ID MYO3_YEAS7 Reviewed; 1270 AA.
AC A6ZZJ1;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 13-SEP-2023, entry version 69.
DE RecName: Full=Myosin-3;
DE AltName: Full=Actin-dependent myosin-I MYO3;
DE AltName: Full=Class I unconventional myosin MYO3;
DE AltName: Full=Type I myosin MYO3;
GN Name=MYO3; ORFNames=SCY_3251;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC -!- FUNCTION: One of two redundant type-I myosins implicated in the
CC organization of the actin cytoskeleton. Required for proper actin
CC cytoskeleton polarization and for the internalization step in
CC endocytosis. At the cell cortex, assembles in patch-like structures
CC together with proteins from the actin-polymerizing machinery and
CC promotes actin assembly. Functions redundantly with LAS17 as actin
CC nucleation-promoting factor (NPF) for the Arp2/3 complex. Motor domain
CC phosphorylation by PAK kinases CLA4 and STE20 promotes CDC42-regulated
CC actin assembly. Functions together with the NPF PAN1 in late stages of
CC endocytosis. Motor domain phosphorylation by PDK1 kinases PKH1 and
CC PKH2, and by SGK kinases YPK1 and YPK2, promotes ligand-induced, but
CC not constitutive endocytosis of the G protein-coupled receptor STE2 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via myosin motor domain) with SHE4; this
CC interaction is important for proper localization and may regulate the
CC interaction of the motor domain with actin. Interacts (via SH3 domain)
CC with VRP1; this interaction is required for localization to sites of
CC polarized growth and may regulate the interaction of the tail domain
CC with actin. Interacts (via SH3 domain) with PAN1; this interaction is
CC important for late stages of endocytopsis. Interacts (via SH3 domain)
CC with BBC1 and LAS17. Interacts (via C-terminal acidic tail) with ARC19
CC and ARC40; ARC19 and ARC40 are Arp2/3 complex subunits (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000250}. Note=Localizes to cortical patch-like protein structures
CC that assemble actin patches. Enriched at sites of polarized growth (By
CC similarity). {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 and for ligand-induced, but not
CC for constitutive internalization of STE2. Phosphorylation probably
CC activates the myosin-I ATPase (By similarity). Ser-357 is
CC phosphorylated by CLA4 and STE20 in vitro (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; AAFW02000151; EDN60039.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZZJ1; -.
DR BMRB; A6ZZJ1; -.
DR SMR; A6ZZJ1; -.
DR HOGENOM; CLU_000192_7_6_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
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:0016043; P:cellular component organization; IEA:UniProt.
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; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 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 PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF837; MYOSIN-3-RELATED; 1.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50044; SH3-domain; 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; Repeat;
KW SH3 domain.
FT CHAIN 1..1270
FT /note="Myosin-3"
FT /id="PRO_0000338565"
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..765
FT /note="IQ 2"
FT DOMAIN 771..961
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1118..1180
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..486
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 951..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1215..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1002
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1068
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1087
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1119
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1237
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|UniProtKB:P36006"
SQ SEQUENCE 1270 AA; 142333 MW; 2D269250CE7A13E9 CRC64;
MAVIKKGARR KDVKEPKKRS AKIKKATFDA NKKKEVGVSD LTLLSKISDE SINENLKKRF
KNGIIYTYIG HVLISVNPFR DLGIYTNAVL ESYKGKNRLE VPPHVFAIAE SMYYNLKSYN
ENQCVIISGE SGAGKTEAAK RIMQYIAAAS NSHSESIGKI KDMVLATNPL LESFGCAKTL
RNNNSSRHGK YLEIKFNSQF EPCAGNITNY LLEKQRVVSQ IKNERNFHIF YQFTKGASDT
YRQMFGVQMP EQYIYTAAAG CTTADTIDDV KDYEGTLEAM RTIGLVQEEQ DQIFRMLAAI
LWIGNISFIE NEEGNAQVGD TSVTDFVAYL LQVDASLLVK CLVERIMQTS HGMKRGSVYH
VPLNPVQATA VRDALAKAIY NNLFDWIVDR VNVSLQAFPG ADKSIGILDI YGFEIFEHNS
FEQICINYVN EKLQQIFIQL TLKAEQETYE REKIKWTPIK YFDNKVVCDL IEAKNPPGIL
AAMNDSIATA HADSNAADQA FAQRLNLFNS NPYFELRANK FVIKHYAGDV TYDINGITDK
NKDQLQKDLI ELIGTTTNTF LSTIFPDDVD KDSKRRPPTA GDKIIKSANE LVETLSKAEP
SYIRTIKPNQ TKSPNDYDDH QVLHQVKYLG LQENVRIRRA GFAYRQTFEK FVERFYLLSP
DCSYAGDYTW DGDTLEAVKL ILRDAMIPEK EFQLGVTSVF IKTPESLFAL EDMRDKYWYN
MAARIQRAWR RFLQRRIDAA IKIQRTIREK KGGNKYVKLR DYGTKLLAGK KERRSMSLLG
YRAFMGDYLS CNESKTKGSY IRRQVGIKDK VVFSIKGECL HSKFGRSAQR LKKVFILTKK
TFYIIGQTRE QNAMKYTQDY KIDVGKIKQV SLTNLQDDWM GVILVNSTQP DPLINTPFKT
ELMTRLKKLN EKIMIKVGPT IEYHKQPNKL HTVRSKISDS APKYGDIYKS STIYVRRGHP
ANSKSNKKPK NPGGLSGKPI KSKKSKHKST HKHTHSHRSH RDAAKKQPLP SQKPVNPLSL
AATAAQAAYN PKPDKTVPIK SSAIPAAKVS SKHSSKPSSK EKVAVKKASS SHKSSSAKQN
QVSMPPSKGV EKNKEPLKET TATANIPIPP PPPPMGQPKD PKFEAAYDFP GSGSSSELPL
KKGDIVFISR DEPSGWSLAK LLDGSKEGWV PTAYMTPYKD TRNTVPVAAT GAVNDVTNQK
SSQIDNTISS AQEGVQFGSA TVGPTSDNQS NPVGTFSDGL ASALAARANK MRAESADDDD
NDDGDDDDDW
//
