MYO5_CANAL
ID MYO5_CANAL Reviewed; 1316 AA.
AC Q59MQ0; A0A1D8PM91; Q59MN7;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Myosin-5;
DE AltName: Full=Class I unconventional myosin MYO5;
DE AltName: Full=Type I myosin MYO5;
GN Name=MYO5; OrderedLocusNames=CAALFM_C405100CA;
GN ORFNames=CaO19.738, CaO19.8357;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-366, AND MUTAGENESIS
RP OF SER-366.
RX PubMed=12455956; DOI=10.1128/ec.1.2.213-228.2002;
RA Oberholzer U., Marcil A., Leberer E., Thomas D.Y., Whiteway M.;
RT "Myosin I is required for hypha formation in Candida albicans.";
RL Eukaryot. Cell 1:213-228(2002).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15470256; DOI=10.1128/ec.3.5.1272-1286.2004;
RA Oberholzer U., Iouk T.L., Thomas D.Y., Whiteway M.;
RT "Functional characterization of myosin I tail regions in Candida
RT albicans.";
RL Eukaryot. Cell 3:1272-1286(2004).
CC -!- FUNCTION: Type-I myosin implicated in the organization of the actin
CC cytoskeleton. Required for proper actin cytoskeleton polarization and
CC for the internalization step in endocytosis. At the cell cortex,
CC assembles in patch-like structures together with proteins from the
CC actin-polymerizing machinery and promotes actin assembly. Functions as
CC actin nucleation-promoting factor (NPF) for the Arp2/3 complex (By
CC similarity). Plays a role in chitin deposition in the cell wall, in
CC determination of the budding pattern, and is required for hyphae
CC formation. {ECO:0000250, ECO:0000269|PubMed:12455956,
CC ECO:0000269|PubMed:15470256}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000269|PubMed:12455956, ECO:0000269|PubMed:15470256}.
CC Note=Localizes to cortical patch-like structures. Enriched at sites of
CC polarized growth, like the growing bud tip, the mother-bud neck after
CC cytokinesis, and the hyphal tip.
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). The IQ domain and the TH1 region are essential for hyphal growth
CC and for endocytosis. The SH3 domain together with the TH3 region are
CC required for the organization of the cortical actin. {ECO:0000250}.
CC -!- PTM: Phosphorylation of the TEDS site (Ser-366) is required for the
CC polarization of the actin cytoskeleton. Phosphorylation probably
CC activates the myosin-I ATPase activity. {ECO:0000269|PubMed:12455956}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; CP017626; AOW29251.1; -; Genomic_DNA.
DR RefSeq; XP_710986.2; XM_705894.2.
DR AlphaFoldDB; Q59MQ0; -.
DR SMR; Q59MQ0; -.
DR BioGRID; 1230497; 1.
DR STRING; 237561.Q59MQ0; -.
DR iPTMnet; Q59MQ0; -.
DR PRIDE; Q59MQ0; -.
DR GeneID; 3647404; -.
DR KEGG; cal:CAALFM_C405100CA; -.
DR CGD; CAL0000199209; MYO5.
DR VEuPathDB; FungiDB:C4_05100C_A; -.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; Q59MQ0; -.
DR OrthoDB; 122881at2759; -.
DR PRO; PR:Q59MQ0; -.
DR Proteomes; UP000000559; Chromosome 4.
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 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 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Cytoplasm; Cytoskeleton; Hydrolase;
KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..1316
FT /note="Myosin-5"
FT /id="PRO_0000338543"
FT DOMAIN 43..731
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 735..755
FT /note="IQ 1"
FT DOMAIN 756..781
FT /note="IQ 2"
FT DOMAIN 789..981
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1156..1216
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..497
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 964..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1075
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1154
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1234
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1237..1271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 136..143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12455956"
FT MUTAGEN 366
FT /note="S->A: Exhibits a depolarized distribution of
FT cortical actin patches. Shows random budding pattern and is
FT unable to form hyphae."
FT /evidence="ECO:0000269|PubMed:12455956"
FT MUTAGEN 366
FT /note="S->D: Exhibits a depolarized distribution of
FT cortical actin patches, but allows hyphae formation."
FT /evidence="ECO:0000269|PubMed:12455956"
SQ SEQUENCE 1316 AA; 146955 MW; 15E99C710D91CDB7 CRC64;
MAIVKRGGRT KTKQQQVPAK SSGGGSSGGI KKAEFDITKK KEVGVSDLTL LSKITDEAIN
ENLHKRFMND TIYTYIGHVL ISVNPFRDLG IYTLENLNKY KGRNRLEVPP HVFAIAESMY
YNLKSYGENQ CVIISGESGA GKTEAAKQIM QYIANVSVNQ DNVEISKIKD MVLATNPLLE
SFGCAKTLRN NNSSRHGKYL EIKFSEGNYQ PIAAHITNYL LEKQRVVSQI TNERNFHIFY
QFTKHCPPQY QQMFGIQGPE TYVYTSAAKC INVDGVDDAK DFQDTLNAMK IIGLTQQEQD
NIFRMLASIL WIGNISFVED ENGNAAIRDD SVTNFAAYLL DVNPEILKKA IIERTIETSH
GMRRGSTYHS PLNIVQATAV RDALAKGIYN NLFEWIVERV NISLAGSQQQ SSKSIGILDI
YGFEIFERNS FEQICINYVN EKLQQIFIQL TLKAEQDEYV QEQIKWTPID YFNNKVVCDL
IEATRPQPGL FAALNDSIKT AHADSEAADQ VFAQRLSMVG ASNRHFEDRR GKFIIKHYAG
DVTYDVAGMT DKNKDAMLRD LLELVSTSQN SFINQVLFPP DLLAQLTDSR KRPETASDKI
KKSANILVDT LSQCTPSYIR TIKPNQTKKP RDYDNQQVLH QIKYLGLKEN VRIRRAGFAY
RSTFERFVQR FYLLSPATGY AGDYIWRGDD ISAVKEILKS CHIPPSEYQL GTTKVFIKTP
ETLFALEDMR DKYWHNMAAR IQRAWRRYVK RKEDAAKTIQ NAWRIKKHGN QFEQFRDYGN
GLLQGRKERR RMSMLGSRAF MGDYLGCNYK SGYGRFIINQ VGINESVIFS SKGEILLSKF
GRSSKRLPRI FIVTKTSIYI IAEVLVEKRL QLQKEFTIPI SGINYLGLST FQDNWVAISL
HSPTPTTPDV FINLDFKTEL VAQLKKLNPG ITIKIGPTIE YQKKPGKFHT VKFIIGAGPE
IPNNGDHYKS GTVSVKQGLP ASSKNPKRPR GVSSKVDYSK YYNRGAARKT AAAAQATPRY
NQPTPVANSG YSAQPAYPIP QQPQQYQPQQ SQQQTPYPTQ SSIPSVNQNQ SRQPQRKVPP
PAPSLQVSAA QAALGKSPTQ QRQTPAHNPV ASPNRPASTT IATTTSHTSR PVKKTAPAPP
VKKTAPPPPP PTLVKPKFPT YKAMFDYDGS VAGSIPLVKD TVYYVTQVNG KWGLVKTMDE
TKEGWSPIDY LKECSPNETQ KSAPPPPPPP PAATASAGAN GASNPISTTT STNTTTSSHT
TNATSNGSLG NGLADALKAK KQEETTLAGS LADALKKRQG ATRDSDDEEE EDDDDW
