MYO3_CANGA
ID MYO3_CANGA Reviewed; 1252 AA.
AC Q6FMJ3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Myosin-3;
DE AltName: Full=Class I unconventional myosin MYO3;
DE AltName: Full=Type I myosin MYO3;
GN Name=MYO3; OrderedLocusNames=CAGL0K07590g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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-357) 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; CR380957; CAG61514.1; -; Genomic_DNA.
DR RefSeq; XP_448551.1; XM_448551.1.
DR AlphaFoldDB; Q6FMJ3; -.
DR SMR; Q6FMJ3; -.
DR STRING; 5478.XP_448551.1; -.
DR EnsemblFungi; CAG61514; CAG61514; CAGL0K07590g.
DR GeneID; 2890383; -.
DR KEGG; cgr:CAGL0K07590g; -.
DR CGD; CAL0134555; MYO3.
DR VEuPathDB; FungiDB:CAGL0K07590g; -.
DR eggNOG; KOG0162; Eukaryota.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; Q6FMJ3; -.
DR Proteomes; UP000002428; Chromosome K.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0051641; P:cellular localization; IEA:UniProt.
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..1252
FT /note="Myosin-3"
FT /id="PRO_0000338544"
FT DOMAIN 36..715
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 719..739
FT /note="IQ 1"
FT DOMAIN 740..767
FT /note="IQ 2"
FT DOMAIN 773..963
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1116..1178
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 404..486
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 988..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1203..1252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1086
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 129..136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1252 AA; 141600 MW; EBEB17C7DDBFEBBA CRC64;
MAIIKRVVRS KAGQAPVKKG AKIKKASYDS SRKKEVGVSD LTLLSKISDE SINDNLKKRF
EHGIIYTYIG YVLISVNPFR DLGIYTDDTM KSYQGKNRLE APPHVFAIAE NMYYNLKSYN
ENQCVIISGE SGAGKTEAAK RIMQYIAATS STHSESISKI KDMVLATNPL LESFGCAKTL
RNNNSSRHGK YLEIKFDAHF QPCAGHITNY LLEKQRVVGQ IKNERNFHIF YQFTKGAPEE
YRQLFGVQQP EQYIYTSASQ CTAVENMDDV EEFNETLNAM RTIGLTKSEQ DQIFRALAAI
LWIGNISFVE NEAGNAEIRD KSVTTFVAYL LEVQEELLIK ALIERIIETT HGAKRGSTYH
SPLNIIQATA VRDALAKAIY NNLFEWIVER VNNSLQAFPG ADKSIGILDI YGFEIFEHNS
FEQICINYVN EKLQQIFIQL TLKSEQDTYK KEQIHWTPIE YFDNKIVCDL IEAKRPPGIF
AAMNDAIATA HADSDAADQA FAQRLNLFTT NPHFELRQNK FVVKHYAGDV TYDIFGITDK
NKDQLQKDLV ELLSTTSNSF VREIFPDQPQ TDSRRRPPTS GDKIIKSANE LVETLSKAQP
SYIRTIKPND TKSSTIYDDQ RVLHQIKYLG LKENVRIRRA GFAHRQVFEK FVERFYLLSP
QCSYAGDYVW DGETLDAVKL ILQDASIPTT EYEIGVTQIF IKHPETLFAL ENMRDKYWYN
MAARIQRAWR RYLQKRIDAA IRIQNAIRGK SGVSTFRNDE LRNAGDKVYG GKKERRNMSL
LGLRGFYGDY LSCNESKTRG SYIKRQANIT ERVLFSSHGN SLHAMYGGAS QRLRKTFILT
PTSLWIVGHT KARNAMKYIT DYRIDLGKIR SISVTNLQDD WMAVNLMDSP KPDPLINLPF
KTELITRLTQ LNPRIHVKVS STIEYLRGPK KLFVVKSQYS DSAPKYHDLY RNGTILVRHG
NPPDSTAENR PAFNNEDMYG NLMEAKHKTM KKKVGTKRTP QALPTSSLAA SAAQAAYHPK
GIRSPTSTEQ KSPSKSKPIT KTRKPPVSSP VRNTSKTISN SKVYSAPKAS VTKRTQDTVS
VSKTSVKDDV TQEKNAIIQT EEKQNYSLPE NIPQSSQTDS YQAAYDFPGS GNPSELPLQK
GDIIYVSKSD PSGWSLASTL DNSKEGWVPT SYIVKYNGNV TDPSAQHQDM NTMKIQEDNT
TSINEPETHT NQGPSNTDLG ANLASVLAAR ANKLRSESEE DISREEDDDD DW
