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Myosin ID heavy chain

 MYOD_DICDI              Reviewed;        1109 AA.
P34109; Q553G7; Q869M0;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
07-NOV-2003, sequence version 2.
07-JUN-2017, entry version 119.
RecName: Full=Myosin ID heavy chain;
Name=myoD; Synonyms=dmiD; ORFNames=DDB_G0275447;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 604-610; 733-742 AND
914-928, AND SUBCELLULAR LOCATION.
STRAIN=AX3;
PubMed=8325874;
Jung G., Fukui Y., Martin B., Hammer J.A. III;
"Sequence, expression pattern, intracellular localization, and
targeted disruption of the Dictyostelium myosin ID heavy chain
isoform.";
J. Biol. Chem. 268:14981-14990(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=12097910; DOI=10.1038/nature00847;
Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A.,
Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G.,
Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A.,
Platzer M., Rosenthal A., Noegel A.A.;
"Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
Nature 418:79-85(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
[4]
SUBCELLULAR LOCATION.
PubMed=2797149; DOI=10.1038/341328a0;
Fukui Y., Lynch T.J., Brzeska H., Korn E.D.;
"Myosin I is located at the leading edges of locomoting Dictyostelium
amoebae.";
Nature 341:328-331(1989).
[5]
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=8980908;
Morita Y.S., Jung G., Hammer J.A. III, Fukui Y.;
"Localization of Dictyostelium myoB and myoD to filopodia and cell-
cell contact sites using isoform-specific antibodies.";
Eur. J. Cell Biol. 71:371-379(1996).
[6]
SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=8609164; DOI=10.1083/jcb.133.2.305;
Jung G., Wu X., Hammer J.A. III;
"Dictyostelium mutants lacking multiple classic myosin I isoforms
reveal combinations of shared and distinct functions.";
J. Cell Biol. 133:305-323(1996).
[7]
NOMENCLATURE.
PubMed=16857047; DOI=10.1186/1471-2164-7-183;
Kollmar M.;
"Thirteen is enough: the myosins of Dictyostelium discoideum and their
light chains.";
BMC Genomics 7:183-183(2006).
-!- FUNCTION: Myosin is a protein that binds to actin and has ATPase
activity that is activated by actin. Myosin id may have a role in
chemotaxis and aggregation; it could serve to stabilize and even
retract cortical structures, such as pseudopods and lamellopods.
Involved in the process of phagocytosis.
{ECO:0000269|PubMed:8609164}.
-!- SUBUNIT: Myosin I heavy chain is single-headed. Dimer of a heavy
and a light chain. Inability to self-assemble into filaments.
-!- SUBCELLULAR LOCATION: Cell projection, pseudopodium. Cytoplasm,
cell cortex. Note=Highest concentration just beneath the plasma
membrane in the anterior pseudopod at the leading edge of the
cell.
-!- DEVELOPMENTAL STAGE: Found at leading edges of lamellipodia and at
sites of cell-cell contact in stationary stage cells. Also present
in filopodia. Largely disappears from lamellipodia and cell-cell
contact regions in aggregation stage cells, suggesting the
occurrence of a developmentally regulated relocalization to the
cytoplasm. {ECO:0000269|PubMed:8980908}.
-!- DOMAIN: Myosin tail domain binds directly to anionic phospholipid
membranes; myosins I could therefore move actin relative to
membranes and vice versa. TH.2 and SH3 bind tightly to F-actin;
this together with the nucleotide-sensitive site in the head,
allows single molecules of myosin I to cross-link actin filaments.
-!- DISRUPTION PHENOTYPE: MyoB and myoD double mutant exhibits
reduction in the speed of whole cell translocation. myoB, myoC and
myoD triple mutant exhibits reduction in the speed of whole cell
translocation. {ECO:0000269|PubMed:8609164}.
-!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
superfamily. Myosin family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L16509; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AAFI02000013; EAL69474.1; -; Genomic_DNA.
PIR; A47106; A47106.
RefSeq; XP_643446.1; XM_638354.1.
ProteinModelPortal; P34109; -.
SMR; P34109; -.
STRING; 44689.DDB0191347; -.
PaxDb; P34109; -.
PRIDE; P34109; -.
EnsemblProtists; EAL69474; EAL69474; DDB_G0275447.
GeneID; 8620031; -.
KEGG; ddi:DDB_G0275447; -.
dictyBase; DDB_G0275447; myoD.
eggNOG; KOG0162; Eukaryota.
eggNOG; COG5022; LUCA.
InParanoid; P34109; -.
KO; K10356; -.
OMA; FNRWRAS; -.
PhylomeDB; P34109; -.
PRO; PR:P34109; -.
Proteomes; UP000002195; Chromosome 2.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
GO; GO:0031143; C:pseudopodium; IEA:UniProtKB-SubCell.
GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
GO; GO:0030898; F:actin-dependent ATPase activity; IDA:dictyBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003774; F:motor activity; IEA:InterPro.
GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
InterPro; IPR001609; Myosin_head_motor_dom.
InterPro; IPR010926; Myosin_TH1.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR001452; SH3_domain.
Pfam; PF00063; Myosin_head; 1.
Pfam; PF06017; Myosin_TH1; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00193; MYOSINHEAVY.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00242; MYSc; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS51456; MYOSIN_MOTOR; 1.
PROSITE; PS50002; SH3; 1.
PROSITE; PS51757; TH1; 1.
1: Evidence at protein level;
Actin-binding; ATP-binding; Cell projection; Chemotaxis;
Complete proteome; Cytoplasm; Direct protein sequencing;
Motor protein; Myosin; Nucleotide-binding; Phagocytosis;
Reference proteome; SH3 domain.
CHAIN 1 1109 Myosin ID heavy chain.
/FTId=PRO_0000123368.
DOMAIN 7 687 Myosin motor.
DOMAIN 725 919 TH1. {ECO:0000255|PROSITE-
ProRule:PRU01093}.
DOMAIN 958 1017 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
NP_BIND 101 108 ATP. {ECO:0000250}.
COMPBIAS 493 496 Poly-Ser.
COMPBIAS 1018 1109 Ala/Gly/Pro-rich (TH.2).
COMPBIAS 1036 1040 Poly-Thr.
CONFLICT 613 613 I -> IFGRI (in Ref. 1; L16509).
{ECO:0000305}.
CONFLICT 694 694 A -> R (in Ref. 1; L16509).
{ECO:0000305}.
CONFLICT 837 837 T -> R (in Ref. 1; L16509).
{ECO:0000305}.
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


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