MYO1_CRYNB
ID MYO1_CRYNB Reviewed; 1274 AA.
AC P0CP01; Q55LY2; Q5K8T7;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=MYO1; OrderedLocusNames=CNBI2300;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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-363) 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; AAEY01000044; EAL18969.1; -; Genomic_DNA.
DR RefSeq; XP_773616.1; XM_768523.1.
DR AlphaFoldDB; P0CP01; -.
DR SMR; P0CP01; -.
DR EnsemblFungi; AAW46486; AAW46486; CNL04540.
DR EnsemblFungi; EAL18969; EAL18969; CNBI2300.
DR GeneID; 4938190; -.
DR KEGG; cnb:CNBI2300; -.
DR VEuPathDB; FungiDB:CNBI2300; -.
DR HOGENOM; CLU_000192_7_6_1; -.
DR Proteomes; UP000001435; Chromosome 9.
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: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; Repeat;
KW SH3 domain.
FT CHAIN 1..1274
FT /note="Myosin-1"
FT /id="PRO_0000410157"
FT DOMAIN 41..721
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 725..745
FT /note="IQ 1"
FT DOMAIN 746..771
FT /note="IQ 2"
FT DOMAIN 779..969
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1067..1125
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..492
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 951..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1042..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1069
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1142
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 134..141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1274 AA; 139552 MW; 271CBF77B8C51FDC CRC64;
MAPSKKAGKK GAVGGFLSGA SKPQKVQKAD WSEGFTKKKA AGVPDMTLLS TITNEAINDN
LKVRFQNQEI YTYIAHVLIS VNPFRDLGIY TNDVLNSYRG KNRLEMSPHV FAIAESAYYR
MTTEKENQCV IISGESGAGK TEAAKRIMQY IAAVSGGAEG GGIEGIKEMV LATNPLLESF
GCAKTLRNDN SSRHGKYLEI MFNGMGQPVG AQITNYLLEK NRVVGQIDDE RDFHIFYQFT
KGASAKMKEA FGLQGPEAYA YISRSGCLDV KSINDVSDFQ ETLRAMQVIG LTSDEQDSIF
RILATILWLG NIDFVEGDDG NAAISDSGVA DFAAYLLEVD SAQLQKVLLM RIMETQRGGR
RGSVYEVPQN VAQASSGRDA LAKALYNNLF EWIVSRVNIS MKPQTPSQYV IGVLDIYGFE
IFQDNSFEQL SINYVNEKLQ QIFIELTLKA EQEEYVREQI KWTPIKFFDN SVVCSLIEDR
RPAGIFATLN DATATAHADP SAADNSFIQR SSMLASNPNF EARGNKFLIK HYAGDVLYTV
AGMTDKNKDT LIKDILDLIE GSKDPFLHTL FPDKVDHTSK KRPPTAGDKI KLSANLLVEN
LMNCQPHYIR TIKPNQHRSP TEYDDKAILH QIKYLGLQEN IRVRRAGFAY RAEFSKMIQR
FYLLSPATSY AGDYIWTGDD RSGCERILTD AKIKKEEWQM GVTKAFIKNP ETLFYLEGER
DRYWHTMASR IQRAWRAYVR RKHEAATKIQ RFWRNQREAL VYERKRDYGH QVLAGKKERR
RFSLLGMRKF MGDYLDIAGG SAQGEMLRNA ATISPAEQVH FSSRAELLVS KLGRSSKLSP
RFLIITDKAV YFVVSQARDG RVSTSLERKI PLVTIKAISM TNLRDDFVAL NVNACEEGDP
IFTCVFKTEM ITVILTLTGG NMSVNIGPTI DYAKKKDKRA VIKTQKNEAV RGDATYKSHT
IQVGSGEPPN SLSNPMPPRK PKVKKAAKTA SSSRPVNSGR PAAVALPGAT KPAAPPALSS
MPSHTPVVTK PTAIPTAAIG AARAPPSIPG RAAAPPPPPP PPPPAGPPKE FYKALYNFTG
QEGEMNLVKG EEVEVKEKDD NGWWMVVKNG QEGWAPSNYL KKVEQAPPPP PPPPPPSRPV
AARPPAASSA PTAPAVTNGS AVPSWKAKNA ASATPSADST PPTSRPASSA SKVPPAIKAK
PSIPAKPAIP AKPQVGAKPA PAIGGKPPVP TAPKVQPKAA SKLGQVAQPA KAPGQLDLAA
AFAKRAARAQ QEED
