MYOJ_DICDI
ID MYOJ_DICDI Reviewed; 2245 AA.
AC P54697; Q559Y9; Q86A36;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Myosin-J heavy chain;
DE AltName: Full=Myosin-5b;
GN Name=myoJ; Synonyms=myo5B; ORFNames=DDB_G0272112;
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=8636147; DOI=10.1074/jbc.271.12.7120;
RA Hammer J.A. III, Jung G.;
RT "The sequence of the dictyostelium myo J heavy chain gene predicts a novel,
RT dimeric, unconventional myosin with a heavy chain molecular mass of 258
RT kDa.";
RL J. Biol. Chem. 271:7120-7127(1996).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1021.
RX PubMed=8884597; DOI=10.1007/bf00123358;
RA Peterson M.D., Urioste A.S., Titus M.A.;
RT "Dictyostelium discoideum myoJ: a member of a broadly defined myosin V
RT class or a class XI unconventional myosin?";
RL J. Muscle Res. Cell Motil. 17:411-424(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 182-298.
RX PubMed=7937787; DOI=10.1073/pnas.91.20.9446;
RA Titus M.A., Kuspa A., Loomis W.F.;
RT "Discovery of myosin genes by physical mapping in Dictyostelium.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:9446-9450(1994).
RN [6]
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 [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18650439; DOI=10.1074/jbc.m802957200;
RA Taft M.H., Hartmann F.K., Rump A., Keller H., Chizhov I., Manstein D.J.,
RA Tsiavaliaris G.;
RT "Dictyostelium myosin-5b is a conditional processive motor.";
RL J. Biol. Chem. 283:26902-26910(2008).
CC -!- FUNCTION: Processive motor protein that can move over long distances
CC along F-actin without disassociating; processiveness depends on high
CC physiological Mg(2+) concentrations. Presents a high actin affinity in
CC the presence of ADP, fast ATP hydrolysis, and a high steady-state
CC ATPase activity in the presence of actin that is rate limited by ADP
CC release. Physiological decrease of free Mg(2+) ions leads to an
CC increased rate of ADP release and shortening of the fraction of time it
CC spends in the strong acting binding states.
CC {ECO:0000269|PubMed:18650439}.
CC -!- SUBUNIT: Homodimer that associates with six light chains.
CC -!- SUBCELLULAR LOCATION: Contractile vacuole
CC {ECO:0000269|PubMed:18650439}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; U42409; AAA85186.1; -; Genomic_DNA.
DR EMBL; AAFI02000008; EAL71208.1; -; Genomic_DNA.
DR EMBL; L35322; AAA79858.1; -; Genomic_DNA.
DR PIR; T18278; T18278.
DR RefSeq; XP_645195.1; XM_640103.1.
DR AlphaFoldDB; P54697; -.
DR SMR; P54697; -.
DR STRING; 44689.DDB0185050; -.
DR BindingDB; P54697; -.
DR ChEMBL; CHEMBL1781867; -.
DR PaxDb; P54697; -.
DR PRIDE; P54697; -.
DR EnsemblProtists; EAL71208; EAL71208; DDB_G0272112.
DR GeneID; 8618367; -.
DR KEGG; ddi:DDB_G0272112; -.
DR dictyBase; DDB_G0272112; myoJ.
DR eggNOG; KOG0160; Eukaryota.
DR HOGENOM; CLU_000192_3_1_1; -.
DR InParanoid; P54697; -.
DR OMA; ICCAGFP; -.
DR PhylomeDB; P54697; -.
DR PRO; PR:P54697; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0042641; C:actomyosin; IDA:dictyBase.
DR GO; GO:0000331; C:contractile vacuole; IDA:dictyBase.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR GO; GO:0043531; F:ADP binding; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IDA:dictyBase.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IDA: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:0140027; P:contractile vacuole localization; IMP:dictyBase.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR002710; Dilute_dom.
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 Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 3.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 3.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 3: Inferred from homology;
KW Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil; Motor protein;
KW Myosin; Nucleotide-binding; Reference proteome; Repeat; Vacuole.
FT CHAIN 1..2245
FT /note="Myosin-J heavy chain"
FT /id="PRO_0000123372"
FT DOMAIN 25..77
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 81..821
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 824..851
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 872..901
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 943..972
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1969..2188
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 646..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..749
FT /note="Actin-binding"
FT REGION 1504..1524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 973..1812
FT /evidence="ECO:0000255"
FT COMPBIAS 1509..1524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 174..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 191
FT /note="F -> L (in Ref. 1; AAA85186)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="T -> A (in Ref. 1; AAA85186)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="R -> G (in Ref. 1; AAA85186)"
FT /evidence="ECO:0000305"
FT CONFLICT 332..347
FT /note="NKSGCFEIEGVSDEEH -> IEWMFELKVYRMKS (in Ref. 4;
FT AAA79858)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="K -> N (in Ref. 1; AAA85186)"
FT /evidence="ECO:0000305"
FT CONFLICT 865..866
FT /note="QQ -> HH (in Ref. 1; AAA85186)"
FT /evidence="ECO:0000305"
FT CONFLICT 1041
FT /note="K -> N (in Ref. 1; AAA85186)"
FT /evidence="ECO:0000305"
FT CONFLICT 1389
FT /note="Q -> P (in Ref. 1; AAA85186)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2245 AA; 258684 MW; 4DA40956515A7685 CRC64;
MTTSTIENGA SSPIIVSSST PKLYQEGAGV WIPDQELGWI GADVIEHSET SADQVLVRTE
DDREVKIPLS KVFQKNPDIL EGVDDLSFLS HLHEPAILHN LHHRYNLNQI YTYIGKILIA
INPYTSLPLY GKEMISAYYG KQLGTLAPHV YAVAEDAFKD MRYDGTSQSI LVSGESGAGK
TETTKFLLQY FAAMGNMIKE STSSSSINGI NTSSDGIPVT PPPSPMKKSP VDKSVEERVL
ESTPLLEAFG NAKTLRNDNS SRFGKFIEIH FNEMGSIIGA KILTYLLEKS RIVRQVYNER
NYHIFYQLLS GASEELKEKL NLKTIEEYSY LNKSGCFEIE GVSDEEHFNK TCHAMQVAGI
TLVEQENVFR ILSAILLIGN FEFENIAGSN DDSCQLIDRD PLEKVSVLLG CAQPDELLNS
MLTRKVVTGK ESYISHNTKE RAENARDSLS MFLYGMMFDW LVVKINSSMS ISTQQKSKSF
IGVLDIYGFE SFEVNGFEQF CINYANEKLQ QLFNQHVFKE EQQEYIKEKI DWSYIDFNDN
QDTLDLIEKK PICILTLLDE ETMFPKATPQ TLATKLYSKM TSHSKFEKPR FSSTAFTINH
YAGKVTYETD QFLDKNKDFI IPEQISILQR SNFSFIKVLM SHSDKFTQSP GGHPQGNGGP
TSSNTKGTSG SSSMKFLSVG SQFSTSLATL MKTISTTTPH YVRCIKPNPE KLPQTFNKQD
VIHQLRCGGV MESVRICCAG FPTRRLLSEF YQRYKILYVK DINTGSGGGK KGSNNNKIKD
PKILVQNLLT GIELSDDKYK IGLTKVFLRA GQLASLEDMR LEQLDRSATV IQKRWKGYLY
RKRYKQLRDA SLIIQTKLRS VHAKQQLSAL QRTHSAILIQ KVWRAHRDRV QYQKIRDASL
QLQTVMRRHL FSEQVHRERC ENAAIILQTK IRQILSKREV DKKLRGIILI QARWRMKLAK
RVYIQLRAEA RSLRTVQEQK NKLQEKLEEL QWRLTSEAKR KQQLEDQKVK SDTTISELSS
NNDHLELQLS EIQLKYQELD KSNQSSQLQL SECLSKLEEQ TQQLDHSSKL NKKLEKDLSD
QHDSIEKLQS QFNETEQQLQ QFKQQSEELS SKLSKTTQQL DFNKQEFDRL SQERDTDNTN
NQLEIQQLKK ANSTLEEDYF SLSGIRDNLE RQVLELRDEN QLIKERLDSL GQQSSQFQSG
AALEKQQLEQ LVQEQSEQLI KLSSEKLGSE EEAKKQINQL ELELTDHKSK LQIQLQLTEQ
SNEKIKKLKG KLEEYQDEKK QLQQELERIK QSKQSVEDEK NSLITQLTTV KFESTQVSTN
VSHQKEKITT LKSTIEELNK SIGKLQAEQK NKDDEIRKIQ FELNDQKQQF TRQTKEFSDL
QSQQSIDRQK SEITIHSLER TNETLKSDFE RVQQSLKQQE RDCQQYKDTI NRLENEVKQL
TQLKERFENE FFVAKEQNSN QTQESVYLKE VTTQMQQNQS RIERELEEKK QHITRIDDER
DELKKQLTQL QQQHEQSSTQ LLLAQNELER LRKKELKYKE RGHETSKQQD QFNMEIQSLR
ITNNDQLKSL QDYEQEKKKL KDKLSSSKQE AQQQRESIIK MDAELSAIKQ HSQWVENSFT
DMKQRNQELI ESSALYKQQL LQQTSTIDST IKEKENEISK LQQQLETSNQ QLHQLKEELN
SMKQSNQLES TEQSKQLNQL IQENQQLKSV TNEISKQLDD AVFENQKINN TIKEQEIKSK
RMSVELQQHI DEGKQQEIQQ LQSTIAQLKQ QQQSETDRLE KEIQQMKRER ETQMKLVEST
KLNYHMLEDR MELYRNVMEI IDYKETEWEK LARLAGCKEL DTKLLSDFLL SCKLEHTSLG
SQMWFHQIDY WCPYERDSSK GIFYGIIRSI VDFTIKNFDD VDLLSYLLAC CSLTLFLYKK
NLVKHLNGAN SIMPIIPTLG DLEELNERLS HQSLTTSGKF SGGGGGGGID FIDQLQQSTG
ITFGLIFKAT TLKLSPLVDG AILNENYNKK LTSISASSFG SGSFGLGSNG VGSVLSIELI
TTYLSSIITI FQHRMVHFTL SQRFFNQVFC WIGALIMKGF MLRQTFCTET FATFVKTKID
FLTRWADDIG NVWVGDVANA FQQVREVINV LNIKDKEKII DDKIRKQYCP TLNSNQLKQV
LSLFSPGEFG GKRVSAKVIA SICPPNKSSA GQSFVQDENK LNTIPIDSLH YLEIQDIKTL
SLPLSIRQTI ETEIINLKQQ IACKK
