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P11799 (MYLK_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myosin light chain kinase, smooth muscle

Short name=MLCK
EC=2.7.11.18
Alternative name(s):
Telokin
Gene names
Name:Mylk
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length1906 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphorylates a specific serine in the N-terminus of a myosin light chain, which leads to the formation of calmodulin/MLCK signal transduction complexes which allow selective transduction of calcium signals.

Catalytic activity

ATP + [myosin light-chain] = ADP + [myosin light-chain] phosphate.

Cofactor

Magnesium By similarity.

Calcium By similarity.

Enzyme regulation

Activated by phosphorylation on Tyr-478. Isoforms which lack this tyrosine residue are not regulated in this way. All catalytically active isoforms require binding to calcium and calmodulin for activation.

Subunit structure

All isoforms including Telokin bind calmodulin.

Subcellular location

Cytoplasmcytosol. Membrane. Note: Telokin is cytosolic and can translocate to the membrane upon stimulation. Ref.9

Tissue specificity

Isoform telokinis expressed in gizzard, heart, lung, intestine, and skeletal muscle although the levels of the expression in the latter were much less than that in the gizzard.

Post-translational modification

The C-terminus is deglutamylated, leading to the formation of Myosin light chain kinase, smooth muscle, deglutamylated form. The C-terminus is variable, with one to five C-terminal glutamyl residues being removed producing five forms differring in their number of C-terminal glutamyl residues.

Acetylated. Ref.8

Phosphorylation of telokin by PKG has no significant effect on its myosin binding activity, but promotes translocation to the membrane.

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.

Contains 1 fibronectin type-III domain.

Contains 9 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Alternative products

This entry describes 3 isoforms produced by alternative initiation. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P11799-1)

Also known as: MLCK-108; Smooth-muscle;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P11799-2)

Also known as: MLCK-210; Non-muscle;

The sequence of this isoform differs from the canonical sequence as follows:
     1-934: Missing.
Isoform 3 (identifier: P11799-3)

Also known as: Telokin;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1749: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 19061906Myosin light chain kinase, smooth muscle
PRO_0000024361
Chain1 – 19011901Myosin light chain kinase, smooth muscle, deglutamylated form
PRO_0000424867

Regions

Domain28 – 11790Ig-like C2-type 1
Domain156 – 24489Ig-like C2-type 2
Domain429 – 51789Ig-like C2-type 3
Domain521 – 61393Ig-like C2-type 4
Domain637 – 72589Ig-like C2-type 5
Repeat660 – 67617IIA-1
Repeat693 – 70816IIB-1
Domain735 – 83096Ig-like C2-type 6
Repeat758 – 77417IIA-2
Repeat791 – 80717IIB-2
Repeat970 – 98718III-1
Repeat999 – 101618III-2
Repeat1061 – 107818III-3
Domain1084 – 117289Ig-like C2-type 7
Repeat1107 – 112317IIA-3
Repeat1140 – 115617IIB-3
Repeat1209 – 122618III-4
Domain1225 – 131389Ig-like C2-type 8
Repeat1281 – 129717IIB-4
Domain1321 – 141494Fibronectin type-III
Domain1453 – 1708256Protein kinase
Domain1794 – 188592Ig-like C2-type 9
Repeat1817 – 183317IIA-4
Repeat1851 – 186616IIB-5
Nucleotide binding1459 – 14679ATP By similarity
Region660 – 183311744 X repeats, motif IIA
Region693 – 186611745 X repeats, motif IIB
Region970 – 12262574 X repeats, motif III
Region1317 – 136448Motif IA
Region1385 – 140218Motif IB
Region1700 – 176364Calmodulin-binding
Region1716 – 172813Calmodulin autoinhibition (AM13) region Potential
Region1730 – 174920Calmodulin recognition (RS20) region Potential
Compositional bias1896 – 190611Poly-Glu

Sites

Active site15741Proton acceptor
Binding site14821ATP By similarity

Amino acid modifications

Modified residue4781Phosphotyrosine
Modified residue17481Phosphoserine
Modified residue17621Phosphoserine; by PKG Ref.9
Modified residue17681Phosphoserine; by MAPK Probable

Natural variations

Alternative sequence1 – 17491749Missing in isoform 3.
VSP_018852
Alternative sequence1 – 934934Missing in isoform 2.
VSP_018851

Experimental info

Mutagenesis17621S → A: Decreases membrane translocation. Ref.9
Mutagenesis17681S → A: Decreases membrane translocation. Ref.9
Sequence conflict14391R → Q in AAA49069. Ref.5
Sequence conflict14391R → Q in AAA69964. Ref.5
Sequence conflict17761E → D AA sequence Ref.8

Secondary structure

... 1906
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (MLCK-108) (Smooth-muscle) [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: AD7D8A3B69EE3363

FASTA1,906210,446
        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 

« Hide

Isoform 2 (MLCK-210) (Non-muscle) [UniParc].

Checksum: 375ED3627731EFFE
Show »

FASTA972107,547
Isoform 3 (Telokin) [UniParc].

Checksum: 557E7CD96C672E7D
Show »

FASTA15717,337

References

[1]"Multiple gene products are produced from a novel protein kinase transcription region."
Watterson D.M., Collinge M., Lukas T.J., van Eldik L.J., Birukov K.G., Stepanova O.V., Shirinsky V.P.
FEBS Lett. 373:217-220(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Regulatory and structural motifs of chicken gizzard myosin light chain kinase."
Olson N.J., Pearson R.B., Needleman D.S., Hurwitz M.J., Kemp B.E., Means A.R.
Proc. Natl. Acad. Sci. U.S.A. 87:2284-2288(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"The organization of the genetic locus for chicken myosin light chain kinase is complex: multiple proteins are encoded and exhibit differential expression and localization."
Birukov K.G., Schavocky J.P., Shirinsky V.P., Van Eldik L.J., Watterson D.M.
J. Cell. Biochem. 70:402-413(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.
[4]"Use of DNA sequence and mutant analyses and antisense oligodeoxynucleotides to examine the molecular basis of nonmuscle myosin light chain kinase autoinhibition, calmodulin recognition, and activity."
Shoemaker M.O., Lau W., Shattuck R.L., Kwiatkowski A.P., Matrisian P.E., Guerra-Santos L., Wilson E., Lukas T.J., van Eldik L.J., Watterson D.M.
J. Cell Biol. 111:1107-1125(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 649-1906, PARTIAL PROTEIN SEQUENCE.
Tissue: Fibroblast.
[5]"Domain organization of chicken gizzard myosin light chain kinase deduced from a cloned cDNA."
Guerriero V. Jr., Russo M.A., Olson N.J., Putkey J.A., Means A.R.
Biochemistry 25:8372-8381(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1259-1906.
Tissue: Gizzard.
[6]"Molecular cloning of the chicken gizzard telokin gene and cDNA."
Yoshikai S., Ikebe M.
Arch. Biochem. Biophys. 299:242-247(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1750-1906 (ISOFORM 3).
Tissue: Gizzard.
[7]"Structure and expression of a calcium-binding protein gene contained within a calmodulin-regulated protein kinase gene."
Collinge M., Matrisian P.E., Zimmer W.E., Shattuck R.L., Lukas T.J., van Eldik L.J., Watterson D.M.
Mol. Cell. Biol. 12:2359-2371(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1750-1906 (ISOFORM 3).
[8]"Characterization of the chicken telokin heterogeneity by time-of-flight mass spectrometry."
Rusconi F., Potier M.C., Le Caer J.P., Schmitter J.M., Rossier J.
Biochemistry 36:11021-11026(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1775-1789, ACETYLATION, DEGLUTAMYLATION, PHOSPHORYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"Translocation of telokin by cGMP signaling in smooth muscle cells."
Komatsu S., Miyazaki K., Tuft R.A., Ikebe M.
Am. J. Physiol. 283:C752-C761(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-1762 AND SER-1768, MUTAGENESIS OF SER-1762 AND SER-1768.
[10]"Analysis of the functional coupling between calmodulin's calcium binding and peptide recognition properties."
Mirzoeva S., Weigand S., Lukas T.J., Shuvalova L., Anderson W.F., Watterson D.M.
Biochemistry 38:3936-3947(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1731-1749 IN COMPLEX WITH CALM1 AND CALCIUM.
[11]Erratum
Mirzoeva S., Weigand S., Lukas T.J., Shuvalova L., Anderson W.F., Watterson D.M.
Biochemistry 38:14117-14118(1999) [PubMed] [Europe PMC] [Abstract]
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52876 mRNA. Translation: CAA37056.1.
X52876 mRNA. Translation: CAA37057.1.
X52876 mRNA. Translation: CAA37058.1.
M31048 mRNA. Translation: AAA49069.1.
M14953 mRNA. Translation: AAA69964.1.
AF045285 expand/collapse EMBL AC list , AF045255, AF045256, AF045257, AF045260, AF045259, AF045258, AF045261, AF045263, AF045265, AF045274, AF045273, AF045272, AF045271, AF045270, AF045269, AF045268, AF045267, AF045266, AF045283, AF045282, AF045281, AF045280, AF045279, AF045278, AF045277, AF045276, AF045275, AF045284, AF045264, AF045262 Genomic DNA. Translation: AAC29031.1.
M96655 mRNA. Translation: AAA49083.1.
M88283 mRNA. Translation: AAA48647.1.
M88284 Genomic DNA. Translation: AAB53768.1.
PIRS68235.
RefSeqNP_990790.1. NM_205459.2.
UniGeneGga.4091.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CDLX-ray2.00E/F/G/H1730-1749[»]
1QS7X-ray1.80B/D1731-1750[»]
1VRKX-ray1.90B1731-1749[»]
2O5GX-ray1.08B1730-1748[»]
3EVUX-ray1.75A1731-1749[»]
3EVVX-ray2.60A1731-1749[»]
3O77X-ray2.35A1731-1749[»]
3O78X-ray2.60A/B1731-1749[»]
ProteinModelPortalP11799.
SMRP11799. Positions 525-614, 1221-1325, 1448-1716, 1785-1887.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid676694. 1 interaction.
IntActP11799. 3 interactions.

Chemistry

BindingDBP11799.
ChEMBLCHEMBL3062.

Proteomic databases

PaxDbP11799.
PRIDEP11799.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396445.
KEGGgga:396445.

Organism-specific databases

CTD4638.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000049287.
HOVERGENHBG052551.
InParanoidP11799.
KOK00907.
PhylomeDBP11799.

Enzyme and pathway databases

BRENDA2.7.11.18. 1306.

Family and domain databases

Gene3D2.60.40.10. 10 hits.
InterProIPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR020675. Myosin_light_ch_kinase-rel.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR015725. Telokin/Myosin_light_ch_kin.
[Graphical view]
PANTHERPTHR22964. PTHR22964. 1 hit.
PTHR22964:SF3. PTHR22964:SF3. 1 hit.
PfamPF00041. fn3. 1 hit.
PF07679. I-set. 9 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00060. FN3. 1 hit.
SM00409. IG. 1 hit.
SM00408. IGc2. 8 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50853. FN3. 1 hit.
PS50835. IG_LIKE. 9 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP11799.
NextBio20816486.
PROP11799.

Entry information

Entry nameMYLK_CHICK
AccessionPrimary (citable) accession number: P11799
Secondary accession number(s): P19038, Q549S2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references