MYO1_YARLI
ID MYO1_YARLI Reviewed; 1228 AA.
AC Q6C7C0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=MYO1; OrderedLocusNames=YALI0E02046g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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-358) 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; CR382131; CAG79021.1; -; Genomic_DNA.
DR RefSeq; XP_503442.1; XM_503442.1.
DR AlphaFoldDB; Q6C7C0; -.
DR SMR; Q6C7C0; -.
DR STRING; 4952.CAG79021; -.
DR EnsemblFungi; CAG79021; CAG79021; YALI0_E02046g.
DR GeneID; 2912078; -.
DR KEGG; yli:YALI0E02046g; -.
DR VEuPathDB; FungiDB:YALI0_E02046g; -.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; Q6C7C0; -.
DR OMA; NGWWLCK; -.
DR Proteomes; UP000001300; Chromosome E.
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..1228
FT /note="Myosin-1"
FT /id="PRO_0000338564"
FT DOMAIN 37..716
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 720..740
FT /note="IQ 1"
FT DOMAIN 741..768
FT /note="IQ 2"
FT DOMAIN 776..962
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1109..1170
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..487
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 953..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1169..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1109
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 130..137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1228 AA; 136132 MW; 8001A571BEF6DBCD CRC64;
MAVTKRAGRR AQGGTQPAKG AQGVKKATFE SGKKREVGVS DLTLLSKVSE EAINENLKKR
FENGTIYTYI GHVLISVNPF RDLGIYTDAV LESYKGKNRL EVPPHVFSIA ESMYYNMKSY
SENQCVIISG ESGAGKTEAS KRIMQYIASA SGGSSSNIQK IKDMVLATNP LLEAFGCAKT
LRNDNSSRHG KYLEIQFNNQ AEPVGANITN YLLEKGRVVG QIRNERNFHI FYQFAKAASE
NYRSTFGIQP PEAYTYTSAS GCTSVNGIND EAEFKETLAA MNLIGLTQAE QDNLFKLLAA
ILWIGNMSFV EDKDGNAAIA DVSVPNFVAY LLEVDAESVV KAVTQRIMET SRGGRRGSVY
EVALNIAQAT SVRDALAKGI YNNLFDWIVE RVNQSLRAPQ DAARTIGILD IYGFEIFESN
SFEQICINYV NEKLQQIFIQ LTLKTEQDEY VREQIAWTPI NYFNNKIVCD LIEEKRPPGI
FAALNDACAT AHADPNAADE NFIQRMSMVG QNPHFEQRQR KFVIKHYAGD VTYDVKGITD
KNKDQLLKDI LILLQKSGNP FLVSLFPDPV NTDNRRRPPT ASDKIKKSAN DLVTTLSAAQ
PSYIRTIKPN QNRSPTEYDE KAVLHQVKYL GLQENVRIRR AGFAYRQTFE KFVERFMLLS
GKTSYAGDYI WQGSAYDATL CILRDAGIPQ TEYQMGTTKV FIKTPETLFA LEHMRDMWWH
NMAARIQRAW RRYLAYKTEC AIKIQRFWRL KRGLDGLKEI QFRDSGHKLL GGRKERRTYS
LIGYRRFQGD YLGCNNGSGF GDFLMKQIGV TDKVFFSCRG QLQQSRLGRS SVRVPRTFIL
TKNNFYVVAQ QIHQKQLVVT NEYTIPVRNI THMSMSNLRD DWFCLNQASS PYGDQLMWCV
FKTELAVQLR VVKPGVDIRI GPQIDYFKKQ GKKASVKFQK TTTLQTKFDM YKSGSVQVPP
GAPPNSVSKE TPRGRAKGSR GGAPSRPAAR GNAAHTPTPG AAALGYQQHQ PGSAQPASPR
ARKAPPPAPN SRGNGHAESA QPQAYNNLQP HYQSLVNPRS GQGQQQQQHH QAYQQPTAAQ
PAATSYSPAP AKAAPPPPPP APPAAPAAPA EPTYKALYDY VANGLNQLSI SAGEQVLISV
KEDQGWWLAK RMDGSEEGWT PAAYLEEVQG GAAAPPPAAP TAGGASAGAS LAEALKQKQQ
SNQTLGAGIA DAIKARTGRP ADDDDDDW
