MYO1_ASHGO
ID MYO1_ASHGO Reviewed; 1292 AA.
AC Q758Q9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=MYO1; OrderedLocusNames=AEL306C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 575; 577; 640-641 AND
RP 645-648.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Type-I myosin implicated in the organization of the actin
CC cytoskeleton. Required for proper actin cytoskeleton polarization. At
CC the cell cortex, assembles in patch-like structures together with
CC proteins from the actin-polymerizing machinery and promotes actin
CC assembly. Functions as actin nucleation-promoting factor (NPF) for the
CC Arp2/3 complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000250}.
CC -!- DOMAIN: The myosin motor domain displays actin-stimulated ATPase
CC activity and generates a mechanochemical force. {ECO:0000250}.
CC -!- DOMAIN: The tail domain participates in molecular interactions that
CC specify the role of the motor domain (By similarity). It is composed of
CC several tail homology (TH) domains, namely a putative phospholipid-
CC binding myosin tail domain (also named TH1), an Ala- and Pro-rich
CC domain (TH2), followed by an SH3 domain and a C-terminal acidic domain
CC (TH3). {ECO:0000250}.
CC -!- PTM: Phosphorylation of the TEDS site (Ser-356) is required for the
CC polarization of the actin cytoskeleton. Phosphorylation probably
CC activates the myosin-I ATPase activity (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; AE016818; AAS52378.2; -; Genomic_DNA.
DR RefSeq; NP_984554.2; NM_209907.2.
DR AlphaFoldDB; Q758Q9; -.
DR SMR; Q758Q9; -.
DR STRING; 33169.AAS52378; -.
DR EnsemblFungi; AAS52378; AAS52378; AGOS_AEL306C.
DR GeneID; 4620729; -.
DR KEGG; ago:AGOS_AEL306C; -.
DR eggNOG; KOG0162; Eukaryota.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; Q758Q9; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0030479; C:actin cortical patch; IBA:GO_Central.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0051285; C:cell cortex of cell tip; IEA:EnsemblFungi.
DR GO; GO:0051286; C:cell tip; IBA:GO_Central.
DR GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
DR GO; GO:0031097; C:medial cortex; IEA:EnsemblFungi.
DR GO; GO:0045160; C:myosin I complex; IEA:EnsemblFungi.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0044853; C:plasma membrane raft; IEA:EnsemblFungi.
DR GO; GO:0005628; C:prospore membrane; IEA:EnsemblFungi.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0071933; F:Arp2/3 complex binding; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0000147; P:actin cortical patch assembly; IEA:EnsemblFungi.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IEA:EnsemblFungi.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:EnsemblFungi.
DR GO; GO:0044855; P:plasma membrane raft distribution; IEA:EnsemblFungi.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:EnsemblFungi.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IEA:EnsemblFungi.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01378; MYSc_Myo1; 1.
DR CDD; cd11858; SH3_Myosin-I_fungi; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR035535; Fungal_myosin-I_SH3.
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 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 3: Inferred from homology;
KW Actin-binding; ATP-binding; Cytoplasm; Cytoskeleton; Hydrolase;
KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..1292
FT /note="Myosin-1"
FT /id="PRO_0000338535"
FT DOMAIN 35..714
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 718..738
FT /note="IQ 1"
FT DOMAIN 739..764
FT /note="IQ 2"
FT DOMAIN 770..960
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1157..1219
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 403..485
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 956..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1227..1258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1047
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1082
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1121
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1158
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 128..135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1292 AA; 143575 MW; F26EEB3F0234904C CRC64;
MAIIKRGVRQ KTQPPAKRTT NIKKATFDSG KKKEVGVSDL TLLSKISDEH INENLKRRFE
NGSIYTYIGH VLISVNPFRD LGIYTDQVLE TYKGRNRLEV PPHVFAIAEA MYYNLKAYNE
NQCVIISGES GAGKTEAAKR IMQYIAAASS SHEASIGRIK DMVLATNPLL ESFGCAKTLR
NNNSSRHGKY LEIRFNAQFE PCAGQITNYL LEKQRVVGQI KNERNFHIFY QFSKGASDRY
RKTYGVQLPE QYVYTSASGC TSVDTIDDLN DYEATLEAMN VIGLSQAEQD EIFRLLSAIL
WIGNVTFMED DEGNAKIADT SITDFVAYLL QVDAGLLVKS LVERTIETTH GMRRGSIYNV
PLNIVQATAV RDALAKAIYN NLFEWIVDRV NVSLQALPGA EKSIGILDIY GFEIFEHNSF
EQICINYVNE KLQQIFIQLT LKSEQEEYAK EQIQWTPIKY FDNKVVCELI EAKRPPGIFA
ALNDSVATAH ADSNAADQAF AQRLNLFTSN PHFELRSSKF VIKHYAGDVT YDIGGMTDKN
KDQLQRDLVE LLNSTSNTFL ATIFPDTGDK DSKRRPPTAG DKIIRSANEL VDTLSKAQPS
YIRTIKPNQT KSPLDYDDRQ VLHQVKYLGL QENVRIRRAG FAYRQTFEKF VERFYLLSPQ
CSYAGDYTWQ GNTLDAVNLI LRDTSIPVTE YQLGVTKVFI KTPETLFALE NMRDKYWHNM
ASRIQRAWRR FLQRRIDSAI RIQRAIREMK HGNQFEQLRD YGNKLLGGRK ERRAMSLLGY
RAFLGDYLSC NELKSKGAFV KRKAGINDHV VFSINGQALH SKFGRSAQRL PKTFILTPSH
FYIIGKTLVN NQLTYAVDYK IDVRQIVYVS LTNLQDDWVG IFVSNSTQPD PLINTYFKTE
LITHLKKLNN RIEIKIGPTI EYQKKPGKIH AVKSQINENA PPLGDIYKSS TIMVRRGRPG
NCSQRKKPLS TRLPDTYTTR ETGYKNAGHP TNIRQVQEPT HISHSQQHTS SNLGFVYSLN
PSAVNHPRPV PSGSVGTTST PPKQAASAAQ AAYNPHKLGG NMDNSSAAYG NASALPNSAP
SQAPKPASRP VPKPAPRPGP KPGPKPGPKP GPKPAPKPMP RPAKSVENSV PRPNAIEQGK
TAPPPPPPPP PPPAAVPSEP VYEAAFDFPG SGSPNEFPLK KGDRIYVTRQ EPSGWSLAKA
LDGSKEGWVP TAYIVESKAA FSQLEQPVAS SAPLGNSGVA TREAGTTSAA TAAASAATPT
AFSAGLADAL AARANKMRHE DSGSDDNADD DW
