MYSN_ACACA
ID MYSN_ACACA Reviewed; 1509 AA.
AC P05659;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Myosin-2 heavy chain, non muscle;
DE AltName: Full=Myosin II heavy chain, non muscle;
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=3040773; DOI=10.1083/jcb.105.2.913;
RA Hammer J.A. III, Bowers B., Paterson B.M., Korn E.D.;
RT "Complete nucleotide sequence and deduced polypeptide sequence of a
RT nonmuscle myosin heavy chain gene from Acanthamoeba: evidence of a hinge in
RT the rodlike tail.";
RL J. Cell Biol. 105:913-925(1987).
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 II heavy chain is two-headed. It self-assembles into
CC filaments. Hexamer of 2 heavy chain subunits (MHC), 2 alkali light
CC chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2).
CC -!- DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles
CC of a 28-residue repeat pattern composed of 4 heptapeptides,
CC characteristic of alpha-helical structures. This region is interrupted
CC by a hinge and joined by a nonhelical tailpiece where the regulatory
CC phosphorylation sites reside.
CC -!- MISCELLANEOUS: The hinge region may play a key role in mediating the
CC effect of heavy chain phosphorylation on enzymatic activity.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; Y00624; CAA68663.1; -; Genomic_DNA.
DR PIR; A27224; A27224.
DR AlphaFoldDB; P05659; -.
DR SMR; P05659; -.
DR BindingDB; P05659; -.
DR ChEMBL; CHEMBL4295699; -.
DR PRIDE; P05659; -.
DR VEuPathDB; AmoebaDB:ACA1_326740; -.
DR BRENDA; 5.6.1.8; 15.
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:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 2.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 3: Inferred from homology;
KW Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil; Methylation;
KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein.
FT CHAIN 1..1509
FT /note="Myosin-2 heavy chain, non muscle"
FT /id="PRO_0000123364"
FT DOMAIN 32..85
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 89..787
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 790..819
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 623..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..682
FT /note="Actin-binding"
FT REGION 766..780
FT /note="Actin-binding"
FT REGION 848..1226
FT /note="Alpha-helical tailpiece (S2)"
FT REGION 958..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1227..1252
FT /note="Hinge"
FT REGION 1253..1509
FT /note="Light meromyosin (LMM)"
FT REGION 1253..1482
FT /note="Alpha-helical tailpiece (LMM)"
FT REGION 1352..1425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1474..1509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1483..1509
FT /note="Nonhelical tailpiece"
FT COILED 848..1509
FT /evidence="ECO:0000255"
FT COMPBIAS 1068..1085
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1478..1492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 182..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 133
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000255"
FT MOD_RES 1489
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 1494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 1499
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1509 AA; 171202 MW; 2CE49BE51173D17E CRC64;
MAAQRRRKGG EVESDYIKYL KYKNTGFQVS ASDKTLAWWP TKDADRAFCH VEVTKDDGKN
FTVRLENGEE KSQPKNEKNF LGVNPPKFDG VEDMGELGYL NEPAVLHNLK KRYDADLFHT
YSGLFLVVVN PYKRLPVYTP EIIDIYRGRQ RDKVAPHIFA ISDAAYRAML NTRQNQSMLI
TGESGAGKTE NTKKVIQYLT AIAGRAEGGL LEQQLLEFNP ILEAFGNAKT TKNNNSSRFG
KFIELQFNAG GQITGANTFI YLLEKSRVTA QGAGERNFHI FYQILSKAMP EELKQKLKLT
KPEDYFFLNQ NACYTVDDMD DAKEFDHMLK AFDILNINEE ERLAIFQTIS AILHLGNLPF
IDVNSETAGL KDEVELNIAA ELLGVSAAGL KAGLLSPRIK AGNEWVTRAL NKPKAMASRD
ALCKALFGRL FLWIVQKINR ILSHKDKTAL WIGVLDISGF EIFQHNSFEQ LCINYTNEKL
QQFFNHHMFT LEQQEYEREK IDWTFVDYGM DSQDCIDLIE KKPMGILPLL DEQTVFPDAD
DTSFTKKLFQ THENHRNFRR PRFDANNFKI VHYAGEVEYQ TSAWLEKNRD PLEDDLSNLC
KKSSVRFVTG LFDEDLMPSF KAAPAEEEKA AAGGSRNRST GRGKGGAQFI TVAFQYKEQL
AHLMSMLSST APHFIRCIIP NLGKKPGVVS DQLVLDQLKC NGVLEGIRIA RKGWPNRLKY
DEFLKRYFLL KPGATPTSPS TKDAVKDLIE HLIAKEPTKV NKDEVRFGVT KIFFRSGQLA
AIEELREQAI SKMVVSIQAG ARAFLARRMY DKMREQTVSA KILQRNIRAW LELKNWAWYQ
LYVKARPLIS QRNFQKEIDD LKKQVKDLEK ELAALKDANA KLDKEKQLAE EDADKLEKDL
AALKLKILDL EGEKADLEED NALLQKKVAG LEEELQEETS ASNDILEQKR KLEAEKGELK
ASLEEEERNR KALQEAKTKV ESERNELQDK YEDEAAAHDS LKKKEEDLSR ELRETKDALA
DAENISETLR SKLKNTERGA DDVRNELDDV TATKLQLEKT KKSLEEELAQ TRAQLEEEKS
GKEAASSKAK QLGQQLEDAR SEVDSLKSKL SAAEKSLKTA KDQNRDLDEQ LEDERTVRAN
VDKQKKALEA KLTELEDQVT ALDGQKNAAA AQAKTLKTQV DETKRRLEEA EASAARLEKE
RKNALDEVAQ LTADLDAERD SGAQQRRKLN TRISELQSEL ENAPKTGGAS SEEVKRLEGE
LERLEEELLT AQEARAAAEK NLDKANLELE ELRQEADDAA RDNDKLVKDN RKLKADLDEA
RIQLEEEQDA KSHADSSSRR LLAEIEELKK RVAKETSDKQ KAQDQKANYQ RENESLKADR
DSIERRNRDA ERQVRDLRAQ LDDALSRLDS EKRAKEKSVE ANRELKKVVL DRERQSLESL
SKFNSALESD KQILEDEIGD LHEKNKQLQA KIAQLQDEID GTPSSRGGST RGASARGASV
RAGSARAEE
