MYOC_DICDI
ID MYOC_DICDI Reviewed; 1182 AA.
AC P42522; Q551D3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Myosin IC heavy chain;
GN Name=myoC; Synonyms=dmiC; ORFNames=DDB_G0276617;
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=AX2;
RX PubMed=7622596; DOI=10.1242/jcs.108.3.1093;
RA Peterson M.D., Novak K.D., Reedy M.C., Ruman J.I., Titus M.A.;
RT "Molecular genetic analysis of myoC, a Dictyostelium myosin I.";
RL J. Cell Sci. 108:1093-1103(1995).
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.
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 [6]
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 [7]
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 [8]
RP DISRUPTION PHENOTYPE.
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 [9]
RP SUBCELLULAR LOCATION.
RX PubMed=11425877; DOI=10.1083/jcb.153.7.1479;
RA Jung G., Remmert K., Wu X., Volosky J.M., Hammer J.A. III;
RT "The Dictyostelium CARMIL protein links capping protein and the Arp2/3
RT complex to type I myosins through their SH3 domains.";
RL J. Cell Biol. 153:1479-1497(2001).
RN [10]
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. Involved in the process of
CC phagocytosis and appears to support streaming behavior.
CC {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, lamellipodium
CC {ECO:0000269|PubMed:11425877, ECO:0000269|PubMed:2797149,
CC ECO:0000269|PubMed:8325874, ECO:0000269|PubMed:8609164}. Note=Found in
CC the leading edge of translocating cells.
CC -!- DISRUPTION PHENOTYPE: Exhibits significant reduction in initial rate of
CC phagocytosis. MyoB and myoC double mutant exhibits profound defects in
CC growth, endocytosis and rearrangement of F-actin. myoB, myoC and myoD
CC triple mutant exhibits reduction in the speed of whole cell
CC translocation. {ECO:0000269|PubMed:8522584, ECO:0000269|PubMed:8609164,
CC ECO:0000269|PubMed:9436992}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC37427.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L35323; AAC37427.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AAFI02000016; EAL69121.1; -; Genomic_DNA.
DR PIR; T30578; T30578.
DR RefSeq; XP_643060.1; XM_637968.1.
DR PDB; 5IBW; X-ray; 1.90 A; C=699-739.
DR PDBsum; 5IBW; -.
DR AlphaFoldDB; P42522; -.
DR SMR; P42522; -.
DR STRING; 44689.DDB0215355; -.
DR PaxDb; P42522; -.
DR EnsemblProtists; EAL69121; EAL69121; DDB_G0276617.
DR GeneID; 8620597; -.
DR KEGG; ddi:DDB_G0276617; -.
DR dictyBase; DDB_G0276617; myoC.
DR eggNOG; KOG0162; Eukaryota.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; P42522; -.
DR OMA; KPMPTPG; -.
DR PhylomeDB; P42522; -.
DR PRO; PR:P42522; -.
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:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0070685; C:macropinocytic cup; IDA:dictyBase.
DR GO; GO:0070687; C:macropinocytic cup cytoskeleton; IDA:dictyBase.
DR GO; GO:1990498; C:mitotic spindle microtubule; IDA:dictyBase.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0097203; C:phagocytic cup lip; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; 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; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; 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:0048870; P:cell motility; IGI:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0046847; P:filopodium assembly; IGI:dictyBase.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0006907; P:pinocytosis; 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 3D-structure; Actin-binding; ATP-binding; Cell projection; Chemotaxis;
KW Motor protein; Myosin; Nucleotide-binding; Reference proteome; SH3 domain.
FT CHAIN 1..1182
FT /note="Myosin IC heavy chain"
FT /id="PRO_0000123367"
FT DOMAIN 15..698
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 774..957
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1123..1182
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 571..593
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 999..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1064..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1049
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1094
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT HELIX 699..736
FT /evidence="ECO:0007829|PDB:5IBW"
SQ SEQUENCE 1182 AA; 132965 MW; C0C772BCC3E71824 CRC64;
MAQQKPEWGN QMKNEGLDDM TLLSKVSNDQ ILDNLKKRFE KDIIYTNIGD VLISVNPFKF
IDGMYSDEVL QEYIGKSRIE LPPHVFAVAE QTYRSMINEK ENQCVIISGE SGAGKTEAAK
KIMQYIADVS GERGSSSNQK VEHVKSIILE TNPLLEAFGN AKTLRNNNSS RFGKYFEIQF
NQKNEPEGGK ITNYLLEKSR VVFQLKGERN FHIFYQFCRG ATPQEQQEFG IYGPENFAYL
TKGDTLDIDG VDDVEEFALT RNAMNVIGIP ANEQKQIFKL LAAILWIGNI DFKEQAGDKV
TIADTSVLDF VSQLLDVPSH FLKTALEFRQ METRHGNQRG TQYNVPLNKT QAIAGRDALA
KAIYDRLFNW LVDRINKEMD NPQKGLMIGV LDIYGFEVFD RNGFEQFCIN YVNEKLQQIF
IEFTLKMEQE EYVREGIKWE PIPFFDNKIV CELIEGKNPP GIFSILDDVC RAVHSQAEGA
DQKLLQSIAV CKSNPHFDTR GNAFCVKHYA GDVVYEGPGM IEKNKDTLLK DHLEILQMSA
NNFLVGLFPD VIDTDSKKLP STAGFKIKSQ AAELVATLMK STPHYIRTIK PNDLKKPNIL
EGGRVLHQVK YLGLLDNIKV RRAGFAYRAT FDRFFQRYYL LSDKTCYAGN NIWKGDALSA
CRAILASQNV DNTQYQIGKT KIFIRYPEML FSLEETRERY WHDMASRIKN AYRNYKAFQF
ECSNRIKNAF RNYKLYRQRC AQTIQGYFRA WKQASPFFDL RMQNEQLFQG RKERNRFSMI
SVRKYFGDYL DVRSQSYFLD AMAEGRNEDV IFSSKSQVMV HPILSANKLS PRFLIVTKQA
IYLIKLKQKK NLATYLLDRR VPLAEVTSFS LSSLADNLLV IHTSTQFDVA VTTEFKTELV
ALINKQKGTT LAVNFGQSIQ YFKKKGSNNT VTFLKDEMHK EIFLKKNQFH IASGLPASTT
VAKVRKNPSQ VSTPSKPIAK PVAKPMVAKP SGGSVIMKKP APAAPPSGPP VMKKPAPTAP
GGAPMMKKPA PAPGGAPMMK KPAPVPGGPA PGGSAIMKPA GGVSKPLPSP TGAPMMKKPA
PTAPGGPAPA GAPTPMMKKP AGQPMMKPIA KPQPTPMKKP AAPPPQQYIA LYEYDAMQPD
ELTFKENDVI NLIKKVDADW WQGELVRTKQ IGMLPSNYVQ QI
