MYO1_KLULA
ID MYO1_KLULA Reviewed; 1260 AA.
AC Q6CVE9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=MYO1; OrderedLocusNames=KLLA0B12562g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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-355) 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; CR382122; CAH02483.1; -; Genomic_DNA.
DR RefSeq; XP_452090.1; XM_452090.1.
DR AlphaFoldDB; Q6CVE9; -.
DR SMR; Q6CVE9; -.
DR STRING; 28985.XP_452090.1; -.
DR EnsemblFungi; CAH02483; CAH02483; KLLA0_B12562g.
DR GeneID; 2897213; -.
DR KEGG; kla:KLLA0_B12562g; -.
DR eggNOG; KOG0162; Eukaryota.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; Q6CVE9; -.
DR OMA; MESKWGT; -.
DR Proteomes; UP000000598; Chromosome B.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR GO; GO:0051285; C:cell cortex of cell tip; IEA:EnsemblFungi.
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:0044853; C:plasma membrane raft; IEA:EnsemblFungi.
DR GO; GO:0005628; C:prospore membrane; IEA:EnsemblFungi.
DR GO; GO:0051015; F:actin filament binding; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
DR GO; GO:0000147; P:actin cortical patch assembly; IEA:EnsemblFungi.
DR GO; GO:0006897; P:endocytosis; IEA:EnsemblFungi.
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 CDD; cd01378; MYSc_Myo1; 1.
DR Gene3D; 3.40.850.10; -; 1.
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..1260
FT /note="Myosin-1"
FT /id="PRO_0000338552"
FT DOMAIN 34..713
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 717..737
FT /note="IQ 1"
FT DOMAIN 738..763
FT /note="IQ 2"
FT DOMAIN 769..959
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1103..1165
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 402..484
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 948..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..1088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1104
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 127..134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1260 AA; 140209 MW; A21DE370E65A59A3 CRC64;
MALIRRAKNK VAPQKRAETT IKKATFDATK KKEVGVSDLT LLSSISDDAI NQNLKKRFEN
GTIYTYIGHV LISVNPFRDL GIYTDAVLES YKGKNRLEVP PHVFAIAEAM YYNLKAYNEN
QCVIISGESG AGKTEAAKRI MQYIAAASST HEASIGKIKD MVLATNPLLE SFGCAKTLRN
NNSSRHGKYL EIRFNEQFEP CAGQITNYLL EKQRVVGQIR NERNFHIFYQ FTKGASDTYR
QNFGVLQPDQ YIYTSASGCT SVDTIDDLHD YQETIKAMQV IGLSQEEQDQ IFRMLSAILW
IGNVTFVENN EGNAEVRDTS VTDFVAYLMQ VDSGLLIKCL VERVMETGHG SRRGSVYHVP
LNVVQATAVR DALAKAIYNN LFDWIVDRVN VSLKAFPGAV KSIGILDIYG FEIFEHNSFE
QICINYVNEK LQQIFIQLTL KSEQEEYNKE QIQWTPIKYF DNKVVCDLIE SKRPPGIFAT
LDDSVATAHA DSNAADQAFA QRLNLFSTNA HFDLRSSKFV IKHYAGDVTY DISGMTDKNK
DQLVKDLAEL VQTTTNPFLS TIFPDTIDKS SKRRPPTAGN KIIKSANELV ETLSKAQPSY
IRTIKPNQTK SPRDYDDQQV LHQVKYLGLQ ENVRIRRAGF AYRQTFEKFV ERFYLLSPKC
SYAGDYTWQG DTLGAVKQIL QDASIPTTEY QLGVTKVFIK TPETLFALEH MRDRYWYNMA
ARIQRAWRRF IQRRIDSAIK IQRAIREKKG GNQYEQLRDY GHRLLGGRKE RRAMSLLGYR
AFMGDYLSCN EMKSKGAFIK RQAGISEIVV FSIKGEALHS KFGRSAVRLP ITIILTPTTL
YIVGQTVAQN QVSYTVDRKV NISHIKHVSL TNLADDWVGI YVQGENLPDP FINTIFKTEL
ITHLKQLNRA IEVKIGPTIE YQKKPGKLHT VKCQISESAP KYSDIYKSST ISVRQGRPAN
SRQAPKPEKK STLLSDGPSY NSNQSKGYGQ QQHAQPSYGQ QQQQQQRYAP QSHATPQTTQ
KKRAPPPPGQ QNFAASAAQT AYHPQQASHA RVPSTNNAHT QHNRQPAQQA AQPVQQAAQP
AATTSQPTRR VAPPPPPPPP TKQNIPKFQA AYDFTGTGSA SELPLSKGTV ITVSKQDPSG
WSLGKLLDGS KEGWVPTNYI VEYKESSGPP PPPAPPVASS TTGYANSNNN AFAANDNVAA
VAGAAAGATA GAAVAAASLA NPGQNAFSVG LADALAARAN TMRLESDDES TGNADEDDDW
