MYSC_ACACA
ID MYSC_ACACA Reviewed; 1168 AA.
AC P10569;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Myosin IC heavy chain;
GN Name=MIC;
OS Acanthamoeba castellanii (Amoeba).
OC Eukaryota; Amoebozoa; Discosea; Longamoebia; Centramoebida;
OC Acanthamoebidae; Acanthamoeba.
OX NCBI_TaxID=5755;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3477803; DOI=10.1073/pnas.84.19.6720;
RA Jung G., Korn E.D., Hammer J.A. III;
RT "The heavy chain of Acanthamoeba myosin IB is a fusion of myosin-like and
RT non-myosin-like sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6720-6724(1987).
RN [2]
RP PARTIAL NUCLEOTIDE SEQUENCE.
RX PubMed=3014500; DOI=10.1073/pnas.83.13.4655;
RA Hammer J.A. III, Jung G., Korn E.D.;
RT "Genetic evidence that Acanthamoeba myosin I is a true myosin.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:4655-4659(1986).
RN [3]
RP PHOSPHORYLATION AT SER-311.
RX PubMed=2530230; DOI=10.1016/s0021-9258(19)47307-9;
RA Brzeska H., Lynch T.J., Martin B., Korn E.D.;
RT "The localization and sequence of the phosphorylation sites of Acanthamoeba
RT myosins I. An improved method for locating the phosphorylated amino acid.";
RL J. Biol. Chem. 264:19340-19348(1989).
CC -!- FUNCTION: Myosin is a protein that binds to F-actin and has ATPase
CC activity that is activated by F-actin.
CC -!- SUBUNIT: Myosin I heavy chain is single-headed. Dimer of a heavy and a
CC light chain. Inability to self-assemble into filaments.
CC -!- DOMAIN: Myosin tail domain binds directly to anionic phospholipid
CC membranes; myosins I could therefore move actin relative to membranes
CC and vice versa. TH.2 and SH3 bind tightly to F-actin; this together
CC with the nucleotide-sensitive site in the head, allows single molecules
CC of myosin I to cross-link actin filaments.
CC -!- MISCELLANEOUS: This organism expresses at least three isoforms of
CC myosin I heavy-chain, encoded by genes MIA, MIB, and MIC.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be myosin IB. {ECO:0000305}.
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DR EMBL; J02974; AAA27707.1; -; Genomic_DNA.
DR PIR; A33891; MWAXIC.
DR AlphaFoldDB; P10569; -.
DR SMR; P10569; -.
DR IntAct; P10569; 1.
DR MINT; P10569; -.
DR BindingDB; P10569; -.
DR ChEMBL; CHEMBL4295712; -.
DR iPTMnet; P10569; -.
DR PRIDE; P10569; -.
DR VEuPathDB; AmoebaDB:ACA1_173680; -.
DR GO; GO:0031252; C:cell leading edge; IEA:UniProt.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0120025; C:plasma membrane bounded cell projection; IEA:UniProt.
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:0030036; P:actin cytoskeleton organization; IEA:UniProt.
DR GO; GO:0022607; P:cellular component assembly; IEA:UniProt.
DR GO; GO:0006897; P:endocytosis; IEA:UniProt.
DR GO; GO:0040011; P:locomotion; IEA:UniProt.
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; PF14604; SH3_9; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR PRINTS; PR00452; SH3DOMAIN.
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; Motor protein; Myosin; Nucleotide-binding;
KW Phosphoprotein; SH3 domain.
FT CHAIN 1..1168
FT /note="Myosin IC heavy chain"
FT /id="PRO_0000123362"
FT DOMAIN 7..666
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 704..892
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 976..1035
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 542..564
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 876..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1128
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 101..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2530230"
SQ SEQUENCE 1168 AA; 127310 MW; D07084B373A37A32 CRC64;
MAYTSKHGVD DMVMLTSISN DAINDNLKKR FAADLIYTYI GHVLISVNPY KQINNLYTER
TLKDYRGKYR YELPPHVYAL ADDMYRTMLS ESEDQCVIIS GESGAGKTEA SKKIMQYIAA
VSGATGDVMR VKDVILEAFG NAKTIRNNNS SRFGKYMEIQ FDLKGDPVGG RISNYLLEKS
RVVYQTNGER NFHIFYQLLA ARARRPEAKF GLQTPDYYFY LNQGKTYTVD GMDDNQEFQD
TWNAMKVIGF TAEEQHEIFR LVTAILYLGN VQFVDDGKGG STIADSRPVA VETALLYRTI
TTGEQGRGRS SVYSCPQDPL GAIYSRDALS KALYSRMFDY IIQRVNDAMY IDDPEALTTG
ILDIYGFEIF GKNGFEQLCI NFVNEKLQQI FIQLTLKAEQ EEYGAEGIQW ENIDYFNNKI
CCDLIEEKRP PGLMTILDDV CNFPKGTDDK FREKLLGAFP THAHLAATSQ PDEFVIKHYA
GDVVYNVDGF CDKNKDLLFK DLIGLAECTS STFFAGLFPE AKEVATSKKK PTTAGFKIKE
SINILVATLS KCTPHYIRCI KPNEKKAANA FNNSLVLHQV KYLGLLENVR IRRAGYAYRQ
SYDKFFYRYR VVCPKTWSGW NGDMVSGAEA ILNHVGMSLG KEYQKGKTKI FIRQPESVFS
LEELRDRTVF SYANKIQRFL RKTAMRKYYY EVKKGGNDAL VNKKERRRLS LERPFKTDYI
NYRQNFKLKD CIGDKGTEKV LFADLCNNLD KSFWGSKVER RIMVLTSNAM FLVAIDPNKD
KIEKKVKPFL YVLKRRIDFN KIGSITLSPL QDNFMLISVN GEHSNLLECR RKTELIGVLL
KHNPSVRIQF ADTFNVTLKG GKTCVVKFIR DPQGGDGKVK GTKVSVAPGL PPSSAPNIQA
PQETSGGASF TVAEQSYKDQ ILGAKGGGGG GGRGRGGPSP SGAVSPRPSP GGGGGGPSPF
GGRPSPSGPP AAASAPGPEQ ARALYDFAAE NPDELTFNEG AVVTVINKSN PDWWEGELNG
QRGVFPASYV ELIPRAAAPA PGPSGGPRPA PPGGKSGRAA PMGGPGPMRG RGGPAPGGPG
RGGAPPPGAG RAGPPGGRGM PAPGGAAPRG RGAPPPGAGG PPGGGRGGAP PPGGMRGRGG
PGPAPPGGMA RGGMMPPRGR AGPPPPGM
