20210801201808032018022820210801IID50181Smoothelin-like protein 1Calponin homology-associated smooth muscle proteinMus musculus459Q99LM3Plays a role in the regulation of contractile properties of both striated and smooth muscles. When unphosphorylated, may inhibit myosin dephosphorylation. Phosphorylation at Ser-301 reduces this inhibitory activity.Nucleus.SL-0191unkown00Phosphoserine; by PKA and PKG301301MEQTEGNSSEDGTTVSPTAGNLETPGSQGIAEEVAEGTVGTSDKEGPSDWAEHLCKAASKSGESGGSPGEASILDELKTDLQGEARGKDEAQGDLAEEKVGKEDTTAASQEDTGKKEETKPEPNEVREKEEAMLASEKQKVDEKETNLESKEKSDVNDKAKPEPKEDAGAEVTVNEAETESQEEADVKDQAKPELPEVDGKETGSDTKELVEPESPTEEQEQGKENESEERAAVIPSSPEEWPESPTDEGPSLSPDGLAPESTGETSPSASESSPSEVPGSPTEPQPSEKKKDRAPERRVSAPSRPRGPRAQNRKAIMDKFGGAASGPTALFRNTKAAGAAIGGVKNMLLEWCRAMTRNYEHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAELDPAKRRHNFTLAFSTAEKLADCAQLLEVDDMVRLAVPDSKCVYTYIQELYRSLVQKGLVKTKKK12jv9A346459order222k3sA346459order132jv9A459459high_rmsd242k3sA458459high_rmsd112k3sNMR18477568H.ISHIDA,M.A.BORMAN,J.OSTRANDER,H.J.VOGEL,J.A.MACDONALDSOLUTION STRUCTURE OF THE CALPONIN HOMOLOGY (CH) DOMAIN FROM THE SMOOTHELIN-LIKE 1 PROTEIN: A UNIQUE APOCALMODULIN-BINDING MODE AND THE POSSIBLE ROLE OF THE C-TERMINAL TYPE-2 CH-DOMAIN IN SMOOTH MUSCLE RELAXATION.2008J.BIOL.CHEM.28320569nmr2k3sA346459100012k3s3712Hetero dimer2k3sAQ99LM3IID501812k3sBP0DP33IID503092k3sA-2k3sB22jv9NMR18477568H.ISHIDA,M.A.BORMAN,J.OSTRANDER,H.J.VOGEL,J.A.MACDONALDSOLUTION STRUCTURE OF THE CALPONIN HOMOLOGY (CH) DOMAIN FROM THE SMOOTHELIN-LIKE 1 PROTEIN: A UNIQUE APOCALMODULIN-BINDING MODE AND THE POSSIBLE ROLE OF THE C-TERMINAL TYPE-2 CH-DOMAIN IN SMOOTH MUSCLE RELAXATION.2008J.BIOL.CHEM.28320569nmr2jv9A346459100012jv93705Monomer monomer2jv9AQ99LM3IID50181344-4591-3432552PF00307346->4464.2e-26Calponin homology (CH) domainhmmpfm49261pxyA_343->4465e-32hmmscp7526PF00307346->4467e-08Calponin homology (CH) domainrpspfm97702jv9A1346->4597e-53rpsscp