MYOE_DICDI
ID MYOE_DICDI Reviewed; 1005 AA.
AC Q03479; Q54IK6;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Myosin IE heavy chain;
GN Name=myoE; Synonyms=dmiE; ORFNames=DDB_G0288679;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AX3;
RX PubMed=8504170; DOI=10.1016/0167-4781(93)90185-g;
RA Urrutia R., Jung G., Hammer J.A. III;
RT "The Dictyostelium myosin IE heavy chain gene encodes a truncated isoform
RT that lacks sequences corresponding to the actin binding site in the tail.";
RL Biochim. Biophys. Acta 1173:225-229(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP NOMENCLATURE.
RX PubMed=16857047; DOI=10.1186/1471-2164-7-183;
RA Kollmar M.;
RT "Thirteen is enough: the myosins of Dictyostelium discoideum and their
RT light chains.";
RL BMC Genomics 7:183-183(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-695.
RX PubMed=12032065; DOI=10.1093/emboj/21.11.2517;
RA Kollmar M., Duerrwang U., Kliche W., Manstein D.J., Kull F.J.;
RT "Crystal structure of the motor domain of a class-I myosin.";
RL EMBO J. 21:2517-2525(2002).
CC -!- FUNCTION: Myosin is a protein that binds to actin and has ATPase
CC activity that is activated by actin. May play a role in moving
CC membranes relative to actin.
CC -!- SUBUNIT: Myosin I heavy chain is single-headed. Dimer of a heavy and a
CC light chain. Inability to self-assemble into filaments.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA33201.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L06805; AAA33201.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AAFI02000120; EAL63071.1; -; Genomic_DNA.
DR PIR; S33760; S33760.
DR RefSeq; XP_636580.1; XM_631488.1.
DR PDB; 1LKX; X-ray; 3.00 A; A/B/C/D=1-697.
DR PDB; 4A7F; EM; 7.70 A; C/G/J=1-697.
DR PDB; 4A7H; EM; 7.80 A; C/I/J=1-697.
DR PDB; 4A7L; EM; 8.10 A; C/G/J=1-697.
DR PDBsum; 1LKX; -.
DR PDBsum; 4A7F; -.
DR PDBsum; 4A7H; -.
DR PDBsum; 4A7L; -.
DR AlphaFoldDB; Q03479; -.
DR SMR; Q03479; -.
DR STRING; 44689.DDB0216200; -.
DR PaxDb; Q03479; -.
DR EnsemblProtists; EAL63071; EAL63071; DDB_G0288679.
DR GeneID; 8626753; -.
DR KEGG; ddi:DDB_G0288679; -.
DR dictyBase; DDB_G0288679; myoE.
DR eggNOG; KOG0164; Eukaryota.
DR HOGENOM; CLU_000192_7_7_1; -.
DR InParanoid; Q03479; -.
DR OMA; PLYGNEY; -.
DR PhylomeDB; Q03479; -.
DR EvolutionaryTrace; Q03479; -.
DR PRO; PR:Q03479; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0062201; C:actin wave; IDA:dictyBase.
DR GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0032009; C:early phagosome; IDA:dictyBase.
DR GO; GO:0031256; C:leading edge membrane; IDA:dictyBase.
DR GO; GO:0070685; C:macropinocytic cup; IDA:dictyBase.
DR GO; GO:0070687; C:macropinocytic cup cytoskeleton; IDA:dictyBase.
DR GO; GO:0070686; C:macropinocytic cup membrane; IDA:dictyBase.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0001891; C:phagocytic cup; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0031143; C:pseudopodium; IDA:dictyBase.
DR GO; GO:0031260; C:pseudopodium membrane; IDA:dictyBase.
DR GO; GO:0003779; F:actin binding; IDA:dictyBase.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:dictyBase.
DR GO; GO:0005516; F:calmodulin binding; IDA:dictyBase.
DR GO; GO:0000146; F:microfilament motor activity; IDA:dictyBase.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:dictyBase.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030041; P:actin filament polymerization; IGI:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IGI:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0006911; P:phagocytosis, engulfment; IGI:dictyBase.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01378; MYSc_Myo1; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_TH1.
DR InterPro; IPR036072; MYSc_Myo1.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 2.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51757; TH1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; ATP-binding; Calmodulin-binding;
KW Motor protein; Myosin; Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..1005
FT /note="Myosin IE heavy chain"
FT /id="PRO_0000123369"
FT DOMAIN 8..693
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 694..722
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 716..745
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 810..1004
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT REGION 539..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..630
FT /note="Actin-binding"
FT BINDING 101..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT CONFLICT 26
FT /note="E -> D (in Ref. 1; AAA33201)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="T -> R (in Ref. 1; AAA33201)"
FT /evidence="ECO:0000305"
FT CONFLICT 427..429
FT /note="VRE -> K (in Ref. 1; AAA33201)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="Missing (in Ref. 1; AAA33201)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="I -> N (in Ref. 1; AAA33201)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="V -> D (in Ref. 1; AAA33201)"
FT /evidence="ECO:0000305"
FT CONFLICT 681..683
FT /note="NPT -> IPR (in Ref. 1; AAA33201)"
FT /evidence="ECO:0000305"
FT CONFLICT 735
FT /note="K -> N (in Ref. 1; AAA33201)"
FT /evidence="ECO:0000305"
FT CONFLICT 763
FT /note="H -> D (in Ref. 1; AAA33201)"
FT /evidence="ECO:0000305"
FT CONFLICT 828
FT /note="S -> W (in Ref. 1; AAA33201)"
FT /evidence="ECO:0000305"
FT CONFLICT 889
FT /note="K -> N (in Ref. 1; AAA33201)"
FT /evidence="ECO:0000305"
FT CONFLICT 997..998
FT /note="NQ -> KE (in Ref. 1; AAA33201)"
FT /evidence="ECO:0000305"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:1LKX"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:1LKX"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 59..65
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 77..91
FT /evidence="ECO:0007829|PDB:1LKX"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 107..121
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 127..147
FT /evidence="ECO:0007829|PDB:1LKX"
FT STRAND 160..168
FT /evidence="ECO:0007829|PDB:1LKX"
FT STRAND 174..182
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 211..217
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:1LKX"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 242..255
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 260..276
FT /evidence="ECO:0007829|PDB:1LKX"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:1LKX"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:1LKX"
FT STRAND 293..298
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 299..309
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 313..321
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 342..372
FT /evidence="ECO:0007829|PDB:1LKX"
FT STRAND 381..386
FT /evidence="ECO:0007829|PDB:1LKX"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 398..418
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 420..428
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 443..447
FT /evidence="ECO:0007829|PDB:1LKX"
FT STRAND 450..454
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 455..464
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 470..480
FT /evidence="ECO:0007829|PDB:1LKX"
FT STRAND 481..484
FT /evidence="ECO:0007829|PDB:1LKX"
FT TURN 490..492
FT /evidence="ECO:0007829|PDB:1LKX"
FT STRAND 502..507
FT /evidence="ECO:0007829|PDB:1LKX"
FT STRAND 510..515
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 519..524
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 529..536
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 541..546
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 562..577
FT /evidence="ECO:0007829|PDB:1LKX"
FT STRAND 580..588
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 601..610
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 614..622
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 631..634
FT /evidence="ECO:0007829|PDB:1LKX"
FT STRAND 639..641
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 654..661
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 667..669
FT /evidence="ECO:0007829|PDB:1LKX"
FT STRAND 670..672
FT /evidence="ECO:0007829|PDB:1LKX"
FT STRAND 674..682
FT /evidence="ECO:0007829|PDB:1LKX"
FT HELIX 683..689
FT /evidence="ECO:0007829|PDB:1LKX"
SQ SEQUENCE 1005 AA; 114795 MW; 8E3D638C7043CF0A CRC64;
MIPKTKAEGV PDFVLLNQIT ENAFIENLTM RHKSDNIYTY IGDVVISTNP FKNLNIYKES
DIKAYNGRYK YEMPPHIYAL ANDAYRSMRQ SQENQCVIIS GESGAGKTEA SKKIMQFLTF
VSSNQSPNGE RISKMLLDSN PLLEAFGNAK TLRNDNSSRF GKYMEMQFNA VGSPIGGKIT
NYLLEKSRVV GRTQGERSFH IFYQMLKGLS QSKLNELGLT PNAPAYEYLK KSGCFDVSTI
DDSGEFKIIV KAMETLGLKE SDQNSIWRIL AAILHIGNIT FAEAAEQRTG TTTVKVSDTK
SLAAAASCLK TDQQSLSIAL CYRSISTGVG KRCSVISVPM DCNQAAYSRD ALAKALYERL
FNWLVSKINT IINCTTEKGP VIGILDIYGF EVFQNNSFEQ LNINFCNEKL QQLFIELTLK
SEQEEYVREG IEWKNIEYFN NKPICELIEK KPIGLISLLD EACLIAKSTD QTFLDSICKQ
FEKNPHLQSY VVSKDRSIGD TCFRLKHYAG DVTYDVRGFL DKNKDTLFGD LISSMQSSSD
PLVQGLFPPT RPEDSKKRPE TAGSQFRNAM NALITTLLAC SPHYVRCIKS NDNKQAGVID
EDRVRHQVRY LGLLENVRVR RAGFAGRIEY TRFYNRYKML CKKTWPSFNG TAKQATELIL
QQHNIDKEEI RMGKTKVFIR NPTTLFYFEE KRELEMPRIV TLIQKTWRGY RARSKWNQRK
AAIKIQLFYR SYRYKKWFRE LHRAFKDVAR DPQWGKQVFW PKHPSILDRA VQLTHKIHNC
WRAEKMILSL GAGQNHMRQK VMAYDIFHGK KKWDFRRHFD ADYLEKPSNP NQQKYVLAMQ
NLFSTYGDTE VLFADYVIKV NPKGVPQRRG IVVTGTNIYK HDPKNYKVKK WGTPLVDVTS
ISISPMADTF LVLHCKAPQR DFVLDLGCNG YEAVSEITTV IVQQVLKLTG VKLSVQFTSS
ITYNNARPKG SDTILTFAPI NNDPKLIGSQ FKKGKGNQAT IQFKD
