MYOF_DICDI
ID MYOF_DICDI Reviewed; 1071 AA.
AC P54695; Q54HT0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Myosin IF heavy chain;
GN Name=myoF; ORFNames=DDB_G0289177;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 143-228.
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 [3]
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.
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 -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; AAFI02000131; EAL62822.1; -; Genomic_DNA.
DR EMBL; L35319; AAA61401.1; -; Genomic_DNA.
DR RefSeq; XP_636359.1; XM_631267.1.
DR AlphaFoldDB; P54695; -.
DR SMR; P54695; -.
DR STRING; 44689.DDB0220021; -.
DR PaxDb; P54695; -.
DR PRIDE; P54695; -.
DR EnsemblProtists; EAL62822; EAL62822; DDB_G0289177.
DR GeneID; 8627032; -.
DR KEGG; ddi:DDB_G0289177; -.
DR dictyBase; DDB_G0289177; myoF.
DR eggNOG; KOG0164; Eukaryota.
DR HOGENOM; CLU_000192_7_7_1; -.
DR InParanoid; P54695; -.
DR OMA; DQHIYKY; -.
DR PhylomeDB; P54695; -.
DR PRO; PR:P54695; -.
DR Proteomes; UP000002195; Chromosome 5.
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:0005911; C:cell-cell junction; IDA:dictyBase.
DR GO; GO:0070685; C:macropinocytic cup; IDA:dictyBase.
DR GO; GO:0070687; C:macropinocytic cup cytoskeleton; IDA:dictyBase.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0031143; C:pseudopodium; IDA:dictyBase.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:dictyBase.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030041; P:actin filament polymerization; IGI:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IGI:dictyBase.
DR GO; GO:0048870; P:cell motility; IMP:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IGI:dictyBase.
DR GO; GO:0120320; P:lateral pseudopodium retraction; IMP:dictyBase.
DR GO; GO:0030011; P:maintenance of cell polarity; IMP:dictyBase.
DR GO; GO:0006911; P:phagocytosis, engulfment; IGI: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; IPR000048; IQ_motif_EF-hand-BS.
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 Pfam; PF00612; IQ; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51757; TH1; 1.
PE 3: Inferred from homology;
KW Actin-binding; ATP-binding; Calmodulin-binding; Motor protein; Myosin;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..1071
FT /note="Myosin IF heavy chain"
FT /id="PRO_0000123370"
FT DOMAIN 40..736
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 739..768
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 870..1069
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT REGION 610..632
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT BINDING 134..141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 173..174
FT /note="NI -> DV (in Ref. 2; AAA61401)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1071 AA; 124048 MW; B8419B77F9518F72 CRC64;
MEPLPLENED NQLNSNKSTT VSSKNFSNIF HNNIHNKDVV GLTDMCFLEN VEENELMNNL
QNRFNKDHIY TYIGEQVISV NPFSNKANIY TEQVLKSYQN MYMYEVSPHI YALAQDTYKK
LLLSKESQCV IITGESGSGK TEASKIFLNY ISKVCSGNLE NIQGIMRLII ESNIVLESFG
NAKTLRNDNS SRFGKFIEIE FDGKGSPISG KISQFLLEKS RVHSRAIGER SFHVFYQFLT
DKRITSKLGL SNDPTQYKYL KDSMCFSISS INDSKDFQKV LESLKQLAWT EQEMESIWRV
LGAILLIGNI EFSNDVEKSN VDAVYISTPE TLKKVSQLLQ CSEDSLEKSL ISRSLTLGAG
KRQSSIKVLL NQTQAKETRD AFSKVLYDRL FTSIIDKINS TISSKSNNGS NYIIESTIGI
LDIYGFEIFE NNSFEQFIIN YSNEKLQQLF INLVLRQEQE EYLKEGIEWK TIDNYFDNTP
IIDLIEGQPV GLLKLLEEAC LIGQSTPELL IQKFNQFFSK NKHFESFETS NNLSIESQSF
TLKHYASPVT YNLDSFIYKN KDPLYQDLIF TMESSKDKFI LSLFNKDFQK NSLGVKKIPI
TAATQFKNAI NDLIGKLNTC QPHYIRCIKS NEDKRSNHFD YEAVRHQVRY LNMLETIRVR
KAGYCHKQHY TRFLGRYKMI SKETWPFWNG TPKDGVMAIV RAASAIQNST SECQFGKKKL
FIKSASTLFH FEELRQKILP SIVITIQRVW RGYKVRKWYK QELQRLREEK EEIQKQIKRK
NSANLIQTYY LRYKVLTYIK KLKPWSVGPH YNKGHIMPTL WLRRTPIDSL MQSIHIIWWA
KVKVTSLSME ARSLVRQKIL ALDLFGMGYS RKKEWDCRRK FQADYLSDDS NPKKSQFSES
VQAMFQKGGD KEILFADNVI KINKRGKSQL RSLIITDQHI YKYDTKKYTQ KKVGLKLHSI
VALSTSNKKD TFLAIHFKQP IRDLYIDLGC DFVEKVSEVC TNLVQQVYKL TGTTIPLVFR
DPLTFNNSRD SRNNGTDFVV SFSQYPKGKE QRQSTFVKGK GNTAIVYYNL D
