MYOD_DICDI
ID MYOD_DICDI Reviewed; 1109 AA.
AC P34109; Q553G7; Q869M0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Myosin ID heavy chain;
GN Name=myoD; Synonyms=dmiD; ORFNames=DDB_G0275447;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 604-610; 733-742 AND
RP 914-928, AND SUBCELLULAR LOCATION.
RC STRAIN=AX3;
RX PubMed=8325874; DOI=10.1016/s0021-9258(18)82428-0;
RA Jung G., Fukui Y., Martin B., Hammer J.A. III;
RT "Sequence, expression pattern, intracellular localization, and targeted
RT disruption of the Dictyostelium myosin ID heavy chain isoform.";
RL J. Biol. Chem. 268:14981-14990(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
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 [4]
RP SUBCELLULAR LOCATION.
RX PubMed=2797149; DOI=10.1038/341328a0;
RA Fukui Y., Lynch T.J., Brzeska H., Korn E.D.;
RT "Myosin I is located at the leading edges of locomoting Dictyostelium
RT amoebae.";
RL Nature 341:328-331(1989).
RN [5]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=8980908;
RA Morita Y.S., Jung G., Hammer J.A. III, Fukui Y.;
RT "Localization of Dictyostelium myoB and myoD to filopodia and cell-cell
RT contact sites using isoform-specific antibodies.";
RL Eur. J. Cell Biol. 71:371-379(1996).
RN [6]
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=8609164; DOI=10.1083/jcb.133.2.305;
RA Jung G., Wu X., Hammer J.A. III;
RT "Dictyostelium mutants lacking multiple classic myosin I isoforms reveal
RT combinations of shared and distinct functions.";
RL J. Cell Biol. 133:305-323(1996).
RN [7]
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).
CC -!- FUNCTION: Myosin is a protein that binds to actin and has ATPase
CC activity that is activated by actin. Myosin id may have a role in
CC chemotaxis and aggregation; it could serve to stabilize and even
CC retract cortical structures, such as pseudopods and lamellopods.
CC Involved in the process of phagocytosis. {ECO:0000269|PubMed:8609164}.
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 -!- SUBCELLULAR LOCATION: Cell projection, pseudopodium. Cytoplasm, cell
CC cortex. Note=Highest concentration just beneath the plasma membrane in
CC the anterior pseudopod at the leading edge of the cell.
CC -!- DEVELOPMENTAL STAGE: Found at leading edges of lamellipodia and at
CC sites of cell-cell contact in stationary stage cells. Also present in
CC filopodia. Largely disappears from lamellipodia and cell-cell contact
CC regions in aggregation stage cells, suggesting the occurrence of a
CC developmentally regulated relocalization to the cytoplasm.
CC {ECO:0000269|PubMed:8980908}.
CC -!- DOMAIN: Myosin tail domain binds directly to anionic phospholipid
CC membranes; myosins I could therefore move actin relative to membranes
CC and vice versa. TH.2 and SH3 bind tightly to F-actin; this together
CC with the nucleotide-sensitive site in the head, allows single molecules
CC of myosin I to cross-link actin filaments.
CC -!- DISRUPTION PHENOTYPE: MyoB and myoD double mutant exhibits reduction in
CC the speed of whole cell translocation. myoB, myoC and myoD triple
CC mutant exhibits reduction in the speed of whole cell translocation.
CC {ECO:0000269|PubMed:8609164}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; L16509; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AAFI02000013; EAL69474.1; -; Genomic_DNA.
DR PIR; A47106; A47106.
DR RefSeq; XP_643446.1; XM_638354.1.
DR AlphaFoldDB; P34109; -.
DR SMR; P34109; -.
DR STRING; 44689.DDB0191347; -.
DR PaxDb; P34109; -.
DR EnsemblProtists; EAL69474; EAL69474; DDB_G0275447.
DR GeneID; 8620031; -.
DR KEGG; ddi:DDB_G0275447; -.
DR dictyBase; DDB_G0275447; myoD.
DR eggNOG; KOG0162; Eukaryota.
DR eggNOG; KOG4225; Eukaryota.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; P34109; -.
DR OMA; NGWWLCK; -.
DR PhylomeDB; P34109; -.
DR PRO; PR:P34109; -.
DR Proteomes; UP000002195; Chromosome 2.
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:0005911; C:cell-cell junction; IDA:dictyBase.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0030175; C:filopodium; IDA:dictyBase.
DR GO; GO:0061851; C:leading edge of lamellipodium; IDA:dictyBase.
DR GO; GO:0070687; C:macropinocytic cup cytoskeleton; IDA:dictyBase.
DR GO; GO:0045160; C:myosin I complex; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0031143; C:pseudopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0051233; C:spindle midzone; IDA:dictyBase.
DR GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IDA:dictyBase.
DR GO; GO:0032027; F:myosin light chain binding; IPI:dictyBase.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:dictyBase.
DR GO; GO:0005543; F:phospholipid 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:0006897; P:endocytosis; IBA:GO_Central.
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; 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 InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51757; TH1; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Cell projection; Chemotaxis; Cytoplasm;
KW Direct protein sequencing; Motor protein; Myosin; Nucleotide-binding;
KW Phagocytosis; Reference proteome; SH3 domain.
FT CHAIN 1..1109
FT /note="Myosin ID heavy chain"
FT /id="PRO_0000123368"
FT DOMAIN 7..687
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 725..919
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 958..1017
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 564..586
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 1017..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 101..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 613
FT /note="I -> IFGRI (in Ref. 1; L16509)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="A -> R (in Ref. 1; L16509)"
FT /evidence="ECO:0000305"
FT CONFLICT 837
FT /note="T -> R (in Ref. 1; L16509)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1109 AA; 124024 MW; 40A702C4F769611F CRC64;
MAYKSQHGVD DMVMLSKIAN DSILDNLKKR YGGDVIYTYI GNVLISVNPF KQIKNLYSER
NLLEYRGKFR YELPPHAYAV ADDMYRSMYA EGQSQCVIIS GESGAGKTEA AKLIMQYIAA
VSGKGADVSR VKDVILESNP LLEAFGNAKT LRNNNSSRFG KYMEVQFNGI GDPEGGRVTN
YLLEKSRVVY QTKGERNFHI FYQLLSGANQ QLKSELRLDT PDKFNYLSAS GCYTVDGVDD
SGEFQDVCKA MKVIGLTDSE QKEVFRLVAA ILYLGNVGFK NNAKDEAAID QQSKKALENF
AFLMQTDVSS CEKALCFRTI STGTQGRSAR VSTYACPQNS EGAYYSRDAL AKALYSRLFD
WIVGRVNSAL GYKQNSQSLM IGILDIYGFE IFEKNGFEQM VINYVNERLQ QIFIELTLKT
EQEEYFNEGI QWEQIDYFNN KICCDLIESK KPAGILTILD DVCNFPKGDD QKFLDRLKES
FSSHAHFQSA AQSSSSFTIK HYAGDVEYCA EGFVDKNKDL LFNDLVELAA CTTSKLIPQL
FPEINCEKDK RKPTTAGFKI KESIGALVKA LSACTPHYIR CIKPNGNKRA NDFDTSLVMH
QVKYLGLLEN VRIRRAGYAY RQTYDKFFYR YRVCCKETWP NWTGGFESGV ETILKSMDLE
PKQYSKGKTK IFIRAPETVF NLEELRERKV FTYANKLQRF FLRFTLMSYY YSIQKGAADS
MKSNKERRRL SIERPYQGDY INYRENFELK DIVKKNGNEK IMFTHAVNKY DRRSRCQRRV
LLLSDTAIYF IATEKNKDKE DRKKRPWIYV QKRRLLLAGI TSVELSKLSD GFVVLKTMNE
HDQIFECRRK TEFLGTLIKA YKTGTLRINY NNSIGVAIKA SKQGGKGKER IILFEKGIKP
GESVFKGTKV STPSDGLPAD TVPNLTPPES LPVVSIPIYK PAMNAKNAPQ NSGGPASNVK
PSAKALYDFD AESSMELSFK EGDILTVLDQ SSGDWWDAEL KGRRGKVPSN YLQLIKNAAP
PRAGGPPVPT GNRAPTTTTT SGGSTRGGFN NGPSTAPSGR GAAPPSSRGG MAPRGGSVAP
PSSRGGIAPR GGIAPRGGMA PRGGMAPRV
