MYOH_DICDI
ID MYOH_DICDI Reviewed; 1771 AA.
AC P54696; B0G166; Q54HG3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Myosin-H heavy chain;
DE AltName: Full=Myosin-5a;
GN Name=myoH; Synonyms=myo5A; ORFNames=DDB_G0289447;
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 163-261.
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; AAFI02000141; EDR41040.1; -; Genomic_DNA.
DR EMBL; L35320; AAA61402.1; -; Genomic_DNA.
DR RefSeq; XP_001733030.1; XM_001732978.1.
DR AlphaFoldDB; P54696; -.
DR SMR; P54696; -.
DR STRING; 44689.DDB0233685; -.
DR PaxDb; P54696; -.
DR PRIDE; P54696; -.
DR EnsemblProtists; EDR41040; EDR41040; DDB_G0289447.
DR GeneID; 8627161; -.
DR KEGG; ddi:DDB_G0289447; -.
DR dictyBase; DDB_G0289447; myoH.
DR eggNOG; KOG0160; Eukaryota.
DR HOGENOM; CLU_000192_3_1_1; -.
DR InParanoid; P54696; -.
DR OMA; ISELEHW; -.
DR PhylomeDB; P54696; -.
DR PRO; PR:P54696; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
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:0007015; P:actin filament organization; IBA:GO_Central.
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; 2.
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; 2.
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.
FT CHAIN 1..1771
FT /note="Myosin-H heavy chain"
FT /id="PRO_0000123371"
FT DOMAIN 7..57
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 61..840
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 843..872
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 866..895
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 940..969
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1427..1695
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 690..712
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 1070..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1312..1343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1180..1224
FT /evidence="ECO:0000255"
FT COMPBIAS 1078..1139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 154..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1771 AA; 200699 MW; EC9F967E85776177 CRC64;
MMIDNNCGKE KVWVPNPEKG WINGDLIKEI PGEGWLVRDE NGKEIKIEKD ELRMQNPVIQ
EGIDDMTSLS HLHEAAVIHN LIKRYEINSI YTYTGSILIA INPYTKLPIY SKEMIESFCD
QPVSKLAPHV YSIAESAYRE MLNFQKNQSI LVSGESGAGK TETTKFLLQY FAAMGEKGNG
VNTSLISEED IVEGNNIETQ VIKSTPILEA FGNSKTLRND NSSRFGKFIE IHFDKIKGTI
VGAKLETYLL EKSRIVKPPE NERGYHIFYQ LIKGFNNSCC LKNSSNNNKD EDSSSSSNNN
IDDLKSLLKC KASDFNYLIS SGCDSIDGVD DSQVFIKTEN ALKVMGLSND ELIGIYKILL
SILHIGNIEF EKGKEEDSSI IKYGNSSFGE SFSDDDAGGY NPLEISCKLL GCSVDSLKST
FCSRKMKAGN ESYTINHTVE QASQARDSLS MFLYSRLFDW LVVRINQSID KIGTEKKDNS
FLFIGILDIY GFESFESNSY EQFTINYANE KLQNQFNHQI FKLEQLEYEK EKIDWSYIEF
SDNQECIDLI EKKPLGILSI LDEESQFPKS TPSTLCTKLY NNHSKSKNFE KPRFSQTHFI
IDHYAGKVEY DTNLFLEKNK DFIISEQVSA LESSNWKFLT NLFQILSKKM NGGGGTSGGG
GAGGNKASSS AAGKSTFKFT SVSSQFKESL NSLMTTINST NPHYIRCIKP NTEKRANLFD
NVMVLHQLRC SGVIEQLRIS RSGYPSRLVY DNFIKRYKLI VAKDFKNDDD SNESKEWNSI
LKETDLNSSN GGTNNQIELK RKGAELMINK LSIDISSVQF GLTKLFFKSG IIANLELLRS
QTMINSATFI QKIWRGYTDR KAYTSTKHSS IYFQSLIRSY LQQLEYNSMV EENSAIHLQS
LIRTNELEKQ FNQLLSTTIH FQSLLRRLED SKEFNTLMDR IKKIVKIQSL WRSNLAKKQL
KLLKAEAKSL TNVVAEKNKL ASKLGDIQSK LDMESQLAQK IKNENEQLSS QFSNIQIEKE
KLQKDFGNIN LEKEELLLKY SALESEYHQY KQQNELIISK LKQHINDLEE KQHQHSYKNN
EVVGNTSFEG STTTNNGVTS PPKSSPASPI RNSINSNSDT TISGSSDDSI DNTDSLILSP
KQHKGEDRKR NHEISSISPP RSRETIGHDD DDNNVDVIPR RQFNELEKEY KELKQMDETH
KQYIESLKLQ ITQLEEKVKK SSSHPRSLLP GIPSNINDSP KVVYTKSSIT NDNSSSHHQQ
QQQQHNISPS NSITSTTSPI NMMDSNIKSL SYKDFTNSQE IDAQQQLHQY HLNNGTNPAT
STTNGSGNPL SQSSPTGSDK HIQQSTISDL VSALNFNNCQ LESGKYLVDL IIKNHDSIVS
KYVPSEMGGI PEPAFILSRC FLKNIYDVDA TVIGTPNSTN SGGGSGTGVL DPIETNVNIL
IYFCDKVEEV IYRDPKSNCS ALCYWFSNFY TLFNIMETYN QDTKDQLSLN DQDKALIEKL
KITLQTMIVK AHKNVVKNIT DYIQPILHKS LNDTTSEIDF MDPITNYLNQ IQISLSLENC
YINNNLCKLL FEQLFSFINA MIFNEILLRK DLCCLRSSIP IKMNISELEH WVKLHHGKEW
SSSVCDKLRL LKEVVYILMI DKTQLQNDEL RDEICPTLSI AQLKQLLTMY SPDVDSFEDP
IPLEILTSLM DSPKYNPDEN ILLDLSKIFT LKFINSNQTL SSSTSSENDL MATINLNALE
SVQYACDDLV SNIVKKNIEI VSLNNQKSIK K
