MYO1_NEUCR
ID MYO1_NEUCR Reviewed; 1235 AA.
AC Q7SDM3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=myo-1; ORFNames=NCU02111;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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 -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; CM002236; EAA34869.1; -; Genomic_DNA.
DR RefSeq; XP_964105.1; XM_959012.2.
DR AlphaFoldDB; Q7SDM3; -.
DR SMR; Q7SDM3; -.
DR STRING; 5141.EFNCRP00000001310; -.
DR PRIDE; Q7SDM3; -.
DR EnsemblFungi; EAA34869; EAA34869; NCU02111.
DR GeneID; 3880254; -.
DR KEGG; ncr:NCU02111; -.
DR VEuPathDB; FungiDB:NCU02111; -.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; Q7SDM3; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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 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; Reference proteome; Repeat;
KW SH3 domain.
FT CHAIN 1..1235
FT /note="Myosin-1"
FT /id="PRO_0000338558"
FT DOMAIN 41..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 773..962
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1075..1134
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..487
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 949..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1135..1235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..977
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1075
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1155
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1211
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"
SQ SEQUENCE 1235 AA; 136308 MW; 3683C01C2E26A03B CRC64;
MGITKRSKDK AARAERSAGG DKSSSAKPKK ATFDTTKKKE IGVSDLTLLS KVSNEAINEN
LKKRFEGREI YTYIGHVLVS VNPFRDLGIY TDQVLESYKG KNRLEMPPHV FAIAESAYYN
MKAYSENQCV IISGESGAGK TEAAKRIMQY IANVSGGGSG DIQQIKDMVL ATNPLLESFG
NAKTLRNNNS SRFGKYLQIH FNAQGEPIGA DITNYLLEKS RVVGQIANER NFHIFYQFTK
GASQQYREMY GIQKPETYLY TSKAKCFDVD GIDDLAEYQD TLNAMKIIGL SQQEQDNIFR
MLSAILWAGN LVFKEGDDGY AAVSDQSVVD FLAYLLEVDP AQLVHALTIR ILTPRPGEVI
ESPANVPQAT ATRDALAMAI YYNLFDWIVE RINLSLKARQ ATTNSIGILD IYGFEIFEKN
SFEQLCINYV NEKLQQIFIQ LTLKAEQDEY AREQIKWTPI KYFDNKIVCD LIESTRPPGI
FSAMKDATKT AHADPAASDR TFMQSINGMS NPHLTPRQGA FIVKHYAGDV TYSVDGITDK
NKDLLLKGVQ NLFQASQNQF VHTLFPQQVD LDNRRQPPSA GDRIRTSANA LVDTLMKCQP
SYIRTIKPNE NKSPTEYNEP NVLHQVKYLG LQENVRIRRA GFAYRQSFEK FVDRFFLLSP
ATSYAGEYTW TGSYEAATKQ ILKDTSIPQE EWQLGVTKAF IKSPETLFAL EHMRDRYWHN
MATRIQRMWR AYLAYRAEAA IRIQRIWRKK RVGAEYLQLR EEGHKVLGGR KERRRMSILG
SRRFLGDYLG INATTGPGAQ IRNAIGIGSN EKAVFSCRGE LLEHKFGRSS KPSPRILVVT
NSKFYIVAQV LNQGHVQIMA EKAFPLASIK FIGASTARDD WFSLGVGSQQ EPDPLLNCVL
KTEMFTQMKR VMPGSFNLKI GDAIEYAKKP GKMQLVKVLK DAPTSQDFYK SSTVHTQPGE
PPNSVSRPQP KAKPVPPRPI TKGKLIKPGG PGGRPARNAN PNRTAQPRPG GGPSIAASNP
LASSAAAASS RPVPAHPGAA ATPAAAKSLP SHTRQQSSTS TVRPPPPPPP APAAKPKIMA
KVLYDFAGTR ENELSIKAGD MIEIVQKENN GWWLAKTPEG QAWVPAAYVE EQAPAPPVVA
PRPPPPPPPA ANGGGRVAPQ PPAKRPVAGR KPAPAPAVAS LQNRDSGMSL NGANGSGSDA
SRSSTPTPSI AGSLADALKA RKQAMAKRDD DEDDW
