ID MYOK_DICDI Reviewed; 858 AA.
AC Q9XXV8; Q555W0; Q86J00; Q9UA70;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=Myosin-K heavy chain;
GN Name=myoK; Synonyms=myoIG; ORFNames=DDB_G0274575;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=AX2;
RX PubMed=10049776; DOI=10.1006/bbrc.1999.0264;
RA Yazu M., Adachi H., Sutoh K.;
RT "Novel Dictyostelium unconventional myosin MyoK is a class I myosin with
RT the longest loop-1 insert and the shortest tail.";
RL Biochem. Biophys. Res. Commun. 255:711-716(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
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 [3]
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 [4]
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 [5]
RP FUNCTION.
RX PubMed=10652255; DOI=10.1242/jcs.113.4.621;
RA Schwarz E.C., Neuhaus E.M., Kistler C., Henkel A.W., Soldati T.;
RT "Dictyostelium myosin IK is involved in the maintenance of cortical tension
RT and affects motility and phagocytosis.";
RL J. Cell Sci. 113:621-633(2000).
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).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Involved in phagocytosis and motility, and in the maintenance and
CC dynamics of cell cortex. {ECO:0000269|PubMed:10049776,
CC ECO:0000269|PubMed:10652255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10403059}.
CC Note=Enriched in actin cortex regions.
CC -!- DEVELOPMENTAL STAGE: Expression stimulated at early developmental
CC stages, before aggregation. {ECO:0000269|PubMed:10049776}.
CC -!- DOMAIN: The head domain possess two actin-binding sites, a classic ATP-
CC dependent one and a secondary salt-dependent one (located inside the
CC GPR domain).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; AB017909; BAA76319.1; -; Genomic_DNA.
DR EMBL; AF090534; AAD47904.1; -; mRNA.
DR EMBL; AAFI02000012; EAL70180.1; -; Genomic_DNA.
DR PIR; JG0183; JG0183.
DR RefSeq; XP_643950.1; XM_638858.1.
DR AlphaFoldDB; Q9XXV8; -.
DR SMR; Q9XXV8; -.
DR BioGRID; 1244381; 1.
DR STRING; 44689.Q9XXV8; -.
DR PaxDb; 44689-DDB0185086; -.
DR EnsemblProtists; EAL70180; EAL70180; DDB_G0274575.
DR GeneID; 8619378; -.
DR KEGG; ddi:DDB_G0274575; -.
DR dictyBase; DDB_G0274575; myoK.
DR eggNOG; KOG0162; Eukaryota.
DR HOGENOM; CLU_000192_7_5_1; -.
DR InParanoid; Q9XXV8; -.
DR OMA; WKDISFF; -.
DR PhylomeDB; Q9XXV8; -.
DR PRO; PR:Q9XXV8; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0032009; C:early phagosome; IDA:dictyBase.
DR GO; GO:0070685; C:macropinocytic cup; IDA:dictyBase.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0001891; C:phagocytic cup; IDA:dictyBase.
DR GO; GO:0097203; C:phagocytic cup lip; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; IDA:dictyBase.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
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:0005522; F:profilin binding; IPI:dictyBase.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0043327; P:chemotaxis to cAMP; IBA:GO_Central.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:dictyBase.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:dictyBase.
DR GO; GO:2000147; P:positive regulation of cell motility; IMP:dictyBase.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:dictyBase.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF743; MYOSIN-K HEAVY CHAIN; 1.
DR Pfam; PF00063; Myosin_head; 2.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; ATP-binding; Cytoplasm; Motor protein; Myosin;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..858
FT /note="Myosin-K heavy chain"
FT /id="PRO_0000328607"
FT DOMAIN 7..820
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 121..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..722
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 821..858
FT /note="Tail"
FT COMPBIAS 178..231
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 659
FT /note="Y -> C (in Ref. 2; AAD47904)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 858 AA; 94364 MW; E459F2AFDC9C2C1E CRC64;
MFRLFSSGVD DLVLVSNPSN GEVTSQIGAR FDRELIYTNI GEVLIAVNPY KALPITGPEF
IKLYQNASGS DASPHIYALA ERAYRRMVDE NESQCVIISG ESGAGKTVSA KLILQYVTSV
SPNNSSGGGI GGSGGGNGGI PQYDGGSDDR PSPPMGRGMG MPGMVGRGGL PTRGGGPPSR
GGGPPPTRGR GGPPPPIPQN RGAPPPVSNG GAPPPVARGP VAPPPTRGAP PTRGGGPANR
GGRGGGPPPV STSRGGGGYG GSSKTVDVEH IKKVILDSNP LMEAIGNAKT VRNDNSSRFG
KYLEIQFDDN NAPVGGLIST FLLEKTRVTF QQKNERNFHI FYQMLGGLDQ TTKSEWGLTQ
ATDFYYLAQS KCTTVEDVDD GKDFHEVKAA METVGISRDE QTEIFRILAA ILHVGNIRFQ
GEAPASVIDE TPLQWAASLL GCDPTFLCQS LNHRQIQSGS ARHTQYQVPQ NPDQSAGLRD
ALAKTLYERI FDFIVARVNK AMSFSGNCKV IGVLDIYGFE VFERNSFEQF CINYVNERLQ
QIFIDLTVRG EQREYHEEGM KWKDISFFDN KIVVDLIDGN KPPGIMRVLD DVCKTVHAVD
SAAADIKFME KLIHSIQSHP HLVISNTGSS ADEFTIKHYA GEVSYSIEEF CFKNNDNLYA
SIVGCLQNST YQFIVSLFPE NIQDNKQAPT TSSFKIRQSS SYLVTRLSAC TPHYIRCIKP
NDKKQPMNFV SSRVEHQVKY LGILENIKVK RSGYAYRQLK DIFLNRFGKI MDVQPRNVQE
FVEYITRTHK DINADEFEEG KTKIFVKNPE TIFVMEDLLM QKIDPIGYKN RVQAYKENEK
LAQMKQGKHS MKQKCLIQ
//
