Cytoplasm; Cytoskeleton; Disease variant; Dynein; Microtubule;
KW Mitosis; Motor protein; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14204"
FT CHAIN 2..4644
FT /note="Cytoplasmic dynein 1 heavy chain 1"
FT /id="PRO_0000114628"
FT REGION 2..1865
FT /note="Stem"
FT /evidence="ECO:0000250"
FT REGION 446..701
FT /note="Interaction with DYNC1I2"
FT /evidence="ECO:0000250"
FT REGION 649..800
FT /note="Interaction with DYNC1LI2"
FT /evidence="ECO:0000250"
FT REGION 1866..2097
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 2178..2450
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 2388..2408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2554..2803
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2897..3166
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 3187..3498
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 3551..3780
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT REGION 4003..4219
FT /note="AAA 6"
FT /evidence="ECO:0000250"
FT COILED 48..69
FT /evidence="ECO:0000255"
FT COILED 179..200
FT /evidence="ECO:0000255"
FT COILED 453..476
FT /evidence="ECO:0000255"
FT COILED 541..564
FT /evidence="ECO:0000255"
FT COILED 1169..1201
FT /evidence="ECO:0000255"
FT COILED 1229..1250
FT /evidence="ECO:0000255"
FT COILED 1355..1371
FT /evidence="ECO:0000255"
FT COILED 3187..3273
FT /evidence="ECO:0000255"
FT COILED 3394..3498
FT /evidence="ECO:0000255"
FT COILED 3735..3798
FT /evidence="ECO:0000255"
FT COMPBIAS 2388..2406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1904..1911
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2222..2229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2593..2600
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2935..2942
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q14204"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14204"
FT MOD_RES 1123
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14204"
FT MOD_RES 1228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3478
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14204"
FT MOD_RES 4160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14204"
FT MOD_RES 4281
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 4364
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14204"
FT MOD_RES 4366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14204"
FT VARIANT 580
FT /note="F -> Y (in LOA)"
FT /evidence="ECO:0000269|PubMed:12730604"
FT VARIANT 1055
FT /note="Y -> C (in CRA1)"
FT /evidence="ECO:0000269|PubMed:12730604"
FT CONFLICT 517
FT /note="A -> T (in Ref. 1; AAF91078)"
FT /evidence="ECO:0000305"
FT CONFLICT 2373
FT /note="F -> L (in Ref. 1; AAF91078)"
FT /evidence="ECO:0000305"
FT CONFLICT 2689
FT /note="G -> A (in Ref. 1; AAF91078)"
FT /evidence="ECO:0000305"
FT CONFLICT 3760
FT /note="D -> V (in Ref. 1; AAF91078)"
FT /evidence="ECO:0000305"
FT CONFLICT 3856
FT /note="I -> V (in Ref. 1; AAF91078)"
FT /evidence="ECO:0000305"
FT HELIX 3260..3295
FT /evidence="ECO:0007829|PDB:3ERR"
FT HELIX 3299..3306
FT /evidence="ECO:0007829|PDB:3ERR"
FT HELIX 3313..3325
FT /evidence="ECO:0007829|PDB:3ERR"
FT HELIX 3333..3336
FT /evidence="ECO:0007829|PDB:3ERR"
FT HELIX 3339..3341
FT /evidence="ECO:0007829|PDB:3ERR"
FT HELIX 3345..3351
FT /evidence="ECO:0007829|PDB:3ERR"
FT HELIX 3354..3356
FT /evidence="ECO:0007829|PDB:3ERR"
FT HELIX 3359..3368
FT /evidence="ECO:0007829|PDB:3ERR"
FT TURN 3369..3371
FT /evidence="ECO:0007829|PDB:3ERR"
FT HELIX 3377..3383
FT /evidence="ECO:0007829|PDB:3ERR"
FT HELIX 3387..3427
FT /evidence="ECO:0007829|PDB:3ERR"
FT TURN 3455..3457
FT /evidence="ECO:0007829|PDB:5AYH"
FT HELIX 3458..3471
FT /evidence="ECO:0007829|PDB:5AYH"
SQ SEQUENCE 4644 AA; 532045 MW; C88C9FC21D41DD56 CRC64;
MSEPGGGEDG SAGLEVSAVQ NVADVAVLQK HLRKLVPLLL EDGGDAPAAL EAALEEKSAL
EQMRKFLSDP QVHTVLVERS TLKEDVGDEG EEEKEFISYN INIDIHYGVK SNSLAFIKRA
PVIDADKPVS SQLRVLTLSE DSPYETLHSF ISNAVAPFFK SYIRESGKAD RDGDKMAPSV
EKKIAELEMG LLHLQQNIEI PEISLPIHPI ITNVAKQCYE RGEKPKVTDF GDKVEDPTFL
NQLQSGVNRW IREIQKVTKL DRDPASGTAL QEISFWLNLE RALYRIQEKR ESPEVLLTLD
ILKHGKRFHA TVSFDTDTGL KQALETVNDY NPLMKDFPLN DLLSATELDK IRQALVAIFT
HLRKIRNTKY PIQRALRLVE AISRDLSSQL LKVLGTRKLM HVAYEEFEKV MVACFEVFQT
WDDEYEKLQV LLRDIVKRKR EENLKMVWRI NPAHRKLQAR LDQMRKFRRQ HEQLRAVIVR
VLRPQVTAVA QQNQGEAPEP QDMKVAEVLF DAADANAIEE VNLAYENVKE VDGLDVSKEG
TEAWEAAMKR YDERIDRVET RITARLRDQL GTAKNANEMF RIFSRFNALF VRPHIRGAIR
EYQTQLIQRV KDDIESLHDK FKVQYPQSQA CKMSHVRDLP PVSGSIIWAK QIDRQLTAYM
KRVEDVLGKG WENHVEGQKL KQDGDSFRMK LNTQEIFDDW ARKVQQRNLG VSGRIFTIES
ARVRGRTGNV LKLKVNFLPE IITLSKEVRN LKWLGFRVPL AIVNKAHQAN QLYPFAISLI
ESVRTYERTC EKVEERNTIS LLVAGLKKEV QALIAEGIAL VWESYKLDPY VQRLAETVFN
FQEKVDDLLI IEEKIDLEVR SLETCMYDHK TFSEILNRVQ KAVDDLNLHS YSNLPIWVNK
LDMEIERILG VRLQAGLRAW TQVLLGQAED KAEVDMDTDA PQVSHKPGGE PKIKNVVHEL
RITNQVIYLN PPIEECRYKL YQEMFAWKMV VLSLPRIQSQ RYQVGVHYEL TEEEKFYRNA
LTRMPDGPVA LEESYSAVMG IVTEVEQYVK VWLQYQCLWD MQAENIYNRL GEDLNKWQAL
LVQIRKARGT FDNAETKKEF GPVVIDYGKV QSKVNLKYDS WHKEVLSKFG QMLGSNMTEF
HSQISKSRQE LEQHSVDTAS TSDAVTFITY VQSLKRKIKQ FEKQVELYRN GQRLLEKQRF
QFPPSWLYID NIEGEWGAFN DIMRRKDSAI QQQVANLQMK IVQEDRAVES RTTDLLTDWE
KTKPVTGNLR PEEALQALTI YEGKFGRLKD DREKCAKAKE ALELTDTGLL SGSEERVQVA
LEELQDLKGV WSELSKVWEQ IDQMKEQPWV SVQPRKLRQN LDGLLNQLKN FPARLRQYAS
YEFVQRLLKG YMKINMLVIE LKSEALKDRH WKQLMKRLHV NWVVSELTLG QIWDVDLQKN
EAVVKDVLLV AQGEMALEEF LKQIREVWNT YELDLVNYQN KCRLIRGWDD LFNKVKEHIN
SVSAMKLSPY YKVFEEDALS WEDKLNRIMA LFDVWIDVQR RWVYLEGIFT GSADIKHLLP
VETQRFQSIS TEFLALMKKV SKSPLVMDVL NIQGVQRSLE RLADLLGKIQ KALGEYLERE
RSSFPRFYFV GDEDLLEIIG NSKNVAKLQK HFKKMFAGVS SIILNEDNSV VLGISSREGE
EVMFKTPVSI TEHPKINEWL TLVEKEMRVT LAKLLAESVT EVEIFGKATS IDPNTYITWI
DKYQAQLVVL SAQIAWSENV ENALSNVGGG GDVGPLQSVL SNVEVTLNVL ADSVLMEQPP
LRRRKLEHLI TELVHQRDVT RSLIKSKIDN AKSFEWLSQM RFYFDPKQTD VLQQLSIQMA
NAKFNYGFEY LGVQDKLVQT PLTDRCYLTM TQALEARLGG SPFGPAGTGK TESVKALGHQ
LGRFVLVFNC DETFDFQAMG RIFVGLCQVG AWGCFDEFNR LEERMLSAVS QQVQCIQEAL
REHSNPNYDK TSAPITCELL NKQVKVSPDM AIFITMNPGY AGRSNLPDNL KKLFRSLAMT
KPDRQLIAQV MLYSQGFRTA EVLANKIVPF FKLCDEQLSS QSHYDFGLRA LKSVLVSAGN
VKRERIQKIK REKEERGEAV DEGEIAENLP EQEILIQSVC ETMVPKLVAE DIPLLFSLLS
DVFPGVQYHR GEMTALREEL KKVCQEMYLT YGDGEEVGGM WVEKVLQLYQ ITQINHGLMM
VGPSGSGKSM AWRVLLKALE RLEGVEGVAH IIDPKAISKD HLYGTLDPNT REWTDGLFTH
VLRKIIDNVR GELQKRQWIV FDGDVDPEWV ENLNSVLDDN KLLTLPNGER LSLPPNVRIM
FEVQDLKYAT LATVSRCGMV WFSEDVLSTD MIFNNFLARL RSIPLDEGED EAQRRRKGKE
DEGEEAASPM LQIQRDAATI MQPYFTSNGL VTKALEHAFK LEHIMDLTRL RCLGSLFSML
HQACRNVAQY NANHPDFPMQ IEQLERYIQR YLVYAILWSL SGDSRLKMRA ELGEYIRRIT
TVPLPTAPNV PIIDYEVSIS GEWSPWQAKV PQIEVETHKV AAPDVVVPTL DTVRHEALLY
TWLAEHKPLV LCGPPGSGKT MTLFSALRAL PDMEVVGLNF SSATTPELLL KTFDHYCEYR
RTPNGVVLAP VQLGKWLVLF CDEINLPDMD KYGTQRVISF IRQMVEHGGF YRTSDQTWVK
LERIQFVGAC NPPTDPGRKP LSHRFLRHVP VVYVDYPGPA SLTQIYGTFN RAMLRLIPSL
RTYAEPLTAA MVEFYTMSQE RFTQDTQPHY IYSPREMTRW VRGIFEALRP LETLPVEGLI
RIWAHEALRL FQDRLVEDEE RRWTDENIDM VALKHFPNID KEKAMSRPIL YSNWLSKDYI
PVDQEELRDY VKARLKVFYE EELDVPLVLF NEVLDHVLRI DRIFRQPQGH LLLIGVSGAG
KTTLSRFVAW MNGLSVYQIK VHRKYTGEDF DEDLRTVLRR SGCKNEKIAF IMDESNVLDS
GFLERMNTLL ANGEVPGLFE GDEYATLMTQ CKEGAQKEGL MLDSHEELYK WFTSQVIRNL
HVVFTMNPSS EGLKDRAATS PALFNRCVLN WFGDWSTEAL YQVGKEFTSK MDLEKPNYIV
PDYMPVVYDK LPQPPTHREA IVNSCVFVHQ TLHQANARLA KRGGRTMAIT PRHYLDFINH
YANLFHEKRS ELEEQQMHLN VGLRKIKETV DQVEELRRDL RIKSQELEVK NAAANDKLKK
MVKDQQEAEK KKVMSQEIQE QLHKQQEVIA DKQMSVKEDL DKVEPAVIEA QNAVKSIKKQ
HLVEVRSMAN PPAAVKLALE SICLLLGEST TDWKQIRSII MRENFIPTIV NFSAEEISDA
IREKMKKNYM SNPSYNYEIV NRASLACGPM VKWAIAQLNY ADMLKRVEPL RNELQKLEDD
AKDNQQKANE VEQMIRDLEA SIARYKEEYA VLISEAQAIK ADLAAVEAKV NRSTALLKSL
SAERERWEKT SETFKNQMST IAGDCLLSAA FIAYAGYFDQ QMRQNLFTTW SHHLQQANIQ
FRTDIARTEY LSNADERLRW QASSLPADDL CTENAIMLKR FNRYPLIIDP SGQATEFIMN
EYKDRKITRT SFLDDAFRKN LESALRFGNP LLVQDVESYD PVLNPVLNRE VRRTGGRVLI
TLGDQDIDLS PSFVIFLSTR DPTVEFPPDL CSRVTFVNFT VTRSSLQSQC LNEVLKAERP
DVDEKRSDLL KLQGEFQLRL RQLEKSLLQA LNEVKGRILD DDTIITTLEN LKREAAEVTR
KVEETDIVMQ EVETVSQQYL PLSTACSSIY FTMESLKQVH FLYQYSLQFF LDIYHNVLYE
NPNLKGATDH TQRLSIITKD LFQVAFNRVA RGMLHQDHIT FAMLLARIKL KGTVGEPTYD
AEFQHFLRGK EIVLSAGSTP KIQGLTVEQA EAVVRLSCLP AFKDLIAKVQ ADEQFGIWLD
SSSPEQTVPY LWSEETPTTP IGQAIHRLLL IQAFRPDRLL AMAHMFVSTN LGESFMSIME
QPLDLTHIVG TEVKPNTPVL MCSVPGYDAS GHVEDLAAEQ NTQITSIAIG SAEGFNQADK
AINTAVKSGR WVMLKNVHLA PGWLMQLEKK LHSLQPHACF RLFLTMEINP KVPVNLLRAG
RIFVFEPPPG VKANMLRTFS SIPVSRICKS PNERARLYFL LAWFHAIIQE RLRYAPLGWS
KKYEFGESDL RSACDTVDTW LDDTAKGRQN ISPDKIPWSA LKTLMAQSIY GGRVDNEFDQ
RLLNTFLERL FTTRSFDSEF KLACKVDGHK DIQMPDGIRR EEFVQWVELL PDAQTPSWLG
LPNNAERVLL TTQGVDMISK MLKMQMLEDE DDLAYAETEK KARTDSTSDG RPAWMRTLHT
TASNWLHLIP QTLSPLKRTV ENIKDPLFRF FEREVKMGAK LLQDVRQDLA DVVQVCEGKK
KQTNYLRTLI NELVKGILPR SWSHYTVPAG MTVIQWVSDF SERIKQLQNI SQAAASGGAK
ELKNIHVCLG GLFVPEAYIT ATRQYVAQAN SWSLEELCLE VNVTASQSAT LDACSFGVTG
LKLQGATCSN NKLSLSNAIS TVLPLTQLRW VKQTSAEKKA SVVTLPVYLN FTRADLIFTV
DFEIATKEDP RSFYERGVAV LCTE
