MYSB_ACACA
ID MYSB_ACACA Reviewed; 1147 AA.
AC P19706;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Myosin heavy chain IB;
DE AltName: Full=Myosin heavy chain IL;
GN Name=MIB; Synonyms=MIL;
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=2511079; DOI=10.1016/0378-1119(89)90052-8;
RA Jung G., Schmidt C.J., Hammer J.A. III;
RT "Myosin I heavy-chain genes of Acanthamoeba castellanii: cloning of a
RT second gene and evidence for the existence of a third isoform.";
RL Gene 82:269-280(1989).
RN [2]
RP PROTEIN SEQUENCE OF 538-559, AND PHOSPHORYLATION AT SER-315.
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}.
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DR EMBL; M30780; AAA27708.1; -; Genomic_DNA.
DR PIR; JQ0095; MWAXIB.
DR PDB; 2DRK; X-ray; 1.42 A; A=1094-1147.
DR PDB; 2DRM; X-ray; 1.35 A; A/B/C/D=1094-1147.
DR PDBsum; 2DRK; -.
DR PDBsum; 2DRM; -.
DR AlphaFoldDB; P19706; -.
DR SMR; P19706; -.
DR iPTMnet; P19706; -.
DR VEuPathDB; AmoebaDB:ACA1_173680; -.
DR EvolutionaryTrace; P19706; -.
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; PF00018; SH3_1; 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 3D-structure; Actin-binding; ATP-binding; Direct protein sequencing;
KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein; SH3 domain.
FT CHAIN 1..1147
FT /note="Myosin heavy chain IB"
FT /id="PRO_0000123361"
FT DOMAIN 9..677
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 715..900
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1090..1147
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 551..573
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 901..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103..110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2530230"
FT STRAND 1094..1099
FT /evidence="ECO:0007829|PDB:2DRM"
FT STRAND 1116..1121
FT /evidence="ECO:0007829|PDB:2DRM"
FT STRAND 1126..1132
FT /evidence="ECO:0007829|PDB:2DRM"
FT STRAND 1135..1140
FT /evidence="ECO:0007829|PDB:2DRM"
FT HELIX 1141..1143
FT /evidence="ECO:0007829|PDB:2DRM"
FT STRAND 1144..1146
FT /evidence="ECO:0007829|PDB:2DRM"
SQ SEQUENCE 1147 AA; 124959 MW; B76DE9C076381054 CRC64;
MGKAAVEQRG VDDLVLMPKI TEQDICANLE KRYFNDLIYT NIGPVLISVN PFRRIDALLT
DECLHCYRGR YQHEQPPHVY ALAEAAYRGV KSENINQCVI ISGESGAGKT EASKLVMQYV
AAVSGNSGGV DFVKHSNPLL EAFGNAKTLR NNNSSRFGKY FEIHFNRLGE PCGGRITNYL
LEKSRVTFQT RGERSFHIFY QLLAGASDAE AQEMQLYAPE NFNYLNQSAC YTVDGIDDIK
EFADTRNAIN VMGMTAEEQR QVFHLVAGIL HLGNVAFHDG GKGTAAVHDR TPFALKNALL
FRVLNTGGAG AKKMSTYNVP QNVEQAASAR DALAKTIYSR MFDWIVSKVN EALQKQGGSG
DHNNNMIGVL DIFGFEIFEQ NGFEQFCINY VNEKLQQYFI ELTLKAEQEE YVNEGIQWTP
IKYFNNKVVC ELIEGKRPPG IFSLLDDICF TMHAQSDGMD GKFLQKCQGG FPSHLHFRGM
NNAFSIKHYA GEVTYEAEGF CEKNKDTLFD DLIAVIQESE NRLLVSWFPE DTKQLQKKRP
TTAGFKLKTS CDALMEALSR CSPHYIRCIK PNDNKAYHDW DATRTKHQVQ YLGLLENVRV
RRAGFAYRAE FDRFLRRYKK LSPKTWGIWG EWSGAPKDGC QTLLNDLGLD TSQWQLGKSK
VFIRYPETLF HLEECLDRKD YDCTLRIQKA WRHWKSRKHQ LEQRKMAADL LKGKKERQRH
SVNRKYEFDY INYDANYPLQ DCVRSSGRDK EATAFTDQVL VLNRRGKPER RDLIVTNEAV
YFAMRKKKSG QVVYNLKRRI PLGEIASLSL STLQDNYVVI HHNQYDMVFE NDKKTEIVTI
LMENYKMSGG RDLPVNFNDN ITYKASNGAQ RRLTFSKNES ASAQPSIKKS RANIQIGIAT
GLPKETDSSP PNWTPSGGGG GYGGGRGGGG GGRGAAGGGR GGFGGGGGGG YSQPVAQAQP
VAQVPQPVAA VPSAGRGGPG MGGPGAGRGG PGMGRGGPGM GGPGAGRGGP GMGGPGGPGR
GGPGGPGAGR GGPGGPGAGR GGPGMGGPGG AGRGGPGAGR GGPGMGGPGA GRGGPGAGRG
AAPAPAPAAP AKPQVKALYD YDAQTGDELT FKEGDTIIVH QKDPAGWWEG ELNGKRGWVP
ANYVQDI
