P11799

SS
Gene name
Mylk
Protein name
Myosin light chain kinase, smooth muscle
Names
MLCK , EC 2.7.11.18 , Telokin [Cleaved into: Myosin light chain kinase, smooth muscle, deglutamylated form]
Species
Gallus gallus (Chicken)
KEGG Pathway
EC number
2.7.11.18: Protein-serine/threonine kinases
Protein Class

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)

812-834 (Autoinhibitory pseudosubstrate) SS

Target domain

1453-1708 (Protein kinase domain)

Relief mechanism

Partner binding

Assay

Accessory elements

1593-1615 (Activation loop from InterPro)

Target domain

1453-1708 (Protein kinase domain)

Relief mechanism

Assay

1593-1615 (Activation loop from InterPro)

Target domain

1450-1708 (Protein kinase domain)

Relief mechanism

Assay

References

Autoinhibited structure

Activated structure

16 structures for P11799

Entry ID Method Resolution Chain Position Source
1CDL X-ray 200 A E/F/G/H 1730-1749 PDB
1QS7 X-ray 180 A B/D 1731-1749 PDB
1QTX X-ray 165 A B 1731-1749 PDB
1VRK X-ray 190 A B 1731-1749 PDB
2O5G X-ray 108 A B 1730-1748 PDB
3EK7 X-ray 185 A A 1730-1763 PDB
3EK8 X-ray 280 A A 1730-1763 PDB
3EKH X-ray 200 A A 1730-1763 PDB
3EKJ X-ray 280 A A 1730-1763 PDB
3EVR X-ray 200 A A 1730-1763 PDB
3EVU X-ray 175 A A 1731-1749 PDB
3EVV X-ray 260 A A 1731-1749 PDB
3O77 X-ray 235 A A 1730-1749 PDB
3O78 X-ray 260 A A/B 1731-1749 PDB
4OY4 X-ray 203 A PDB
AF-P11799-F1 Predicted AlphaFoldDB

No variants for P11799

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P11799

No associated diseases with P11799

41 regional properties for P11799

Type Name Position InterPro Accession
domain Protein kinase domain 1453 - 1708 IPR000719
domain Immunoglobulin subtype 2 40 - 108 IPR003598-1
domain Immunoglobulin subtype 2 168 - 235 IPR003598-2
domain Immunoglobulin subtype 2 441 - 508 IPR003598-3
domain Immunoglobulin subtype 2 540 - 604 IPR003598-4
domain Immunoglobulin subtype 2 649 - 716 IPR003598-5
domain Immunoglobulin subtype 2 747 - 814 IPR003598-6
domain Immunoglobulin subtype 2 1096 - 1163 IPR003598-7
domain Immunoglobulin subtype 2 1237 - 1304 IPR003598-8
domain Immunoglobulin subtype 2 1806 - 1874 IPR003598-9
domain Immunoglobulin subtype 34 - 119 IPR003599-1
domain Immunoglobulin subtype 162 - 246 IPR003599-2
domain Immunoglobulin subtype 435 - 519 IPR003599-3
domain Immunoglobulin subtype 534 - 615 IPR003599-4
domain Immunoglobulin subtype 643 - 727 IPR003599-5
domain Immunoglobulin subtype 741 - 825 IPR003599-6
domain Immunoglobulin subtype 1090 - 1174 IPR003599-7
domain Immunoglobulin subtype 1231 - 1315 IPR003599-8
domain Immunoglobulin subtype 1800 - 1885 IPR003599-9
domain Fibronectin type III 1318 - 1414 IPR003961
domain Immunoglobulin-like domain 28 - 117 IPR007110-1
domain Immunoglobulin-like domain 156 - 244 IPR007110-2
domain Immunoglobulin-like domain 429 - 517 IPR007110-3
domain Immunoglobulin-like domain 521 - 613 IPR007110-4
domain Immunoglobulin-like domain 637 - 725 IPR007110-5
domain Immunoglobulin-like domain 735 - 830 IPR007110-6
domain Immunoglobulin-like domain 1084 - 1160 IPR007110-7
domain Immunoglobulin-like domain 1225 - 1313 IPR007110-8
domain Immunoglobulin-like domain 1794 - 1885 IPR007110-9
active_site Serine/threonine-protein kinase, active site 1570 - 1582 IPR008271
domain Immunoglobulin I-set 28 - 118 IPR013098-1
domain Immunoglobulin I-set 156 - 245 IPR013098-2
domain Immunoglobulin I-set 429 - 518 IPR013098-3
domain Immunoglobulin I-set 529 - 614 IPR013098-4
domain Immunoglobulin I-set 639 - 726 IPR013098-5
domain Immunoglobulin I-set 736 - 822 IPR013098-6
domain Immunoglobulin I-set 1084 - 1173 IPR013098-7
domain Immunoglobulin I-set 1225 - 1314 IPR013098-8
domain Immunoglobulin I-set 1794 - 1884 IPR013098-9
domain Myosin Light Chain Kinase 1, Kinase domain 1450 - 1708 IPR015725
binding_site Protein kinase, ATP binding site 1459 - 1482 IPR017441

Functions

Description
EC Number 2.7.11.18 Protein-serine/threonine kinases
Subcellular Localization
  • Cytoplasm, cytosol
  • Membrane
  • Telokin is cytosolic and can translocate to the membrane upon stimulation
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
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.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
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.
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.

4 GO annotations of molecular function

Name Definition
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.
metal ion binding Binding to a metal ion.
myosin light chain kinase activity Catalysis of the reaction

3 GO annotations of biological process

Name Definition
muscle structure development The progression of a muscle structure over time, from its formation to its mature state. Muscle structures are contractile cells, tissues or organs that are found in multicellular organisms.
phosphorylation The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.
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
Q8WZ42 TTN Titin Homo sapiens (Human) EV
Q15746 MYLK Myosin light chain kinase, smooth muscle Homo sapiens (Human) SS
Q62407 Speg Striated muscle-specific serine/threonine-protein kinase Mus musculus (Mouse) SS
A2ASS6 Ttn Titin Mus musculus (Mouse) SS
Q6PDN3 Mylk Myosin light chain kinase, smooth muscle Mus musculus (Mouse) EV
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
MGDVKLVTST RVSKTSLTLS PSVPAEAPAF TLPPRNIRVQ LGATARFEGK VRGYPEPQIT
70 80 90 100 110 120
WYRNGHPLPE GDHYVVDHSI RGIFSLVIKG VQEGDSGKYT CEAANDGGVR QVTVELTVEG
130 140 150 160 170 180
NSLKKYSLPS SAKTPGGRLS VPPVEHRPSI WGESPPKFAT KPNRVVVREG QTGRFSCKIT
190 200 210 220 230 240
GRPQPQVTWT KGDIHLQQNE RFNMFEKTGI QYLEIQNVQL ADAGIYTCTV VNSAGKASVS
250 260 270 280 290 300
AELTVQGPDK TDTHAQPLCM PPKPTTLATK AIENSDFKQA TSNGIAKELK STSTELMVET
310 320 330 340 350 360
KDRLSAKKET FYTSREAKDG KQGQNQEANA VPLQESRGTK GPQVLQKTSS TITLQAVKAQ
370 380 390 400 410 420
PEPKAEPQTT FIRQAEDRKR TVQPLMTTTT QENPSLTGQV SPRSRETENR AGVRKSVKEE
430 440 450 460 470 480
KREPLGIPPQ FESRPQSLEA SEGQEIKFKS KVSGKPKPDV EWFKEGVPIK TGEGIQIYEE
490 500 510 520 530 540
DGTHCLWLKK ACLGDSGSYS CAAFNPRGQT STSWLLTVKR PKVEEVAPCF SSVLKGCTVS
550 560 570 580 590 600
EGQDFVLQCY VGGVPVPEIT WLLNEQPIQY AHSTFEAGVA KLTVQDALPE DDGIYTCLAE
610 620 630 640 650 660
NNAGRASCSA QVTVKEKKSS KKAEGTQAAK LNKTFAPIFL KGLTDLKVMD GSQVIMTVEV
670 680 690 700 710 720
SANPCPEIIW LHNGKEIQET EDFHFEKKGN EYSLYIQEVF PEDTGKYTCE AWNELGETQT
730 740 750 760 770 780
QATLTVQEPQ DGIQPWFISK PRSVTAAAGQ NVLISCAIAG DPFPTVHWFK DGQEITPGTG
790 800 810 820 830 840
CEILQNEDIF TLILRNVQSR HAGQYEIQLR NQVGECSCQV SLMLRESSAS RAEMLRDGRE
850 860 870 880 890 900
SASSGERRDG GNYGALTFGR TSGFKKSSSE TRAAEEEQED VRGVLKRRVE TREHTEESLR
910 920 930 940 950 960
QQEAEQLDFR DILGKKVSTK SFSEEDLKEI PAEQMDFRAN LQRQVKPKTL SEEERKVHAP
970 980 990 1000 1010 1020
QQVDFRSVLA KKGTPKTPLP EKVPPPKPAV TDFRSVLGAK KKPPAENGSA STPAPNARAG
1030 1040 1050 1060 1070 1080
SEAQNATPNS EAPAPKPVVK KEEKNDRKCE HGCAVVDGGI IGKKAENKPA ASKPTPPPSK
1090 1100 1110 1120 1130 1140
GTAPSFTEKL QDAKVADGEK LVLQCRISSD PPASVSWTLD SKAIKSSKSI VISQEGTLCS
1150 1160 1170 1180 1190 1200
LTIEKVMPED GGEYKCIAEN AAGKAECACK VLVEDTSSTK AAKPAEKKTK KPKTTLPPVL
1210 1220 1230 1240 1250 1260
STESSEATVK KKPAPKTPPK AATPPQITQF PEDRKVRAGE SVELFAKVVG TAPITCTWMK
1270 1280 1290 1300 1310 1320
FRKQIQENEY IKIENAENSS KLTISSTKQE HCGCYTLVVE NKLGSRQAQV NLTVVDKPDP
1330 1340 1350 1360 1370 1380
PAGTPCASDI RSSSLTLSWY GSSYDGGSAV QSYTVEIWNS VDNKWTDLTT CRSTSFNVQD
1390 1400 1410 1420 1430 1440
LQADREYKFR VRAANVYGIS EPSQESEVVK VGEKQEEELK EEEAELSDDE GKETEVNYRT
1450 1460 1470 1480 1490 1500
VTINTEQKVS DVYNIEERLG SGKFGQVFRL VEKKTGKVWA GKFFKAYSAK EKENIRDEIS
1510 1520 1530 1540 1550 1560
IMNCLHHPKL VQCVDAFEEK ANIVMVLEMV SGGELFERII DEDFELTERE CIKYMRQISE
1570 1580 1590 1600 1610 1620
GVEYIHKQGI VHLDLKPENI MCVNKTGTSI KLIDFGLARR LESAGSLKVL FGTPEFVAPE
1630 1640 1650 1660 1670 1680
VINYEPIGYE TDMWSIGVIC YILVSGLSPF MGDNDNETLA NVTSATWDFD DEAFDEISDD
1690 1700 1710 1720 1730 1740
AKDFISNLLK KDMKSRLNCT QCLQHPWLQK DTKNMEAKKL SKDRMKKYMA RRKWQKTGHA
1750 1760 1770 1780 1790 1800
VRAIGRLSSM AMISGMSGRK ASGSSPTSPI NADKVENEDA FLEEVAEEKP HVKPYFTKTI
1810 1820 1830 1840 1850 1860
LDMEVVEGSA ARFDCKIEGY PDPEVMWYKD DQPVKESRHF QIDYDEEGNC SLTISEVCGD
1870 1880 1890 1900
DDAKYTCKAV NSLGEATCTA ELLVETMGKE GEGEGEGEED EEEEEE