MYOB_DICDI
ID MYOB_DICDI Reviewed; 1111 AA.
AC P34092; Q54HY1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Myosin IB heavy chain;
GN Name=myoB; Synonyms=dmiB, myoA; ORFNames=DDB_G0289117;
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=2762320; DOI=10.1073/pnas.86.16.6186;
RA Jung G., Saxe C.L. III, Kimmel A.R., Hammer J.A. III;
RT "Dictyostelium discoideum contains a gene encoding a myosin I heavy
RT chain.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:6186-6190(1989).
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 PROTEIN SEQUENCE OF 481-490; 656-666 AND 783-798, 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 [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 DISRUPTION PHENOTYPE.
RX PubMed=2141028; DOI=10.1083/jcb.110.6.1955;
RA Jung G., Hammer J.A. III;
RT "Generation and characterization of Dictyostelium cells deficient in a
RT myosin I heavy chain isoform.";
RL J. Cell Biol. 110:1955-1964(1990).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=1666340; DOI=10.1002/cm.970200406;
RA Wessels D., Murray J., Jung G., Hammer J.A. III, Soll D.R.;
RT "Myosin IB null mutants of Dictyostelium exhibit abnormalities in
RT motility.";
RL Cell Motil. Cytoskeleton 20:301-315(1991).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=8522584; DOI=10.1083/jcb.131.5.1205;
RA Novak K.D., Peterson M.D., Reedy M.C., Titus M.A.;
RT "Dictyostelium myosin I double mutants exhibit conditional defects in
RT pinocytosis.";
RL J. Cell Biol. 131:1205-1221(1995).
RN [8]
RP SUBCELLULAR LOCATION.
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 [9]
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND
RP 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 [10]
RP FUNCTION.
RX PubMed=9024693; DOI=10.1083/jcb.136.3.633;
RA Novak K.D., Titus M.A.;
RT "Myosin I overexpression impairs cell migration.";
RL J. Cell Biol. 136:633-647(1997).
RN [11]
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-332.
RX PubMed=9436992; DOI=10.1091/mbc.9.1.75;
RA Novak K.D., Titus M.A.;
RT "The myosin I SH3 domain and TEDS rule phosphorylation site are required
RT for in vivo function.";
RL Mol. Biol. Cell 9:75-88(1998).
RN [12]
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 [13]
RP FUNCTION, AND MUTAGENESIS OF SER-332.
RX PubMed=16415352; DOI=10.1074/jbc.m508670200;
RA Crawley S.W., de la Roche M.A., Lee S.F., Li Z., Chitayat S., Smith S.P.,
RA Cote G.P.;
RT "Identification and characterization of an 8-kDa light chain associated
RT with Dictyostelium discoideum MyoB, a class I myosin.";
RL J. Biol. Chem. 281:6307-6315(2006).
CC -!- FUNCTION: Myosin is a protein that binds to actin and has ATPase
CC activity that is activated by actin. Myosin IB 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 whole cell motility of aggregation-stages cells.
CC Overexpression results in significant decrease in the rate of cellular
CC translocation and fluid-phase pinocytosis and abnormalities in the
CC normal rearrangement of the actin cytoskeleton.
CC {ECO:0000269|PubMed:16415352, ECO:0000269|PubMed:8609164,
CC ECO:0000269|PubMed:9024693}.
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 and at sites of
CC cell-cell contact in both stationary and aggregation stage cells. Also
CC found in macropinocytic structures.
CC -!- DEVELOPMENTAL STAGE: Rises dramatically during early development.
CC {ECO:0000269|PubMed:8609164}.
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: Shows defects in pseudopod formation and
CC translocation. Also shows slower speed of locomoting, aggregation-stage
CC cells and significant reduction in initial rate of phagocytosis. MyoB
CC and myoC double mutant exhibits profound defects in growth, endocytosis
CC and rearrangement of F-actin. Expression of the full-length myoB heavy
CC chain in these cells fully rescues the double mutant defects. myoB and
CC myoD double mutant exhibits reduction in the speed of whole cell
CC translocation. myoB, myoC and myoD triple mutant exhibits reduction in
CC the speed of whole cell translocation. {ECO:0000269|PubMed:1666340,
CC ECO:0000269|PubMed:2141028, ECO:0000269|PubMed:8522584,
CC ECO:0000269|PubMed:8609164, ECO:0000269|PubMed:9436992}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; M26037; AAA33229.1; -; Genomic_DNA.
DR EMBL; AAFI02000130; EAL62866.1; -; Genomic_DNA.
DR PIR; A33284; A33284.
DR RefSeq; XP_636382.1; XM_631290.1.
DR AlphaFoldDB; P34092; -.
DR SMR; P34092; -.
DR STRING; 44689.DDB0191351; -.
DR PaxDb; P34092; -.
DR PRIDE; P34092; -.
DR EnsemblProtists; EAL62866; EAL62866; DDB_G0289117.
DR GeneID; 8626983; -.
DR KEGG; ddi:DDB_G0289117; -.
DR dictyBase; DDB_G0289117; myoB.
DR eggNOG; KOG0162; Eukaryota.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; P34092; -.
DR OMA; MESKWGT; -.
DR PhylomeDB; P34092; -.
DR PRO; PR:P34092; -.
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:0098858; C:actin-based cell projection; IDA:dictyBase.
DR GO; GO:0042641; C:actomyosin; 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:0005769; C:early endosome; IDA:dictyBase.
DR GO; GO:0030175; C:filopodium; IDA:dictyBase.
DR GO; GO:0061851; C:leading edge of lamellipodium; IDA:dictyBase.
DR GO; GO:0070685; C:macropinocytic cup; 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:0097203; C:phagocytic cup lip; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0031143; C:pseudopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IDA:dictyBase.
DR GO; GO:0000146; F:microfilament motor activity; IDA:dictyBase.
DR GO; GO:0032027; F:myosin light chain binding; IDA:dictyBase.
DR GO; GO:0005543; F:phospholipid binding; IDA:dictyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IGI:dictyBase.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0033275; P:actin-myosin filament sliding; IDA:dictyBase.
DR GO; GO:0048870; P:cell motility; IMP:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; IGI:dictyBase.
DR GO; GO:0006887; P:exocytosis; IEP:dictyBase.
DR GO; GO:0046847; P:filopodium assembly; IGI:dictyBase.
DR GO; GO:0120320; P:lateral pseudopodium retraction; IMP:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0044655; P:phagosome reneutralization; IMP:dictyBase.
DR GO; GO:0006907; P:pinocytosis; IGI:dictyBase.
DR GO; GO:0044656; P:regulation of post-lysosomal vacuole size; IMP:dictyBase.
DR GO; GO:1903013; P:response to differentiation-inducing factor 1; HDA:dictyBase.
DR GO; GO:0051707; P:response to other organism; TAS:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP: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 Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..1111
FT /note="Myosin IB heavy chain"
FT /id="PRO_0000123366"
FT DOMAIN 9..691
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 729..913
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1053..1111
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 547..627
FT /note="Actin-binding"
FT REGION 910..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MUTAGEN 332
FT /note="S->A: Fail to complement the null phenotype."
FT /evidence="ECO:0000269|PubMed:16415352,
FT ECO:0000269|PubMed:9436992"
FT MUTAGEN 332
FT /note="S->E: Forms a complex in the presence and absence of
FT Ca(2+)."
FT /evidence="ECO:0000269|PubMed:16415352,
FT ECO:0000269|PubMed:9436992"
FT CONFLICT 207
FT /note="A -> R (in Ref. 1; AAA33229)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="R -> K (in Ref. 1; AAA33229)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1111 AA; 124257 MW; B326A1DDF85B86AC CRC64;
MSKKVQAKQG TDDLVMLPKV SEDEICENLK KRYMNDFIYT NIGPVLISVN PFRNLNNSGP
DFIEAYRGKH AQEVPPHVYQ LAESAYRAMK NDQENQCVII SGESGAGKTE AAKLIMGYVS
AISGSTEKVE YVKHVILESN PLLEAFGNAK TLRNNNSSRF GKYFEIQFDK AGDPVGGKIY
NYLLEKSRVV YQNPGERNFH IFYQLLAGAS AQEKRDYVLS SPESYYYLNQ SQCYTVDGIN
DVSDYAEVRQ AMDTIGLTAQ EQSDIIRIVA CVLHIGNIYF IEDDKGNAAI YDPNALELAA
SMLCIDSATL QNAILFRVIN TGGAGGAGNR RSTYNVPQNV EQANGTRDAL ARTIYDRMFS
WLVERVNQSL SYYKSPYQNV IGILDIFGFE IFEKNGFEQF CINFVNEKLQ QFFIELTLKA
EQEEYVREGI KWEPIKYFNN QIVCDLIEGK SPPGIFSLLD DICSTLHAQS TGTDQKFLEK
MAGIYDGHLH WRGMTGAFAI KHYAGEVTYE AEGFSDKNKD TLFFDLIEAI QCSKMPFLAS
LFNEDTGSLQ KKRPTTAGFK IKTSAGELMK ALSQCTPHYI RCIKPNETKK AKDWENSRVK
HQVQYLGLLE NVRVRRAGFA YRNTFDKVLK RYKKLSSKTW GIWGEWKGDA IEGCKTIFQD
MNLEAGQWQL GKTKVFIRHP ETVFLLEEAL DKKDFDCTAK IQKAFRNWKA KKHSLEQRAQ
IAHMFKDKKE RQRNSIDRKF TSDYIDFENQ FGLQEAMQNA HKKERVVFAD TVIKIDRRAK
QKNYEMVLTD QALYFVEKSI KKKVLVHTLI RRVGLREIKG VSISTLSDNV IVFHLPEHDQ
VIENDKKTEI IIVLVEYFKA IGGGSLNVQF SDRINYTLKK GEQKEISFQK SEQCPTLVVK
KGGKGLIGTI ASGLPSSTDS TPKNYNPNSM SQASSRPAPQ QSAGRGRGMP QGAGQPQPQQ
PQQQQRPMPQ PQQGGGARPM PQPQQGGGAR PMGAPQQGGA PQQGAGRQLP QPTQQGGAPG
GRGAPMGRGA PGGGPAGAGG RPLPTVAKPA PQPSRPTAKA LYDYDASSTD ELSFKEGDII
FIVQKDNGGW TQGELKSGQK GWAPTNYLQY N
