Q6PDN3
uniprot
Q6PDN3
canonical
amino_acid_sequence
MGDVKLFASSHMSKTSHSVDPSKVSSMPLTEAPAFILPPRNLCVKEGATAKFEGRVRGYPEPQVTWHRKGQAITNGGRFLLDCGVRGTFSLVIHTVREEDKGKYTCEASNGSGARQVTVELTVEGNSMKKRDQPVLSKASGFPGETRPSIWGECPPKFATKLGRAVVKEGQMWRFSCKITGRPPPQVTWLKGNVPLQPSARVSMSEKNGMQILEIRGVTRDDLGVYTCMVVNGSGKASMSAELSIPGLDNASRLAVRGTKAPSPDIRKEVTNGVSKDPETVAESKNCPSPQRSGSSARATNSHLKSPQEPKPKLCEDAPRKVPQSSILQKSTSTITLQALKVQPEARVPAIGSFSPGEDRKSLAAPQQATLPTRQSSLGGSVGNKFVTGNIPRESQRESTFPRFESQPQSQEVTEGQTVKFICEVSGIPKPDVGWFLEGIPVRRREGITEVYEDGVSHHLCLLRARTRDSRKYSCTASNSLGQVSCSWSLLVDRPNLAQTAPSFSSVLKDSVVIEGQDFVLRCSVQGTPAPRVTWLLNGQPIQFAHSICEAGVAELHIQDALPEDRGTYTCLAENAMGQVSCSATVTVQEKKGEGEREHRLSPARSKPIAPIFLQGLSDLKVMDGSQVTMTVQVSGNPPPEVIWLHDGNEIQESEDFHFEQKGGWHSLCIQEVFPEDTGTYTCEAWNSAGEVRTRAVLTVQEPHDGTQPWFISKPRSVTATLGQSVLISCAIAGDPFPTVHWLRDGRALSKDSGHFELLQNEDVFTLVLKNVQPWHAGQYEILLKNRVGECSCQVSLMLHNSPSRAPPRGREPASCEGLCGGGGVGAHGDGDRHGTLRPCWPARGQGWPEEEDGEDVRGLLKRRVETRLHTEEAIRQQEVGQLDFRDLLGKKVSTKTVSEDDLKDIPAEQMDFRANLQRQVKPKTISEEERKVHSPQQVDFRSVLAKKGTPKTPVPEKAPPKAATPDFRSVLGGKKKSPSENGGNSAEVLNVKAGESPTPAGDAQAIGALKPVGNAKPAETPKPIGNAKPTETLKPVGNTKPAETLKPIANAQPSGSLKPVTNAQPAEPQKPVGNAKSAETSKPAGKEEVKEVKNDVNCKKGQVGATGNEKRPESQGSAPVFKEKLQDVHVAEGEKLLLQCQVISDPPATVTWSLNGKTLKTTKFIVLAQEGSRFSVSIEKALPEDRGLYKCVAKNSAGQAECSCQVTVDDAQTSENTKAPEMKSRRPKSSLPPVLGTESDATVKKKPAPKTPTKAAMPPQIIQFPEDQKVRAGEPVELFGKVAGTQPITCKWMKFRKQIQESEHIKVENGESGSKLTILAARQEHCGCYTLVVENKLGSRQAQVNLTVVDKPDPPAGTPCASDIRSSSLTLSWYGSSYDGGSAVQSYNVEIWDTEDKVWKELATCRSTSFNVQDLLPDREYKFRVRAVNVYGTSEPSQESELTAVGEKPEEPKDEVEVSDDDEKEPEVDYRTVTVNTEQKVSDVYDIEERLGSGKFGQVFRLVEKKTGKIWAGKFFKAYSAKEKDNIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWLMKDTKNMEAKKLSKDRMKKYMARRKWQKTGNAVRAIGRLSSMAMISGLSGRKSSTGSPTSPINAEKLESEDDVSQAFLEAVAEEKPHVKPYFSKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRHFQIDYDEDGNCSLIISDVCGDDDAKYTCKAVNSLGEATCTAELIVETMEEGEGEEGGEEEEEEEE
uniprot
proteins
ec_number
2.7.11.18
uniprot
proteins
function
FUNCTION: Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC) (PubMed:11832329, PubMed:16055522, PubMed:18586037, PubMed:41791372). Also regulates actin-myosin interaction through a non-kinase activity (PubMed:11832329). Phosphorylates PTK2B/PYK2 and myosin light-chains (PubMed:11832329, PubMed:18587400). Involved in the inflammatory response (e.g. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma (PubMed:20018858). Required for tonic airway smooth muscle contraction that is necessary for physiological and asthmatic airway resistance (PubMed:18586037). Necessary for gastrointestinal motility (PubMed:16184195). Implicated in the regulation of endothelial as well as vascular permeability, probably via the regulation of cytoskeletal rearrangements (PubMed:17577141). In the nervous system it has been shown to control the growth initiation of astrocytic processes in culture and to participate in transmitter release at synapses formed between cultured sympathetic ganglion cells (By similarity). Critical participant in signaling sequences that result in fibroblast apoptosis (By similarity). Plays a role in the regulation of epithelial cell survival (By similarity). Required for epithelial wound healing, especially during actomyosin ring contraction during purse-string wound closure (By similarity). Mediates RhoA-dependent membrane blebbing (By similarity). Triggers TRPC5 channel activity in a calcium-dependent signaling, by inducing its subcellular localization at the plasma membrane (By similarity). Promotes cell migration (including tumor cells) and tumor metastasis (By similarity). PTK2B/PYK2 activation by phosphorylation mediates ITGB2 activation and is thus essential to trigger neutrophil transmigration during acute lung injury (ALI) (PubMed:18587400). May regulate optic nerve head astrocyte migration (By similarity). Probably involved in mitotic cytoskeletal regulation (By similarity). Regulates tight junction probably by modulating ZO-1 exchange in the perijunctional actomyosin ring (PubMed:20404178). Mediates burn-induced microvascular barrier injury; triggers endothelial contraction in the development of microvascular hyperpermeability by phosphorylating MLC (PubMed:17577141). Essential for intestinal barrier dysfunction (PubMed:16184195). Mediates Giardia spp.-mediated reduced epithelial barrier function during giardiasis intestinal infection via reorganization of cytoskeletal F-actin and tight junctional ZO-1 (PubMed:12360480). Necessary for hypotonicity-induced Ca(2+) entry and subsequent activation of volume-sensitive organic osmolyte/anion channels (VSOAC) in cervical cancer cells (By similarity). {ECO:0000250|UniProtKB:Q15746, ECO:0000269|PubMed:11832329, ECO:0000269|PubMed:12360480, ECO:0000269|PubMed:16055522, ECO:0000269|PubMed:16184195, ECO:0000269|PubMed:17577141, ECO:0000269|PubMed:18586037, ECO:0000269|PubMed:18587400, ECO:0000269|PubMed:20018858, ECO:0000269|PubMed:20404178, ECO:0000269|PubMed:41791372}.
uniprot
proteins
mass_dalton
212925
uniprot
proteins
post_translational_modification
PTM: Can probably be down-regulated by phosphorylation. Tyrosine phosphorylation by ABL1 increases kinase activity, reverses MLCK-mediated inhibition of Arp2/3-mediated actin polymerization, and enhances CTTN-binding. Phosphorylation by SRC at Tyr-452 promotes CTTN binding (By similarity). {ECO:0000250|UniProtKB:Q15746}.; PTM: The C-terminus is deglutamylated by AGTPBP1/CCP1, AGBL1/CCP4 and AGBL4/CCP6, leading to the formation of Myosin light chain kinase, smooth muscle, deglutamylated form. The consequences of C-terminal deglutamylation are unknown (PubMed:21074048). {ECO:0000269|PubMed:21074048}.
uniprot
proteins
protein_family
CAMK Ser/Thr protein kinase family
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
11029314
uniprot
proteins
pubmed
11121372
uniprot
proteins
pubmed
11472067
uniprot
proteins
pubmed
11832329
uniprot
proteins
pubmed
12360480
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16055522
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16184195
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
17577141
uniprot
proteins
pubmed
17925381
uniprot
proteins
pubmed
18586037
uniprot
proteins
pubmed
18587400
uniprot
proteins
pubmed
20018858
uniprot
proteins
pubmed
20404178
uniprot
proteins
pubmed
21074048
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
41791372
uniprot
proteins
pubmed
8764148
uniprot
proteins
sequence_length
1941
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11832329}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q15746}. Cleavage furrow {ECO:0000250|UniProtKB:Q15746}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:11832329}. Note=Localized to stress fibers during interphase and to the cleavage furrow during mitosis. {ECO:0000250|UniProtKB:Q15746}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:11832329}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:11832329}. Note=Throughout the cytoplasm with higher levels near the plasma membrane. {ECO:0000269|PubMed:11832329}.
uniprot
proteins