MYOM_DICDI
ID MYOM_DICDI Reviewed; 1737 AA.
AC Q9TW28; Q54DE0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Myosin-M heavy chain;
DE AltName: Full=RhoGEF domain-containing protein myoM;
GN Name=myoM; Synonyms=racGEF; ORFNames=DDB_G0292262;
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].
RC STRAIN=AX2;
RX PubMed=10403059; DOI=10.1007/bf02738122;
RA Schwarz E.C., Geissler H., Soldati T.;
RT "A potentially exhaustive screening strategy reveals two novel divergent
RT myosins in Dictyostelium.";
RL Cell Biochem. Biophys. 30:413-435(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=AX2;
RX PubMed=10828443; DOI=10.1016/s0014-5793(00)01564-7;
RA Oishi N., Adachi H., Sutoh K.;
RT "Novel Dictyostelium unconventional myosin, MyoM, has a putative RhoGEF
RT domain.";
RL FEBS Lett. 474:16-22(2000).
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 FUNCTION, DEVELOPMENTAL STAGE, DOMAIN, AND SUBUNIT.
RX PubMed=11208126; DOI=10.1034/j.1600-0854.2000.010505.x;
RA Geissler H., Ullmann R., Soldati T.;
RT "The tail domain of myosin M catalyses nucleotide exchange on Rac1 GTPases
RT and can induce actin-driven surface protrusions.";
RL Traffic 1:399-410(2000).
RN [5]
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: Myosins are actin-based motor molecules with ATPase activity.
CC Involved in macropinocytosis and remodeling of actin cytoskeleton.
CC {ECO:0000269|PubMed:11208126}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11208126}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10828443}.
CC Note=Enriched in actin cortex regions.
CC -!- DEVELOPMENTAL STAGE: Expressed (in low abundance) during the first half
CC of the developmental cycle. {ECO:0000269|PubMed:11208126}.
CC -!- DOMAIN: DH (RhoGEF) domain interacts with Rac1-related GTPases.
CC {ECO:0000269|PubMed:11208126}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; AF090533; AAD47903.1; -; mRNA.
DR EMBL; AB017910; BAA84604.1; -; Genomic_DNA.
DR EMBL; AAFI02000189; EAL61255.1; -; Genomic_DNA.
DR PIR; A59235; A59235.
DR RefSeq; XP_629701.1; XM_629699.1.
DR AlphaFoldDB; Q9TW28; -.
DR SMR; Q9TW28; -.
DR STRING; 44689.DDB0191100; -.
DR PaxDb; Q9TW28; -.
DR PRIDE; Q9TW28; -.
DR EnsemblProtists; EAL61255; EAL61255; DDB_G0292262.
DR GeneID; 8628615; -.
DR KEGG; ddi:DDB_G0292262; -.
DR dictyBase; DDB_G0292262; myoM.
DR eggNOG; KOG0160; Eukaryota.
DR eggNOG; KOG3519; Eukaryota.
DR HOGENOM; CLU_239802_0_0_1; -.
DR InParanoid; Q9TW28; -.
DR OMA; IYTWIGN; -.
DR PhylomeDB; Q9TW28; -.
DR PRO; PR:Q9TW28; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:dictyBase.
DR GO; GO:0000146; F:microfilament motor activity; IDA:dictyBase.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006972; P:hyperosmotic response; IMP:dictyBase.
DR GO; GO:0006971; P:hypotonic response; IMP:dictyBase.
DR GO; GO:0031268; P:pseudopodium organization; IMP:dictyBase.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; IDA:dictyBase.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.850.10; -; 2.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Coiled coil; Cytoplasm; Motor protein; Myosin;
KW Nucleotide-binding; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..1737
FT /note="Myosin-M heavy chain"
FT /id="PRO_0000328608"
FT DOMAIN 4..55
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 59..886
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 889..918
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 912..941
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1389..1572
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 1603..1714
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 640..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..761
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 947..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 926..1039
FT /evidence="ECO:0000255"
FT COMPBIAS 947..1036
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1174
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 154..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1737 AA; 195862 MW; 39CBF9C08EFEF856 CRC64;
MKHLEGDIVW VPHTVNGYCR GKIIGYNEKN QVTVRLLELN EEIKINEQLI QNYNQSDDKD
FSDMVEIQDL SEAIILNNLG LRYKSDQIYT YIGNVLISIN PYKEIKDIYS LNILNKYKDI
NTIKSNPPHI YAVALRAYQS MVSEKKNQSI IISGESGSGK TEASKTILQY LINTSNSNSN
NNTNINNNNN SIEKDILNSN PILEAFGNSR TTKNHNSSRF GKFLKIEFRS SDMKIDGASI
ETYLLEKSRI SHRPDVNNLS YHIFYYLVMG ASKEERERLG LDNDPSKYRY LDASTSVIES
FKKQSNGGSG GGSGNNDLSE SLQLVKQSLE SMSIAKEQCD DIFLTLAAIL HLGNIEFEVD
QTENEQTSGF SKISEQKASV KKSLSMVSKL LGYPEQVFKQ TLLNRNLKGG GRGSVYCRPM
EVYQSEQTRD ALSKALYVRL FASIVEKINV KFIQNTGSKD LQGGYSSKRN NLFIGVLDIF
GFENLSSNSL DQLLINFTNE KLQQQFNLNV FENEQKDYLQ EGIPWSTSNF IDNKECIELF
EKKSYGLLSL LDDECMMPKG SEVTLLEKYN KQYHNTNQYY QRTLAKGTLG IKHFAGDVTY
QTDGWLEKNR DSIPTEVEQL LSASSNNLIK SLFNLKELNK SNDNNSNNNN SNNNSSSSSS
SQSTASITAK ASPPRERFNS GSGSGTTSPL NLSGSSSPLS GSGSYSIIGG NSNSNSNNNN
SSNNKKSQSV SVAGQFIEQL NKLISTINST SVHYIRCIKP NVTMDCNNFN NSHVLSQLRN
VGVLNTVKVR KMGYSYRRDF IQFYSRYNCI LNSLNIKINL TNINHSNLCK EILENVNSQY
KNNNNNKNNN NQIVKITTNS KPTFQIGKTK IFISDELYIY LEKKRYDSLV DSVLKIQAFF
KMIKIRNQYK RNKESSLFLQ TLIRAQRAKK DFEQLVILEN KRKEEERKKE LERQRKEEEE
RQKELERQRR EEEKELERKR KEEERELERQ RKEEEKEQER KRKEEEKEQE RKKKEEKEIE
KKRKEEEKKK KKNEQNLSLP SLDITNSPSL INTTTTTTTT TTTTTNTSSP PLSPPISPRP
STPSSTSSSS STTSSPSTKK QLLFKFNSIS NLLSKSLHGS SHSDKNSKED NNSNNNNNGD
STIILSSDSS FGQPTPKATS TPTPPPPPPL KTQPVPISSG VENNSSPNLW SHRNSPNFNG
LVREKSRARI GRLTIRSASP LDLTYLPDPS KNEGSPQFTS QSLDFTPNIP PIITNSIVEQ
QSSLSGINKP IPQRTISSSE NSPLSRANSS ISSSLLILTP TLTSLSTSTT PSTPTTPKTP
TTLSSSSVST STSLSSVSSS VSSSSSSSIP TPIIESTPSN SNEDLITTLS SPISTGHTGE
SIEEKNKRFR IKIINELIET ERDYVRDLNI VVEVFLNPIR EKQLLSAKDI NSLFSNIEIL
FSINMNVLKA LEKDKDPLCE NISVGQTFLD MSHYLKMYTT YCSNQQNALK ILEEEKIKNQ
PFREYLEFCM NDSVCRGLPL NSFIIKPVQR ICKYPLLIKE TIKFTPNDHP DKPALEEVDK
KISDIVQSIN EAKRTLELFQ KIVDLQNSID GLEDTNLMEQ GRTLLMEGTV SAVKELNSED
SLSRTLFLFN NLILICSFGT NVLSTAINQF KTKKLKLKAK IPISDSRLIF VSDTDSVKYA
LEIVNIKEDS NYILCFNNDQ DRSKWFKQIK ALIQEQKLSN AKKAATIGNS RLIQTTS
