MYO1_COPC7
ID MYO1_COPC7 Reviewed; 1277 AA.
AC A8N2Y6; D6RK57;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=MYO1; ORFNames=CC1G_13719;
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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-360) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EFI28693.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACS02000001; EFI28693.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002912187.1; XM_002912141.1.
DR AlphaFoldDB; A8N2Y6; -.
DR SMR; A8N2Y6; -.
DR STRING; 5346.XP_002912187.1; -.
DR PRIDE; A8N2Y6; -.
DR EnsemblFungi; EFI28693; EFI28693; CC1G_13719.
DR GeneID; 6017031; -.
DR KEGG; cci:CC1G_13719; -.
DR eggNOG; KOG0162; Eukaryota.
DR eggNOG; KOG4151; Eukaryota.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; A8N2Y6; -.
DR OrthoDB; 311886at2759; -.
DR Proteomes; UP000001861; 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 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;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..1277
FT /note="Myosin-1"
FT /id="PRO_0000338548"
FT DOMAIN 39..718
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 722..742
FT /note="IQ 1"
FT DOMAIN 743..768
FT /note="IQ 2"
FT DOMAIN 776..965
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1071..1129
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..489
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 567..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1020
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1069
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1149
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1233
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1277 AA; 140501 MW; 02491586775B757E CRC64;
MAPSKKAGKK VTPKKAAGNN AKSKVAKADW KEGFKKKQVG VTDMTLLTTI SNESINENLQ
KRWTNGEIYT YIGAVLISVN PFRDLGIYTD EVLQRYRGKN RLEVPPHVFS IAESAYYNMN
AYHENQCVII SGESGAGKTE AAKQIMQYIA AVSGGQDSGI QEIKDMVLAT NPLLESFGCA
KTLRNNNSSR HGKYLEIMFN DRGEPVGAQI TNYLLEKGRV VGQIENERNF HIFYQFTKAA
SDEQREAFGL QGPDAYAYTS MSNCLDVQDI DDTRDFEGTI NAMQIIGLSP EEQNEIFKML
ATILWLGNVQ FDENEEGNSV ISDTGVTDFV AYLMEVDAAT VQKALTTRVM ETTRGGRRGS
VYDVPLNPSQ ATSGRDALSK AIYNNLFEWI VAKINVSLKT RSAYSHIIGI LDIFGFEIFE
DNSFEQLCIN YVNEKLQQIF IELTLKTEQE EYVREQIKWT PIKFFNNKVV CDLIEERRPP
GIFAALNDAC ATAHADPTAA DNSFIQRSAG LSSNGHFESR GAQFLVRHYA GDVMYNVAGM
TDKNKDSLIK DLLDLIGTSG NAFLQNLFPD RPDPNSKKRP PTASDRIKQS AGALVDKLMK
SQPSYIRTIK PNGNRSPSEY DTKAILHQIK YLGLQENIRV RRAGFAYRNT FEKMVERFYL
LSPKTSYAGE YIWTGDAKSG CEQILKDTGI AKDEWQMGVT KAFIKNPETL FALETMRDRY
WHNMAARIQR AFRNYMRYKH ECARRIQRFW KNNKEALVYA QVRDYGHQLL AGRKERRRFS
LLSYRRFMGD YLDISGKSSL GEEIGEACSL GREPVKFSAS ARLLVSKLGR SSKPSPRYIV
LTPKAVYIVI VTAKDGQAMF SLERKIALVT IKSIQMSTLR DDWFTLNLGP TEEGDPVLSC
YFKTEFVTHL MQLTQAGINF NIAPTIEYTK KKEKKAQIKF VKDETIPKDD VYKSHTVHVP
SGEPADSVSR PPAKRKAGVV RPITQGKLLR AGGPSKPNNS RPRPTAQPLP GQSKPAVATP
SVVSTPAAAA VVSKPKPAAS TPAAVRAPAV TPAARSVPPP PPPPPPARAE PEKEMYRAKF
DFQGQEGEMS LTKDDEVELI EKDENGWWLV KKDGVEAWAP YNYLERIAPK AAPAPPPPPA
RPRPTSTVPK PPLSSTTADA SAKPVAVFPG MGASNGGPTP WKKSAATTDS TPNSSRPGSA
AAKVPPPVAA KPKPPVVAPK PGVPKPGGKP ALPTTARPAP SGGGAAAGRL GGGGGGPGQL
DLAAALAKRA QRIADED
