Q6PDN3

EV
Gene name
Mylk
Protein name
Myosin light chain kinase, smooth muscle
Names
MLCK, smMLCK, Kinase-related protein, KRP, Telokin
Species
Mus musculus (Mouse)
KEGG Pathway
EC number
2.7.11.18: Protein-serine/threonine kinases
Protein Class
IMMUNOGLOBULIN (PTHR47633)

Descriptions

Myosin light chain kinases (MLCK) are members of the family of Ca2+-calmodulin-dependent protein kinases. The autoinhibitory pseudosubstrate sequence was identified by sequence similarity with the chicken smooth muscle MLCK (P11799-2). The mutational changes of acidic residues in the catalytic core of the kinase domain, which may interact with the basic residues in the pseudosubstrate sequence, increased the catalytic activity of the kinase domain.

Autoinhibitory domains (AIDs)

787-806 (Autoinhibitory pseudosubstrate) EV

Target domain

1486-1741 (Protein kinase domain)

Relief mechanism

Partner binding

Assay

Peptide inhibitor test, Deletion assay, Mutagenesis experiment, Structural analysis

Accessory elements

1626-1648 (Activation loop from InterPro)

Target domain

1486-1741 (Protein kinase domain)

Relief mechanism

Assay

References

Autoinhibited structure

Activated structure

1 structures for Q6PDN3

Entry ID Method Resolution Chain Position Source
AF-Q6PDN3-F1 Predicted AlphaFoldDB

No variants for Q6PDN3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6PDN3

No associated diseases with Q6PDN3

14 regional properties for Q6PDN3

Type Name Position InterPro Accession
domain Protein kinase domain 621 - 882 IPR000719
domain Ephrin receptor ligand binding domain 29 - 206 IPR001090
domain Serine-threonine/tyrosine-protein kinase, catalytic domain 622 - 878 IPR001245
conserved_site Tyrosine-protein kinase, receptor class V, conserved site 182 - 202 IPR001426-1
conserved_site Tyrosine-protein kinase, receptor class V, conserved site 243 - 263 IPR001426-2
domain Sterile alpha motif domain 908 - 975 IPR001660
domain Fibronectin type III 324 - 434 IPR003961-1
domain Fibronectin type III 435 - 530 IPR003961-2
active_site Tyrosine-protein kinase, active site 742 - 754 IPR008266
domain Tyrosine-protein kinase ephrin type A/B receptor-like 269 - 302 IPR011641
binding_site Protein kinase, ATP binding site 627 - 653 IPR017441
domain Tyrosine-protein kinase, catalytic domain 621 - 878 IPR020635
domain Ephrin receptor, transmembrane domain 543 - 618 IPR027936
domain Ephrin type-A receptor 3, ligand binding domain 29 - 200 IPR034266

Functions

Description
EC Number 2.7.11.18 Protein-serine/threonine kinases
Subcellular Localization
  • Cytoplasm
  • Cell projection, lamellipodium
  • Cleavage furrow
  • Cytoplasm, cytoskeleton, stress fiber
  • Localized to stress fibers during interphase and to the cleavage furrow during mitosis
PANTHER Family PTHR47633 IMMUNOGLOBULIN
PANTHER Subfamily PTHR47633:SF3 STRIATED MUSCLE PREFERENTIALLY EXPRESSED PROTEIN KINASE
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 GO annotations of cellular component

Name Definition
actin cytoskeleton The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes.
cell-cell junction A cell junction that forms a connection between two or more cells of an organism; excludes direct cytoplasmic intercellular bridges, such as ring canals in insects.
cleavage furrow The cleavage furrow is a plasma membrane invagination at the cell division site. The cleavage furrow begins as a shallow groove and eventually deepens to divide the cytoplasm.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
lamellipodium A thin sheetlike process extended by the leading edge of a migrating cell or extending cell process; contains a dense meshwork of actin filaments.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
stress fiber A contractile actin filament bundle that consists of short actin filaments with alternating polarity, cross-linked by alpha-actinin and possibly other actin bundling proteins, and with myosin present in a periodic distribution along the fiber.

7 GO annotations of molecular function

Name Definition
actin binding Binding to monomeric or multimeric forms of actin, including actin filaments.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
calmodulin binding Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.
enzyme binding Binding to an enzyme, a protein with catalytic activity.
metal ion binding Binding to a metal ion.
myosin light chain kinase activity Catalysis of the reaction: ATP + myosin-light-chain = ADP + myosin-light-chain phosphate.
protein kinase activity Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP.

11 GO annotations of biological process

Name Definition
aorta smooth muscle tissue morphogenesis The process in which the structure of the smooth muscle tissue surrounding the aorta is generated and organized. An aorta is an artery that carries blood from the heart to other parts of the body.
bleb assembly The assembly of a bleb, a cell extension caused by localized decoupling of the cytoskeleton from the plasma membrane and characterized by rapid formation, rounded shape, and scarcity of organelles within the protrusion. Plasma membrane blebbing occurs during apoptosis and other cellular processes, including cell locomotion, cell division, and as a result of physical or chemical stresses. [GOC:mah, GOC:mtg_apoptosis, PMID:12083798, PMID:16624291, Wikipedia:Bleb_(cell_biology)]
cellular hypotonic response Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a hypotonic environment, i.e. an environment with a lower concentration of solutes than the organism or cell.
cellular response to calcium ion Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a calcium ion stimulus.
cellular response to potassium ion Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a potassium ion stimulus.
cellular response to xenobiotic stimulus Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a xenobiotic, a compound foreign to the organism exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical.
positive regulation of calcium ion transport Any process that activates or increases the frequency, rate or extent of the directed movement of calcium ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
positive regulation of cell migration Any process that activates or increases the frequency, rate or extent of cell migration.
positive regulation of wound healing Any process that increases the rate, frequency, or extent of the series of events that restore integrity to a damaged tissue, following an injury.
smooth muscle contraction A process in which force is generated within smooth muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. Smooth muscle differs from striated muscle in the much higher actin/myosin ratio, the absence of conspicuous sarcomeres and the ability to contract to a much smaller fraction of its resting length.
tonic smooth muscle contraction A process in which force is generated within tonic smooth muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. In the tonic smooth muscle, the muscle contraction occurs without an ordered sarcomeric structure. Tonic smooth muscle contraction occurs as a sustained continuous contraction.

9 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P11799 Mylk Myosin light chain kinase, smooth muscle Gallus gallus (Chicken) SS
Q8WZ42 TTN Titin Homo sapiens (Human) EV
Q15746 MYLK Myosin light chain kinase, smooth muscle Homo sapiens (Human) SS
A2ASS6 Ttn Titin Mus musculus (Mouse) SS
Q62407 Speg Striated muscle-specific serine/threonine-protein kinase Mus musculus (Mouse) SS
Q63638 Speg Striated muscle-specific serine/threonine-protein kinase Rattus norvegicus (Rat) SS
P97924 Kalrn Kalirin Rattus norvegicus (Rat) SS
G4SLH0 ttn-1 Titin homolog Caenorhabditis elegans EV
Q23551 unc-22 Twitchin Caenorhabditis elegans EV
10 20 30 40 50 60
MGDVKLFASS HMSKTSHSVD PSKVSSMPLT EAPAFILPPR NLCVKEGATA KFEGRVRGYP
70 80 90 100 110 120
EPQVTWHRKG QAITNGGRFL LDCGVRGTFS LVIHTVREED KGKYTCEASN GSGARQVTVE
130 140 150 160 170 180
LTVEGNSMKK RDQPVLSKAS GFPGETRPSI WGECPPKFAT KLGRAVVKEG QMWRFSCKIT
190 200 210 220 230 240
GRPPPQVTWL KGNVPLQPSA RVSMSEKNGM QILEIRGVTR DDLGVYTCMV VNGSGKASMS
250 260 270 280 290 300
AELSIPGLDN ASRLAVRGTK APSPDIRKEV TNGVSKDPET VAESKNCPSP QRSGSSARAT
310 320 330 340 350 360
NSHLKSPQEP KPKLCEDAPR KVPQSSILQK STSTITLQAL KVQPEARVPA IGSFSPGEDR
370 380 390 400 410 420
KSLAAPQQAT LPTRQSSLGG SVGNKFVTGN IPRESQREST FPRFESQPQS QEVTEGQTVK
430 440 450 460 470 480
FICEVSGIPK PDVGWFLEGI PVRRREGITE VYEDGVSHHL CLLRARTRDS RKYSCTASNS
490 500 510 520 530 540
LGQVSCSWSL LVDRPNLAQT APSFSSVLKD SVVIEGQDFV LRCSVQGTPA PRVTWLLNGQ
550 560 570 580 590 600
PIQFAHSICE AGVAELHIQD ALPEDRGTYT CLAENAMGQV SCSATVTVQE KKGEGEREHR
610 620 630 640 650 660
LSPARSKPIA PIFLQGLSDL KVMDGSQVTM TVQVSGNPPP EVIWLHDGNE IQESEDFHFE
670 680 690 700 710 720
QKGGWHSLCI QEVFPEDTGT YTCEAWNSAG EVRTRAVLTV QEPHDGTQPW FISKPRSVTA
730 740 750 760 770 780
TLGQSVLISC AIAGDPFPTV HWLRDGRALS KDSGHFELLQ NEDVFTLVLK NVQPWHAGQY
790 800 810 820 830 840
EILLKNRVGE CSCQVSLMLH NSPSRAPPRG REPASCEGLC GGGGVGAHGD GDRHGTLRPC
850 860 870 880 890 900
WPARGQGWPE EEDGEDVRGL LKRRVETRLH TEEAIRQQEV GQLDFRDLLG KKVSTKTVSE
910 920 930 940 950 960
DDLKDIPAEQ MDFRANLQRQ VKPKTISEEE RKVHSPQQVD FRSVLAKKGT PKTPVPEKAP
970 980 990 1000 1010 1020
PKAATPDFRS VLGGKKKSPS ENGGNSAEVL NVKAGESPTP AGDAQAIGAL KPVGNAKPAE
1030 1040 1050 1060 1070 1080
TPKPIGNAKP TETLKPVGNT KPAETLKPIA NAQPSGSLKP VTNAQPAEPQ KPVGNAKSAE
1090 1100 1110 1120 1130 1140
TSKPAGKEEV KEVKNDVNCK KGQVGATGNE KRPESQGSAP VFKEKLQDVH VAEGEKLLLQ
1150 1160 1170 1180 1190 1200
CQVISDPPAT VTWSLNGKTL KTTKFIVLAQ EGSRFSVSIE KALPEDRGLY KCVAKNSAGQ
1210 1220 1230 1240 1250 1260
AECSCQVTVD DAQTSENTKA PEMKSRRPKS SLPPVLGTES DATVKKKPAP KTPTKAAMPP
1270 1280 1290 1300 1310 1320
QIIQFPEDQK VRAGEPVELF GKVAGTQPIT CKWMKFRKQI QESEHIKVEN GESGSKLTIL
1330 1340 1350 1360 1370 1380
AARQEHCGCY TLVVENKLGS RQAQVNLTVV DKPDPPAGTP CASDIRSSSL TLSWYGSSYD
1390 1400 1410 1420 1430 1440
GGSAVQSYNV EIWDTEDKVW KELATCRSTS FNVQDLLPDR EYKFRVRAVN VYGTSEPSQE
1450 1460 1470 1480 1490 1500
SELTAVGEKP EEPKDEVEVS DDDEKEPEVD YRTVTVNTEQ KVSDVYDIEE RLGSGKFGQV
1510 1520 1530 1540 1550 1560
FRLVEKKTGK IWAGKFFKAY SAKEKDNIRQ EISIMNCLHH PKLVQCVDAF EEKANIVMVL
1570 1580 1590 1600 1610 1620
EIVSGGELFE RIIDEDFELT ERECIKYMRQ ISEGVEYIHK QGIVHLDLKP ENIMCVNKTG
1630 1640 1650 1660 1670 1680
TRIKLIDFGL ARRLENAGSL KVLFGTPEFV APEVINYEPI GYATDMWSIG VICYILVSGL
1690 1700 1710 1720 1730 1740
SPFMGDNDNE TLANVTSATW DFDDEAFDEI SDDAKDFISN LLKKDMKNRL DCTQCLQHPW
1750 1760 1770 1780 1790 1800
LMKDTKNMEA KKLSKDRMKK YMARRKWQKT GNAVRAIGRL SSMAMISGLS GRKSSTGSPT
1810 1820 1830 1840 1850 1860
SPINAEKLES EDDVSQAFLE AVAEEKPHVK PYFSKTIRDL EVVEGSAARF DCKIEGYPDP
1870 1880 1890 1900 1910 1920
EVVWFKDDQS IRESRHFQID YDEDGNCSLI ISDVCGDDDA KYTCKAVNSL GEATCTAELI
1930 1940
VETMEEGEGE EGGEEEEEEE E