MYLK_MOUSE
ID MYLK_MOUSE Reviewed; 1941 AA.
AC Q6PDN3; Q3TSJ7; Q80UX0; Q80YN7; Q80YN8; Q8K026; Q924D2; Q9ERD3;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Myosin light chain kinase, smooth muscle;
DE Short=MLCK;
DE Short=smMLCK;
DE EC=2.7.11.18;
DE AltName: Full=Kinase-related protein;
DE Short=KRP;
DE AltName: Full=Telokin;
DE Contains:
DE RecName: Full=Myosin light chain kinase, smooth muscle, deglutamylated form;
GN Name=Mylk {ECO:0000312|EMBL:AAH58610.2, ECO:0000312|MGI:MGI:894806};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC STRAIN=C3H/HeJ; TISSUE=Cardiac myocyte;
RX PubMed=11029314; DOI=10.1152/ajpcell.2000.279.5.c1656;
RA Herring B.P., Dixon S.A., Gallagher P.J.;
RT "Smooth muscle myosin light chain kinase expression in cardiac and skeletal
RT muscle.";
RL Am. J. Physiol. 279:C1656-C1664(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAG34169.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Swiss Webster / NIH {ECO:0000312|EMBL:AAG34169.1};
RX PubMed=11121372; DOI=10.1152/ajpcell.2001.280.1.c12;
RA Herring B.P., Lyons G.E., Hoggatt A.M., Gallagher P.J.;
RT "Telokin expression is restricted to smooth muscle tissues during mouse
RT development.";
RL Am. J. Physiol. 280:C12-C21(2001).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAO85807.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C3H/HeJ {ECO:0000312|EMBL:AAO85807.1};
RC TISSUE=Cardiac myocyte {ECO:0000269|PubMed:11832329};
RX PubMed=11832329; DOI=10.1152/ajpcell.00333.2001;
RA Blue E.K., Goeckeler Z.M., Jin Y., Hou L., Dixon S.A., Herring B.P.,
RA Wysolmerski R.B., Gallagher P.J.;
RT "220- and 130-kDa MLCKs have distinct tissue distributions and
RT intracellular localization patterns.";
RL Am. J. Physiol. 282:C451-C460(2002).
RN [4] {ECO:0000312|EMBL:BAE36678.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE36678.1};
RC TISSUE=Wolffian duct {ECO:0000312|EMBL:BAE36678.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5] {ECO:0000312|EMBL:AAH58610.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C3H/He {ECO:0000312|EMBL:AAH58610.2}, and
RC FVB/N {ECO:0000312|EMBL:AAH34209.1};
RC TISSUE=Colon {ECO:0000312|EMBL:AAH34209.1},
RC Mammary gland {ECO:0000312|EMBL:AAH45197.1}, and
RC Osteoblast {ECO:0000312|EMBL:AAH58610.2};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6] {ECO:0000312|EMBL:AAK53241.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1561 (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAK53241.1};
RX PubMed=11472067; DOI=10.1006/geno.2001.6571;
RA Giorgi D.G., Ferraz C., Mattei M.-G., Demaille J., Rouquier S.;
RT "The myosin light chain kinase gene is not duplicated in mouse: partial
RT structure and chromosomal localization of Mylk.";
RL Genomics 75:49-56(2001).
RN [7]
RP TISSUE SPECIFICITY, AND ALTERNATIVE PROMOTER USAGE (ISOFORM 4).
RX PubMed=8764148; DOI=10.1152/ajpcell.1996.270.6.c1656;
RA Herring B.P., Smith A.F.;
RT "Telokin expression is mediated by a smooth muscle cell-specific
RT promoter.";
RL Am. J. Physiol. 270:C1656-C1665(1996).
RN [8]
RP FUNCTION IN GIARDIASIS.
RX PubMed=12360480; DOI=10.1053/gast.2002.36002;
RA Scott K.G.-E., Meddings J.B., Kirk D.R., Lees-Miller S.P., Buret A.G.;
RT "Intestinal infection with Giardia spp. reduces epithelial barrier function
RT in a myosin light chain kinase-dependent fashion.";
RL Gastroenterology 123:1179-1190(2002).
RN [9] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16055522; DOI=10.1152/ajpheart.00511.2004;
RA Ohlmann P., Tesse A., Loichot C., Ralay Ranaivo H., Roul G., Philippe C.,
RA Watterson D.M., Haiech J., Andriantsitohaina R.;
RT "Deletion of MLCK210 induces subtle changes in vascular reactivity but does
RT not affect cardiac function.";
RL Am. J. Physiol. 289:H2342-H2349(2005).
RN [10]
RP FUNCTION IN INTESTINAL BARRIER DYSFUNCTION.
RX PubMed=16184195; DOI=10.1172/jci24970;
RA Clayburgh D.R., Barrett T.A., Tang Y., Meddings J.B., Van Eldik L.J.,
RA Watterson D.M., Clarke L.L., Mrsny R.J., Turner J.R.;
RT "Epithelial myosin light chain kinase-dependent barrier dysfunction
RT mediates T cell activation-induced diarrhea in vivo.";
RL J. Clin. Invest. 115:2702-2715(2005).
RN [11]
RP INTERACTION WITH SVIL.
RX PubMed=17925381; DOI=10.1242/jcs.008219;
RA Takizawa N., Ikebe R., Ikebe M., Luna E.J.;
RT "Supervillin slows cell spreading by facilitating myosin II activation at
RT the cell periphery.";
RL J. Cell Sci. 120:3792-3803(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355; SER-1782 AND SER-1798,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [13]
RP FUNCTION IN MICROVASCULAR HYPERPERMEABILITY DURING SEVERE BURNS, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=17577141; DOI=10.1097/shk.0b013e31804d415f;
RA Reynoso R., Perrin R.M., Breslin J.W., Daines D.A., Watson K.D.,
RA Watterson D.M., Wu M.H., Yuan S.;
RT "A role for long chain myosin light chain kinase (MLCK-210) in
RT microvascular hyperpermeability during severe burns.";
RL Shock 28:589-595(2007).
RN [14]
RP FUNCTION IN SMOOTH MUSCLE CONTRACTION.
RX PubMed=18586037; DOI=10.1053/j.gastro.2008.05.032;
RA He W.-Q., Peng Y.-J., Zhang W.-C., Lv N., Tang J., Chen C., Zhang C.-H.,
RA Gao S., Chen H.-Q., Zhi G., Feil R., Kamm K.E., Stull J.T., Gao X.,
RA Zhu M.-S.;
RT "Myosin light chain kinase is central to smooth muscle contraction and
RT required for gastrointestinal motility in mice.";
RL Gastroenterology 135:610-620(2008).
RN [15]
RP FUNCTION AS PTK2B/PYK2 KINASE, AND INTERACTION WITH PTK2B/PYK2.
RX PubMed=18587400; DOI=10.1038/ni.1628;
RA Xu J., Gao X.-P., Ramchandran R., Zhao Y.-Y., Vogel S.M., Malik A.B.;
RT "Nonmuscle myosin light-chain kinase mediates neutrophil transmigration in
RT sepsis-induced lung inflammation by activating beta2 integrins.";
RL Nat. Immunol. 9:880-886(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-355; SER-935;
RP SER-1460; SER-1781; SER-1782; SER-1795; SER-1798; THR-1800 AND SER-1801,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [17]
RP DEGLUTAMYLATION.
RX PubMed=21074048; DOI=10.1016/j.cell.2010.10.014;
RA Rogowski K., van Dijk J., Magiera M.M., Bosc C., Deloulme J.C., Bosson A.,
RA Peris L., Gold N.D., Lacroix B., Grau M.B., Bec N., Larroque C.,
RA Desagher S., Holzer M., Andrieux A., Moutin M.J., Janke C.;
RT "A family of protein-deglutamylating enzymes associated with
RT neurodegeneration.";
RL Cell 143:564-578(2010).
RN [18]
RP FUNCTION IN TONIC AIRWAY SMOOTH MUSCLE CONTRACTION.
RX PubMed=20018858; DOI=10.1074/jbc.m109.062836;
RA Zhang W.-C., Peng Y.-J., Zhang G.-S., He W.-Q., Qiao Y.-N., Dong Y.-Y.,
RA Gao Y.-Q., Chen C., Zhang C.-H., Li W., Shen H.-H., Ning W., Kamm K.E.,
RA Stull J.T., Gao X., Zhu M.-S.;
RT "Myosin light chain kinase is necessary for tonic airway smooth muscle
RT contraction.";
RL J. Biol. Chem. 285:5522-5531(2010).
RN [19]
RP FUNCTION IN TIGHT JUNCTION REGULATION.
RX PubMed=20404178; DOI=10.1073/pnas.0908869107;
RA Yu D., Marchiando A.M., Weber C.R., Raleigh D.R., Wang Y., Shen L.,
RA Turner J.R.;
RT "MLCK-dependent exchange and actin binding region-dependent anchoring of
RT ZO-1 regulate tight junction barrier function.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8237-8241(2010).
CC -!- FUNCTION: Calcium/calmodulin-dependent myosin light chain kinase
CC implicated in smooth muscle contraction via phosphorylation of myosin
CC light chains (MLC). Also regulates actin-myosin interaction through a
CC non-kinase activity. Phosphorylates PTK2B/PYK2 and myosin light-chains.
CC Involved in the inflammatory response (e.g. apoptosis, vascular
CC permeability, leukocyte diapedesis), cell motility and morphology,
CC airway hyperreactivity and other activities relevant to asthma.
CC Required for tonic airway smooth muscle contraction that is necessary
CC for physiological and asthmatic airway resistance. Necessary for
CC gastrointestinal motility. Implicated in the regulation of endothelial
CC as well as vascular permeability, probably via the regulation of
CC cytoskeletal rearrangements. In the nervous system it has been shown to
CC control the growth initiation of astrocytic processes in culture and to
CC participate in transmitter release at synapses formed between cultured
CC sympathetic ganglion cells. Critical participant in signaling sequences
CC that result in fibroblast apoptosis. Plays a role in the regulation of
CC epithelial cell survival. Required for epithelial wound healing,
CC especially during actomyosin ring contraction during purse-string wound
CC closure. Mediates RhoA-dependent membrane blebbing. Triggers TRPC5
CC channel activity in a calcium-dependent signaling, by inducing its
CC subcellular localization at the plasma membrane. Promotes cell
CC migration (including tumor cells) and tumor metastasis. PTK2B/PYK2
CC activation by phosphorylation mediates ITGB2 activation and is thus
CC essential to trigger neutrophil transmigration during acute lung injury
CC (ALI). May regulate optic nerve head astrocyte migration. Probably
CC involved in mitotic cytoskeletal regulation. Regulates tight junction
CC probably by modulating ZO-1 exchange in the perijunctional actomyosin
CC ring. Mediates burn-induced microvascular barrier injury; triggers
CC endothelial contraction in the development of microvascular
CC hyperpermeability by phosphorylating MLC. Essential for intestinal
CC barrier dysfunction. Mediates Giardia spp.-mediated reduced epithelial
CC barrier function during giardiasis intestinal infection via
CC reorganization of cytoskeletal F-actin and tight junctional ZO-1.
CC Necessary for hypotonicity-induced Ca(2+) entry and subsequent
CC activation of volume-sensitive organic osmolyte/anion channels (VSOAC)
CC in cervical cancer cells. {ECO:0000269|PubMed:11832329,
CC ECO:0000269|PubMed:12360480, ECO:0000269|PubMed:16055522,
CC ECO:0000269|PubMed:16184195, ECO:0000269|PubMed:17577141,
CC ECO:0000269|PubMed:18586037, ECO:0000269|PubMed:18587400,
CC ECO:0000269|PubMed:20018858, ECO:0000269|PubMed:20404178}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[myosin light chain] = ADP + H(+) + O-phospho-L-
CC seryl-[myosin light chain]; Xref=Rhea:RHEA:22004, Rhea:RHEA-
CC COMP:13684, Rhea:RHEA-COMP:13685, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC ChEBI:CHEBI:456216; EC=2.7.11.18;
CC Evidence={ECO:0000269|PubMed:11832329};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[myosin light chain] = ADP + H(+) + O-
CC phospho-L-threonyl-[myosin light chain]; Xref=Rhea:RHEA:53900,
CC Rhea:RHEA-COMP:13686, Rhea:RHEA-COMP:13687, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.18;
CC Evidence={ECO:0000269|PubMed:11832329};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- SUBUNIT: All isoforms including Telokin bind calmodulin. Interacts with
CC CTTN; this interaction is reduced during thrombin-induced endothelial
CC cell (EC) contraction but is promoted by the barrier-protective agonist
CC sphingosine 1-phosphate (S1P) within lamellipodia. A complex made of
CC ABL1, CTTN and MYLK regulates cortical actin-based cytoskeletal
CC rearrangement critical to sphingosine 1-phosphate (S1P)-mediated
CC endothelial cell (EC) barrier enhancement. Binds to NAA10/ARD1 (By
CC similarity). Interacts with SVIL and PTK2B/PYK2. {ECO:0000250,
CC ECO:0000269|PubMed:17925381, ECO:0000269|PubMed:18587400}.
CC -!- INTERACTION:
CC Q6PDN3; Q9JMG9: Patz1; NbExp=3; IntAct=EBI-647412, EBI-647451;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11832329}. Cell
CC projection, lamellipodium {ECO:0000250|UniProtKB:Q15746}. Cleavage
CC furrow {ECO:0000250|UniProtKB:Q15746}. Cytoplasm, cytoskeleton, stress
CC fiber {ECO:0000269|PubMed:11832329}. Note=Localized to stress fibers
CC during interphase and to the cleavage furrow during mitosis.
CC {ECO:0000250|UniProtKB:Q15746}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton, stress
CC fiber {ECO:0000269|PubMed:11832329}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm
CC {ECO:0000269|PubMed:11832329}. Note=Throughout the cytoplasm with
CC higher levels near the plasma membrane. {ECO:0000269|PubMed:11832329}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000269|PubMed:11832329}; Synonyms=Non muscle isozyme
CC {ECO:0000269|PubMed:11832329};
CC IsoId=Q6PDN3-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16141072};
CC IsoId=Q6PDN3-2; Sequence=VSP_052002, VSP_052003;
CC Name=3; Synonyms=Smooth muscle isozyme;
CC IsoId=Q6PDN3-3; Sequence=VSP_018847;
CC Name=4; Synonyms=Telokin;
CC IsoId=Q6PDN3-4; Sequence=VSP_018848;
CC -!- TISSUE SPECIFICITY: Smooth muscle isoform is expressed in all tissues
CC with highest levels in bladder, uterus, vas deferens, colon, ileum, and
CC tracheae. Isoform 1 is expressed in lung, bladder, and vas deferens.
CC Telokin is expressed in smooth muscle cells of the gut, reproductive
CC tract and urinary tract, including in uterus, vas deferens, bladder,
CC colon, kidney, ureter and ovary. Telokin is also detected in the
CC trachea. {ECO:0000269|PubMed:11121372, ECO:0000269|PubMed:11832329,
CC ECO:0000269|PubMed:8764148}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 is widely expressed at 14.5 dpc embryos
CC with highest levels in some areas of the developing brain, the lower
CC gastrointestinal tract, as well as certain blood vessels. Primary
CC cultures of endothelial cells lose high level expression of smooth
CC muscle isoform with increasing number of passages. Telokin is expressed
CC in the embryonic gut from 11.5 dpc with highest level at 15.5 dpc. Also
CC expressed in developing bronchi from 13.5 dpc. High levels in 15.5 dpc
CC bladder, ureter, urethra and rectum. Telokin expression is induced in
CC reproductive tract during postnatal development.
CC {ECO:0000269|PubMed:11121372, ECO:0000269|PubMed:11832329}.
CC -!- PTM: Can probably be down-regulated by phosphorylation. Tyrosine
CC phosphorylation by ABL1 increases kinase activity, reverses MLCK-
CC mediated inhibition of Arp2/3-mediated actin polymerization, and
CC enhances CTTN-binding. Phosphorylation by SRC at Tyr-452 promotes CTTN
CC binding (By similarity). {ECO:0000250}.
CC -!- PTM: The C-terminus is deglutamylated by AGTPBP1/CCP1, AGBL1/CCP4 and
CC AGBL4/CCP6, leading to the formation of Myosin light chain kinase,
CC smooth muscle, deglutamylated form. The consequences of C-terminal
CC deglutamylation are unknown (PubMed:21074048).
CC {ECO:0000269|PubMed:21074048}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking isoform 1 show a reduced flow-
CC mediated dilation of small mesenteric arteries but no significant
CC changes in main cardiovascular function. Increased survival from burn.
CC Prevention of epithelial MLC phosphorylation, tight junction
CC disruption, protein leak, and diarrhea following T-cell activation.
CC {ECO:0000269|PubMed:16055522, ECO:0000269|PubMed:17577141}.
CC -!- MISCELLANEOUS: [Isoform 2]: Might be produced by alternative promoter
CC usage and alternative splicing. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH58610.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAO85807.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY237727; AAO85808.1; -; mRNA.
DR EMBL; AF314149; AAG34169.1; -; mRNA.
DR EMBL; AY237726; AAO85807.1; ALT_INIT; mRNA.
DR EMBL; AK162008; BAE36678.1; -; mRNA.
DR EMBL; BC034209; AAH34209.1; -; mRNA.
DR EMBL; BC045197; AAH45197.1; -; mRNA.
DR EMBL; BC058610; AAH58610.2; ALT_INIT; mRNA.
DR EMBL; AF335470; AAK53241.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6PDN3; -.
DR SMR; Q6PDN3; -.
DR IntAct; Q6PDN3; 20.
DR MINT; Q6PDN3; -.
DR STRING; 10090.ENSMUSP00000023538; -.
DR MoonDB; Q6PDN3; Predicted.
DR iPTMnet; Q6PDN3; -.
DR PhosphoSitePlus; Q6PDN3; -.
DR jPOST; Q6PDN3; -.
DR MaxQB; Q6PDN3; -.
DR PaxDb; Q6PDN3; -.
DR PeptideAtlas; Q6PDN3; -.
DR PRIDE; Q6PDN3; -.
DR ProteomicsDB; 286099; -. [Q6PDN3-1]
DR ProteomicsDB; 286100; -. [Q6PDN3-2]
DR ProteomicsDB; 286101; -. [Q6PDN3-3]
DR ProteomicsDB; 286102; -. [Q6PDN3-4]
DR Antibodypedia; 4044; 392 antibodies from 37 providers.
DR Ensembl; ENSMUST00000231589; ENSMUSP00000156149; ENSMUSG00000022836. [Q6PDN3-4]
DR UCSC; uc007zbe.1; mouse. [Q6PDN3-1]
DR UCSC; uc007zbh.1; mouse. [Q6PDN3-4]
DR MGI; MGI:894806; Mylk.
DR VEuPathDB; HostDB:ENSMUSG00000022836; -.
DR eggNOG; KOG0613; Eukaryota.
DR GeneTree; ENSGT00940000157879; -.
DR InParanoid; Q6PDN3; -.
DR OMA; MQVLEIQ; -.
DR BRENDA; 2.7.11.18; 3474.
DR Reactome; R-MMU-445355; Smooth Muscle Contraction.
DR Reactome; R-MMU-5627123; RHO GTPases activate PAKs.
DR ChiTaRS; Mylk; mouse.
DR PRO; PR:Q6PDN3; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q6PDN3; protein.
DR Bgee; ENSMUSG00000022836; Expressed in ureter smooth muscle and 244 other tissues.
DR ExpressionAtlas; Q6PDN3; baseline and differential.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0032154; C:cleavage furrow; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004687; F:myosin light chain kinase activity; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0060414; P:aorta smooth muscle tissue morphogenesis; ISO:MGI.
DR GO; GO:0032060; P:bleb assembly; ISO:MGI.
DR GO; GO:0071476; P:cellular hypotonic response; ISO:MGI.
DR GO; GO:0071277; P:cellular response to calcium ion; IDA:MGI.
DR GO; GO:0035865; P:cellular response to potassium ion; IDA:MGI.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:MGI.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0090303; P:positive regulation of wound healing; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0006939; P:smooth muscle contraction; IMP:UniProtKB.
DR GO; GO:0014820; P:tonic smooth muscle contraction; IMP:UniProtKB.
DR CDD; cd00063; FN3; 1.
DR CDD; cd14191; STKc_MLCK1; 1.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR015725; MLCK1_kinase_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07679; I-set; 9.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00409; IG; 9.
DR SMART; SM00408; IGc2; 9.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48726; SSF48726; 9.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 9.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative promoter usage; Alternative splicing;
KW ATP-binding; Calcium; Calmodulin-binding; Cell projection; Cytoplasm;
KW Cytoskeleton; Disulfide bond; Immunoglobulin domain; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1941
FT /note="Myosin light chain kinase, smooth muscle"
FT /id="PRO_0000233949"
FT CHAIN 1..1934
FT /note="Myosin light chain kinase, smooth muscle,
FT deglutamylated form"
FT /id="PRO_0000403732"
FT DOMAIN 33..122
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 156..244
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255"
FT DOMAIN 402..485
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255"
FT DOMAIN 502..587
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255"
FT DOMAIN 611..699
FT /note="Ig-like C2-type 5"
FT /evidence="ECO:0000255"
FT DOMAIN 709..809
FT /note="Ig-like C2-type 6"
FT /evidence="ECO:0000255"
FT REPEAT 856..883
FT /note="1-1"
FT /evidence="ECO:0000250|UniProtKB:Q15746"
FT REPEAT 884..911
FT /note="1-2"
FT /evidence="ECO:0000250|UniProtKB:Q15746"
FT REPEAT 912..939
FT /note="1-3"
FT /evidence="ECO:0000250|UniProtKB:Q15746"
FT REPEAT 940..966
FT /note="1-4"
FT /evidence="ECO:0000250|UniProtKB:Q15746"
FT REPEAT 967..985
FT /note="1-5; truncated"
FT REPEAT 990..1002
FT /note="2-1"
FT /evidence="ECO:0000250|UniProtKB:Q15746"
FT REPEAT 1003..1014
FT /note="2-2"
FT /evidence="ECO:0000250|UniProtKB:Q15746"
FT REPEAT 1015..1026
FT /note="2-3"
FT /evidence="ECO:0000250|UniProtKB:Q15746"
FT REPEAT 1027..1038
FT /note="2-4"
FT /evidence="ECO:0000250|UniProtKB:Q15746"
FT REPEAT 1039..1049
FT /note="2-5"
FT /evidence="ECO:0000250|UniProtKB:Q15746"
FT DOMAIN 1120..1208
FT /note="Ig-like C2-type 7"
FT /evidence="ECO:0000255"
FT DOMAIN 1260..1348
FT /note="Ig-like C2-type 8"
FT /evidence="ECO:0000255"
FT DOMAIN 1356..1449
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1486..1741
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1831..1920
FT /note="Ig-like C2-type 9"
FT /evidence="ECO:0000255"
FT REGION 255..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..985
FT /note="5 X 28 AA approximate tandem repeats"
FT REGION 911..951
FT /note="Actin-binding (calcium/calmodulin-sensitive)"
FT /evidence="ECO:0000250"
FT REGION 920..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..951
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 990..1049
FT /note="5 X 12 AA approximate tandem repeats"
FT REGION 1048..1482
FT /note="Actin-binding (calcium/calmodulin-insensitive)"
FT /evidence="ECO:0000250"
FT REGION 1212..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1435..1469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1733..1796
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q15746"
FT REGION 1789..1809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..937
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1098
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1789..1805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1607
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1492..1500
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1515
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 226
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:Q15746"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15746"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 452
FT /note="Phosphotyrosine; by ABL1 and SRC"
FT /evidence="ECO:0000250|UniProtKB:Q15746"
FT MOD_RES 780
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:Q15746"
FT MOD_RES 935
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1471
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:Q15746"
FT MOD_RES 1597
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:Q15746"
FT MOD_RES 1657
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:Q15746"
FT MOD_RES 1781
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1782
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1794
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15746"
FT MOD_RES 1795
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1798
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1800
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1801
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT DISULFID 177..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 423..475
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 523..571
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 730..793
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1141..1192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1852..1904
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..1782
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11121372"
FT /id="VSP_018848"
FT VAR_SEQ 1..1254
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052002"
FT VAR_SEQ 1..910
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11029314"
FT /id="VSP_018847"
FT VAR_SEQ 1255..1256
FT /note="KA -> MQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052003"
FT CONFLICT 173
FT /note="W -> G (in Ref. 3 and 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="S -> A (in Ref. 6; AAK53241)"
FT /evidence="ECO:0000305"
FT CONFLICT 471..472
FT /note="RK -> GR (in Ref. 3 and 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="S -> T (in Ref. 3; AAO85807)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="G -> A (in Ref. 3; AAO85807)"
FT /evidence="ECO:0000305"
FT CONFLICT 666..667
FT /note="HS -> TP (in Ref. 3; AAO85807)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="D -> S (in Ref. 3; AAO85807)"
FT /evidence="ECO:0000305"
FT CONFLICT 749..750
FT /note="LS -> SP (in Ref. 3; AAO85807)"
FT /evidence="ECO:0000305"
FT CONFLICT 1004
FT /note="A -> G (in Ref. 3; AAO85807)"
FT /evidence="ECO:0000305"
FT CONFLICT 1038
FT /note="G -> A (in Ref. 3; AAO85807)"
FT /evidence="ECO:0000305"
FT CONFLICT 1106
FT /note="A -> R (in Ref. 3; AAO85807)"
FT /evidence="ECO:0000305"
FT CONFLICT 1174..1181
FT /note="RFSVSIEK -> TFLCLHRE (in Ref. 3; AAO85807)"
FT /evidence="ECO:0000305"
FT CONFLICT 1210
FT /note="D -> A (in Ref. 3; AAO85807)"
FT /evidence="ECO:0000305"
FT CONFLICT 1289
FT /note="I -> T (in Ref. 3; AAO85807)"
FT /evidence="ECO:0000305"
FT CONFLICT 1340
FT /note="Missing (in Ref. 4; BAE36678)"
FT /evidence="ECO:0000305"
FT CONFLICT 1409
FT /note="T -> H (in Ref. 3; AAO85807)"
FT /evidence="ECO:0000305"
FT CONFLICT 1657
FT /note="Y -> H (in Ref. 5; AAH58610)"
FT /evidence="ECO:0000305"
FT CONFLICT 1661
FT /note="G -> R (in Ref. 3; AAO85807)"
FT /evidence="ECO:0000305"
FT CONFLICT 1678
FT /note="S -> R (in Ref. 3; AAO85807)"
FT /evidence="ECO:0000305"
FT CONFLICT 1706
FT /note="A -> E (in Ref. 3; AAO85807)"
FT /evidence="ECO:0000305"
FT CONFLICT 1732..1735
FT /note="CTQC -> STHG (in Ref. 3; AAO85807)"
FT /evidence="ECO:0000305"
FT CONFLICT 1825
FT /note="E -> K (in Ref. 3; AAO85807)"
FT /evidence="ECO:0000305"
FT CONFLICT 1888
FT /note="S -> T (in Ref. 2; AAG34169)"
FT /evidence="ECO:0000305"
FT CONFLICT 1941
FT /note="Missing (in Ref. 5; AAH58610)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1941 AA; 212925 MW; 7FF12C60F1BDFFDD CRC64;
MGDVKLFASS HMSKTSHSVD PSKVSSMPLT EAPAFILPPR NLCVKEGATA KFEGRVRGYP
EPQVTWHRKG QAITNGGRFL LDCGVRGTFS LVIHTVREED KGKYTCEASN GSGARQVTVE
LTVEGNSMKK RDQPVLSKAS GFPGETRPSI WGECPPKFAT KLGRAVVKEG QMWRFSCKIT
GRPPPQVTWL KGNVPLQPSA RVSMSEKNGM QILEIRGVTR DDLGVYTCMV VNGSGKASMS
AELSIPGLDN ASRLAVRGTK APSPDIRKEV TNGVSKDPET VAESKNCPSP QRSGSSARAT
NSHLKSPQEP KPKLCEDAPR KVPQSSILQK STSTITLQAL KVQPEARVPA IGSFSPGEDR
KSLAAPQQAT LPTRQSSLGG SVGNKFVTGN IPRESQREST FPRFESQPQS QEVTEGQTVK
FICEVSGIPK PDVGWFLEGI PVRRREGITE VYEDGVSHHL CLLRARTRDS RKYSCTASNS
LGQVSCSWSL LVDRPNLAQT APSFSSVLKD SVVIEGQDFV LRCSVQGTPA PRVTWLLNGQ
PIQFAHSICE AGVAELHIQD ALPEDRGTYT CLAENAMGQV SCSATVTVQE KKGEGEREHR
LSPARSKPIA PIFLQGLSDL KVMDGSQVTM TVQVSGNPPP EVIWLHDGNE IQESEDFHFE
QKGGWHSLCI QEVFPEDTGT YTCEAWNSAG EVRTRAVLTV QEPHDGTQPW FISKPRSVTA
TLGQSVLISC AIAGDPFPTV HWLRDGRALS KDSGHFELLQ NEDVFTLVLK NVQPWHAGQY
EILLKNRVGE CSCQVSLMLH NSPSRAPPRG REPASCEGLC GGGGVGAHGD GDRHGTLRPC
WPARGQGWPE EEDGEDVRGL LKRRVETRLH TEEAIRQQEV GQLDFRDLLG KKVSTKTVSE
DDLKDIPAEQ MDFRANLQRQ VKPKTISEEE RKVHSPQQVD FRSVLAKKGT PKTPVPEKAP
PKAATPDFRS VLGGKKKSPS ENGGNSAEVL NVKAGESPTP AGDAQAIGAL KPVGNAKPAE
TPKPIGNAKP TETLKPVGNT KPAETLKPIA NAQPSGSLKP VTNAQPAEPQ KPVGNAKSAE
TSKPAGKEEV KEVKNDVNCK KGQVGATGNE KRPESQGSAP VFKEKLQDVH VAEGEKLLLQ
CQVISDPPAT VTWSLNGKTL KTTKFIVLAQ EGSRFSVSIE KALPEDRGLY KCVAKNSAGQ
AECSCQVTVD DAQTSENTKA PEMKSRRPKS SLPPVLGTES DATVKKKPAP KTPTKAAMPP
QIIQFPEDQK VRAGEPVELF GKVAGTQPIT CKWMKFRKQI QESEHIKVEN GESGSKLTIL
AARQEHCGCY TLVVENKLGS RQAQVNLTVV DKPDPPAGTP CASDIRSSSL TLSWYGSSYD
GGSAVQSYNV EIWDTEDKVW KELATCRSTS FNVQDLLPDR EYKFRVRAVN VYGTSEPSQE
SELTAVGEKP EEPKDEVEVS DDDEKEPEVD YRTVTVNTEQ KVSDVYDIEE RLGSGKFGQV
FRLVEKKTGK IWAGKFFKAY SAKEKDNIRQ EISIMNCLHH PKLVQCVDAF EEKANIVMVL
EIVSGGELFE RIIDEDFELT ERECIKYMRQ ISEGVEYIHK QGIVHLDLKP ENIMCVNKTG
TRIKLIDFGL ARRLENAGSL KVLFGTPEFV APEVINYEPI GYATDMWSIG VICYILVSGL
SPFMGDNDNE TLANVTSATW DFDDEAFDEI SDDAKDFISN LLKKDMKNRL DCTQCLQHPW
LMKDTKNMEA KKLSKDRMKK YMARRKWQKT GNAVRAIGRL SSMAMISGLS GRKSSTGSPT
SPINAEKLES EDDVSQAFLE AVAEEKPHVK PYFSKTIRDL EVVEGSAARF DCKIEGYPDP
EVVWFKDDQS IRESRHFQID YDEDGNCSLI ISDVCGDDDA KYTCKAVNSL GEATCTAELI
VETMEEGEGE EGGEEEEEEE E
