{PDOC51757}
{PS51757; TH1}
{BEGIN}
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* Class I myosin tail homology (TH1) domain profile *
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Class I  myosins (Myo1s) are widely expressed in eukaryotic cells. Myo1s exist
as monomers  and can sense cellular mechanical forces and function as tension-
sensitive anchors  or  transporters.  Each  Myo1 contains from N terminus to C
terminus, a  motor  domain  (see  <PDOC51456>),  a  neck  region consisting of
several calmodulin  (CaM)-binding  IQ  motifs  (see  <PDOC50096>)  and  a tail
region. All  Myo1s  contain a tail homology (TH1) domain featuring an embedded
pleckstrin-homology (PH)  domain (see <PDOC50003>) capable of binding to lipid
membranes. In  addition,  Myo1s  with  long  tails also contain a TH2 (or GPA)
domain and  a  C-terminal TH3 (or SH3) domain (see <PDOC50002>), the latter of
which may  be  responsible  for  binding  to  cargos. All Myo1s are capable of
bridging actin  cytoskeletons  with lipid membranes by using their motor heads
and tail  TH1  domains.  The  TH1  domain  is an extended PH domain capable of
binding to lipids [1,2].

The TH1 domain forms an extended PH domain, with its N and C termini capped by
two alpha-helices  and  five  beta-strands, respectively (see <PDB:4R8G>). The
center of  TH1  contains a canonical PH domain fold formed by a seven-stranded
beta-barrel and an alpha-helix.

The profile we developed covers the entire TH1 domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: May 2015 / First entry.

[ 1] Lu Q., Li J., Ye F., Zhang M.
     "Structure of myosin-1c tail bound to calmodulin provides insights
     into calcium-mediated conformational coupling."
     Nat. Struct. Mol. Biol. 22:81-88(2015).
     PubMed=25437912; DOI=10.1038/nsmb.2923
[ 2] Patino-Lopez G., Aravind L., Dong X., Kruhlak M.J., Ostap E.M.,
     Shaw S.
     "Myosin 1G is an abundant class I myosin in lymphocytes whose
     localization at the  plasma membrane depends on its ancient divergent
     pleckstrin homology (PH) domain  (Myo1PH)."
     J. Biol. Chem. 285:8675-8686(2010).
     PubMed=20071333; DOI=10.1074/jbc.M109.086959

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