MYO5_YEAS7
ID MYO5_YEAS7 Reviewed; 1219 AA.
AC A6ZMG6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Myosin-5;
DE AltName: Full=Actin-dependent myosin-I MYO5;
DE AltName: Full=Class I unconventional myosin MYO5;
DE AltName: Full=Type I myosin MYO5;
GN Name=MYO5; ORFNames=SCY_4278;
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. Interacts with
CC BZZ1, PKH1, PKH2, YPK1 and YPK2 (By similarity). {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 activity. Ser-357 is phosphorylated by
CC YPK2 in vitro (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; AAFW02000020; EDN64496.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZMG6; -.
DR SMR; A6ZMG6; -.
DR PRIDE; A6ZMG6; -.
DR EnsemblFungi; EDN64496; EDN64496; SCY_4278.
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: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; Repeat;
KW SH3 domain.
FT CHAIN 1..1219
FT /note="Myosin-5"
FT /id="PRO_0000338566"
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 1085..1147
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..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1052
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1086
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1167
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:Q04439"
FT MOD_RES 359
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q04439"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04439"
FT MOD_RES 992
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04439"
FT MOD_RES 1205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04439"
SQ SEQUENCE 1219 AA; 136899 MW; DFFB9EC16B61CD29 CRC64;
MAILKRGARK KVHQEPAKRS ANIKKATFDS SKKKEVGVSD LTLLSKISDE AINENLKKRF
LNATIYTYIG HVLISVNPFR DLGIYTDAVM NEYKGKNRLE VPPHVFAIAE SMYYNMKSYN
ENQCVIISGE SGAGKTEAAK RIMQYIAAAS STHTESIGKI KDMVLATNPL LESFGCAKTL
RNNNSSRHGK YLEIKFNNQF EPCAGNITNY LLEKQRVVSQ IKNERNFHIF YQFTKGASDA
YRQTFGVQKP EQYVYTAAAG CISAETIDDL QDYQETLKAM RVIGLGQEEQ DQIFRMLAAI
LWIGNVSFIE NEEGNAQVRD TSVTDFVAYL LQIDSQLLIK SLVERIMETN HGMKRGSVYH
VPLNIVQADA VRDALAKAIY NNLFDWIVSR VNKSLQAFPG AEKSIGILDI YGFEIFEHNS
FEQICINYVN EKLQQIFIQL TLKSEQETYE REKIQWTPIK YFDNKVVCDL IEARRPPGIF
AAMNDSVATA HADSNAADQA FAQRLNLFTT NPHFDLRSNK FVIKHYAGDV TYDIDGITDK
NKDQLQKDLV ELIGTTTNTF LATIFPDTVD RESKRRPPTA GDKIIKSAND LVETLSKAQP
SYIRTIKPNE TKSPNDYDDR QVLHQIKYLG LQENVRIRRA GFAYRQVFEK FVERFYLLSP
HCSYAGDYTW QGDTLDAVKY ILQDSSIPQQ EYQLGVTSVF IKTPETLFAL EHMRDRYWHN
MAARIQRAWR RFLQRRIDAA TKIQRTIRER KEGNKYEKLR DYGTKVLGGR KERRSMSLLG
YRAFMGDYLS CNESKSKGAY IKRQVSIKEK VIFSIHGEAL HTKFGRSAQR LKKTFLLTPT
TLYIVGQTLV QNAMTYTQDY KIDVRNIQAV SLTNLQDDWV AIKLASSGQP DPLINTYFKT
ELITHLKRLN DKIQIKIGSA IEYQKKPGKL HSVKCQINES APKYGDIYKS STISVRRGNP
PNSQVHKKPR KKSSISSGYH ASSSQATRRP VSIAAAQHVP TAPASRHSKK PAPPPPGMQN
KAATRRSVPN PASTLTASQS NARPSPPTAA TRATPAATPA AAAMGSGRQA NIPPPPPPPP
PSSKPKEPMF EAAYDFPGSG SPSELPLKKG DVIYITREEP SGWSLGKLLD GSKEGWVPTA
YMKPHSGNNN IPTPPQNRDV PKPVLNSVQH DNTSANVIPA AAQASLGDGL ANALAARANK
MRLESDDEEA NEDEEEDDW
