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MRCKA_HUMAN
ID   MRCKA_HUMAN             Reviewed;        1732 AA.
AC   Q5VT25; O75039; Q59GZ1; Q5H9N9; Q5T797; Q5VT26; Q5VT27; Q86XX2; Q86XX3;
AC   Q99646;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 168.
DE   RecName: Full=Serine/threonine-protein kinase MRCK alpha;
DE            EC=2.7.11.1 {ECO:0000269|PubMed:29162624};
DE   AltName: Full=CDC42-binding protein kinase alpha;
DE   AltName: Full=DMPK-like alpha;
DE   AltName: Full=Myotonic dystrophy kinase-related CDC42-binding kinase alpha;
DE            Short=MRCK alpha;
DE            Short=Myotonic dystrophy protein kinase-like alpha;
GN   Name=CDC42BPA {ECO:0000312|EMBL:CAH71336.1}; Synonyms=KIAA0451;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAD57746.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 5), AND FUNCTION.
RC   TISSUE=Colon {ECO:0000312|EMBL:CAD57746.1};
RX   PubMed=15723050; DOI=10.1038/ncb1230;
RA   Wilkinson S., Paterson H.F., Marshall C.J.;
RT   "Cdc42-MRCK and Rho-ROCK signalling cooperate in myosin phosphorylation and
RT   cell invasion.";
RL   Nat. Cell Biol. 7:255-261(2005).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:CAD57745.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT VAL-1712.
RC   TISSUE=Brain {ECO:0000312|EMBL:CAD57745.1};
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ILE-1317
RP   AND VAL-1712.
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5] {ECO:0000305, ECO:0000312|EMBL:AAB37126.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-496, FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Mammary gland {ECO:0000269|PubMed:9092543};
RX   PubMed=9092543; DOI=10.1074/jbc.272.15.10013;
RA   Zhao Y., Loyer P., Li H., Valentine V., Kidd V., Kraft A.S.;
RT   "Cloning and chromosomal location of a novel member of the myotonic
RT   dystrophy family of protein kinases.";
RL   J. Biol. Chem. 272:10013-10020(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 799-1732 (ISOFORM 6), AND VARIANT
RP   VAL-1712.
RC   TISSUE=Brain;
RX   PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA   Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA   Nomura N., Ohara O.;
RT   "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT   human brain.";
RL   DNA Res. 4:345-349(1997).
RN   [7] {ECO:0000305, ECO:0000312|EMBL:CAD57745.1}
RP   SEQUENCE REVISION.
RA   Ohara O.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1521-1644, FUNCTION, INTERACTION WITH CDC42,
RP   AND MUTAGENESIS OF HIS-1579 AND HIS-1582.
RC   TISSUE=Brain {ECO:0000269|PubMed:9418861};
RX   PubMed=9418861; DOI=10.1128/mcb.18.1.130;
RA   Leung T., Chen X.-Q., Tan I., Manser E., Lim L.;
RT   "Myotonic dystrophy kinase-related Cdc42-binding kinase acts as a Cdc42
RT   effector in promoting cytoskeletal reorganization.";
RL   Mol. Cell. Biol. 18:130-140(1998).
RN   [9]
RP   FUNCTION IN PHOSPHORYLATION OF PPP1R12C.
RX   PubMed=11399775; DOI=10.1074/jbc.m102615200;
RA   Tan I., Ng C.H., Lim L., Leung T.;
RT   "Phosphorylation of a novel myosin binding subunit of protein phosphatase 1
RT   reveals a conserved mechanism in the regulation of actin cytoskeleton.";
RL   J. Biol. Chem. 276:21209-21216(2001).
RN   [10]
RP   FUNCTION IN PHOSPHORYLATION OF LIMK1 AND LIMK2.
RX   PubMed=11340065; DOI=10.1074/jbc.c100196200;
RA   Sumi T., Matsumoto K., Shibuya A., Nakamura T.;
RT   "Activation of LIM kinases by myotonic dystrophy kinase-related Cdc42-
RT   binding kinase alpha.";
RL   J. Biol. Chem. 276:23092-23096(2001).
RN   [11] {ECO:0000305}
RP   ACTIVITY REGULATION, OLIGOMERIZATION, PHOSPHORYLATION AT SER-222; SER-234
RP   AND THR-240, AND MUTAGENESIS OF LYS-106; SER-222; SER-234; THR-240 AND
RP   THR-403.
RX   PubMed=11283256; DOI=10.1128/mcb.21.8.2767-2778.2001;
RA   Tan I., Seow K.T., Lim L., Leung T.;
RT   "Intermolecular and intramolecular interactions regulate catalytic activity
RT   of myotonic dystrophy kinase-related Cdc42-binding kinase alpha.";
RL   Mol. Cell. Biol. 21:2767-2778(2001).
RN   [12]
RP   ALTERNATIVE SPLICING.
RX   PubMed=12568720; DOI=10.1016/s0378-1119(02)01185-x;
RA   Tan I., Cheong A., Lim L., Leung T.;
RT   "Genomic organization of human myotonic dystrophy kinase-related Cdc42-
RT   binding kinase alpha reveals multiple alternative splicing and functional
RT   diversity.";
RL   Gene 304:107-115(2003).
RN   [13]
RP   FUNCTION, AND INTERACTION WITH LURAP1 AND MYO18A.
RX   PubMed=18854160; DOI=10.1016/j.cell.2008.09.018;
RA   Tan I., Yong J., Dong J.M., Lim L., Leung T.;
RT   "A tripartite complex containing MRCK modulates lamellar actomyosin
RT   retrograde flow.";
RL   Cell 135:123-136(2008).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1545; SER-1719 AND SER-1721,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [15]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=20188707; DOI=10.1016/j.bbrc.2010.02.148;
RA   Cmejla R., Ptackova P., Petrak J., Savvulidi F., Cerny J., Sebesta O.,
RA   Vyoral D.;
RT   "Human MRCKalpha is regulated by cellular iron levels and interferes with
RT   transferrin iron uptake.";
RL   Biochem. Biophys. Res. Commun. 395:163-167(2010).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [17]
RP   FUNCTION IN PHOSPHORYLATION OF PPP1R12A AND MYL9/MLC2, AND ACTIVITY
RP   REGULATION.
RX   PubMed=21457715; DOI=10.1016/j.febslet.2011.03.054;
RA   Tan I., Lai J., Yong J., Li S.F., Leung T.;
RT   "Chelerythrine perturbs lamellar actomyosin filaments by selective
RT   inhibition of myotonic dystrophy kinase-related Cdc42-binding kinase.";
RL   FEBS Lett. 585:1260-1268(2011).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1651, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1611; SER-1613; SER-1629;
RP   SER-1651; SER-1664 AND SER-1721, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1669 AND SER-1693, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [21]
RP   FUNCTION, CATALYTIC ACTIVITY, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF
RP   ASP-478 AND ASP-984.
RX   PubMed=29162624; DOI=10.1083/jcb.201703044;
RA   Gagliardi P.A., Somale D., Puliafito A., Chiaverina G., di Blasio L.,
RA   Oneto M., Bianchini P., Bussolino F., Primo L.;
RT   "MRCKalpha is activated by caspase cleavage to assemble an apical actin
RT   ring for epithelial cell extrusion.";
RL   J. Cell Biol. 217:231-249(2018).
RN   [22]
RP   VARIANTS [LARGE SCALE ANALYSIS] LYS-50; MET-231; THR-537; MET-780; CYS-790;
RP   THR-1148; HIS-1211; ILE-1317; LYS-1418; VAL-1469 AND ALA-1618.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA   Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA   Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA   Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA   Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA   Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA   Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA   Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA   Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA   Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA   Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA   Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
CC   -!- FUNCTION: Serine/threonine-protein kinase which is an important
CC       downstream effector of CDC42 and plays a role in the regulation of
CC       cytoskeleton reorganization and cell migration (PubMed:15723050,
CC       PubMed:9418861, PubMed:9092543). Regulates actin cytoskeletal
CC       reorganization via phosphorylation of PPP1R12C and MYL9/MLC2
CC       (PubMed:21457715). In concert with MYO18A and LURAP1, is involved in
CC       modulating lamellar actomyosin retrograde flow that is crucial to cell
CC       protrusion and migration (PubMed:18854160). Phosphorylates: PPP1R12A,
CC       LIMK1 and LIMK2 (PubMed:11340065, PubMed:11399775). May play a role in
CC       TFRC-mediated iron uptake (PubMed:20188707). In concert with
CC       FAM89B/LRAP25 mediates the targeting of LIMK1 to the lamellipodium
CC       resulting in its activation and subsequent phosphorylation of CFL1
CC       which is important for lamellipodial F-actin regulation (By
CC       similarity). Triggers the formation of an extrusion apical actin ring
CC       required for epithelial extrusion of apoptotic cells (PubMed:29162624).
CC       {ECO:0000250|UniProtKB:Q3UU96, ECO:0000269|PubMed:11340065,
CC       ECO:0000269|PubMed:11399775, ECO:0000269|PubMed:15723050,
CC       ECO:0000269|PubMed:18854160, ECO:0000269|PubMed:20188707,
CC       ECO:0000269|PubMed:21457715, ECO:0000269|PubMed:29162624,
CC       ECO:0000269|PubMed:9092543, ECO:0000269|PubMed:9418861}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000269|PubMed:9092543};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000269|PubMed:29162624,
CC         ECO:0000269|PubMed:9092543};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:9092543};
CC   -!- ACTIVITY REGULATION: Maintained in an inactive, closed conformation by
CC       an interaction between the kinase domain and the negative
CC       autoregulatory C-terminal coiled-coil region. Agonist binding to the
CC       phorbol ester binding site disrupts this, releasing the kinase domain
CC       to allow N-terminus-mediated dimerization and kinase activation by
CC       transautophosphorylation. Inhibited by chelerythrine chloride.
CC       {ECO:0000269|PubMed:11283256, ECO:0000269|PubMed:21457715}.
CC   -!- SUBUNIT: Homodimer and homotetramer via the coiled coil regions
CC       (PubMed:11283256). Interacts tightly with GTP-bound but not GDP-bound
CC       CDC42 (PubMed:9418861). Forms a tripartite complex with MYO18A and
CC       LURAP1 with the latter acting as an adapter connecting CDC42BPA and
CC       MYO18A. LURAP1 binding results in activation of CDC42BPA by abolition
CC       of its negative autoregulation (PubMed:18854160). Interacts with
CC       LURAP1. Interacts (via AGC-kinase C-terminal domain) with FAM89B/LRAP25
CC       (via LRR repeat). Forms a tripartite complex with FAM89B/LRAP25 and
CC       LIMK1 (By similarity). {ECO:0000250|UniProtKB:Q3UU96,
CC       ECO:0000269|PubMed:11283256, ECO:0000269|PubMed:18854160,
CC       ECO:0000269|PubMed:9418861}.
CC   -!- INTERACTION:
CC       Q5VT25; P60953: CDC42; NbExp=5; IntAct=EBI-689171, EBI-81752;
CC       Q5VT25; Q5VT25: CDC42BPA; NbExp=9; IntAct=EBI-689171, EBI-689171;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O54874}. Cell
CC       projection, lamellipodium {ECO:0000250|UniProtKB:Q3UU96}. Note=Displays
CC       a dispersed punctate distribution and concentrates along the cell
CC       periphery, especially at the leading edge and cell-cell junction. This
CC       concentration is PH-domain dependent. Localizes in the lamellipodium in
CC       a FAM89B/LRAP25-dependent manner. {ECO:0000250|UniProtKB:O54874,
CC       ECO:0000250|UniProtKB:Q3UU96}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC         Comment=Additional isoforms seem to exist. They arise due to a two
CC         alternate splice sites, the first site involves splicing of exons
CC         21-24 while the second site involves exons 36-40.;
CC       Name=1 {ECO:0000305};
CC         IsoId=Q5VT25-1; Sequence=Displayed;
CC       Name=2 {ECO:0000305};
CC         IsoId=Q5VT25-2; Sequence=VSP_051861, VSP_051863;
CC       Name=3 {ECO:0000269|PubMed:15723050};
CC         IsoId=Q5VT25-3; Sequence=VSP_051859, VSP_051860;
CC       Name=4 {ECO:0000269|PubMed:16710414};
CC         IsoId=Q5VT25-4; Sequence=VSP_051862;
CC       Name=5 {ECO:0000269|PubMed:15723050};
CC         IsoId=Q5VT25-5; Sequence=VSP_051860;
CC       Name=6;
CC         IsoId=Q5VT25-6; Sequence=VSP_051860, VSP_035286;
CC   -!- TISSUE SPECIFICITY: Abundant in the heart, brain, skeletal muscle,
CC       kidney, and pancreas, with little or no expression in the lung and
CC       liver. {ECO:0000269|PubMed:9092543}.
CC   -!- INDUCTION: Regulated by cellular iron levels.
CC       {ECO:0000269|PubMed:20188707}.
CC   -!- PTM: Proteolytically cleaved by caspases upon apoptosis induction. The
CC       cleavage at Asp-478 by CASP3 increases its kinase activity (in vitro).
CC       {ECO:0000269|PubMed:29162624}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. DMPK subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD92205.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ518975; CAD57745.1; -; mRNA.
DR   EMBL; AJ518976; CAD57746.1; -; mRNA.
DR   EMBL; AB208968; BAD92205.1; ALT_INIT; mRNA.
DR   EMBL; CR933723; CAI46252.1; -; mRNA.
DR   EMBL; AL353689; CAI19113.1; -; Genomic_DNA.
DR   EMBL; AL451047; CAH71184.1; -; Genomic_DNA.
DR   EMBL; AL353689; CAH71184.1; JOINED; Genomic_DNA.
DR   EMBL; AL627308; CAH71184.1; JOINED; Genomic_DNA.
DR   EMBL; AL451047; CAH71185.1; -; Genomic_DNA.
DR   EMBL; AL627308; CAH71185.1; JOINED; Genomic_DNA.
DR   EMBL; AL353689; CAH71185.1; JOINED; Genomic_DNA.
DR   EMBL; AL627308; CAH71336.1; -; Genomic_DNA.
DR   EMBL; AL353689; CAH71336.1; JOINED; Genomic_DNA.
DR   EMBL; AL451047; CAH71336.1; JOINED; Genomic_DNA.
DR   EMBL; AL627308; CAH71337.1; -; Genomic_DNA.
DR   EMBL; AL353689; CAH71337.1; JOINED; Genomic_DNA.
DR   EMBL; AL451047; CAH71337.1; JOINED; Genomic_DNA.
DR   EMBL; AL353689; CAI19108.1; -; Genomic_DNA.
DR   EMBL; AL451047; CAI19108.1; JOINED; Genomic_DNA.
DR   EMBL; AL627308; CAI19108.1; JOINED; Genomic_DNA.
DR   EMBL; AL451047; CAH71183.1; -; Genomic_DNA.
DR   EMBL; AL353689; CAH71183.1; JOINED; Genomic_DNA.
DR   EMBL; AL627308; CAH71183.1; JOINED; Genomic_DNA.
DR   EMBL; AL627308; CAH71338.1; -; Genomic_DNA.
DR   EMBL; AL353689; CAH71338.1; JOINED; Genomic_DNA.
DR   EMBL; AL451047; CAH71338.1; JOINED; Genomic_DNA.
DR   EMBL; AL353689; CAI19109.1; -; Genomic_DNA.
DR   EMBL; AL627308; CAI19109.1; JOINED; Genomic_DNA.
DR   EMBL; AL451047; CAI19109.1; JOINED; Genomic_DNA.
DR   EMBL; AL353689; CAI19110.1; -; Genomic_DNA.
DR   EMBL; AL451047; CAI19110.1; JOINED; Genomic_DNA.
DR   EMBL; AL627308; CAI19110.1; JOINED; Genomic_DNA.
DR   EMBL; AB007920; BAA32296.2; -; mRNA.
DR   EMBL; U59305; AAB37126.1; -; mRNA.
DR   CCDS; CCDS1558.1; -. [Q5VT25-5]
DR   CCDS; CCDS1559.1; -. [Q5VT25-3]
DR   RefSeq; NP_003598.2; NM_003607.3. [Q5VT25-5]
DR   RefSeq; NP_055641.3; NM_014826.4. [Q5VT25-3]
DR   RefSeq; XP_005273378.1; XM_005273321.3. [Q5VT25-6]
DR   RefSeq; XP_005273379.1; XM_005273322.3. [Q5VT25-2]
DR   RefSeq; XP_005273381.1; XM_005273324.3.
DR   AlphaFoldDB; Q5VT25; -.
DR   SMR; Q5VT25; -.
DR   BioGRID; 114051; 131.
DR   IntAct; Q5VT25; 43.
DR   MINT; Q5VT25; -.
DR   STRING; 9606.ENSP00000355731; -.
DR   BindingDB; Q5VT25; -.
DR   ChEMBL; CHEMBL4516; -.
DR   DrugCentral; Q5VT25; -.
DR   GuidetoPHARMACOLOGY; 1507; -.
DR   GlyGen; Q5VT25; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q5VT25; -.
DR   PhosphoSitePlus; Q5VT25; -.
DR   BioMuta; CDC42BPA; -.
DR   DMDM; 74746874; -.
DR   EPD; Q5VT25; -.
DR   jPOST; Q5VT25; -.
DR   MassIVE; Q5VT25; -.
DR   MaxQB; Q5VT25; -.
DR   PaxDb; Q5VT25; -.
DR   PeptideAtlas; Q5VT25; -.
DR   PRIDE; Q5VT25; -.
DR   ProteomicsDB; 65291; -. [Q5VT25-1]
DR   ProteomicsDB; 65292; -. [Q5VT25-2]
DR   ProteomicsDB; 65293; -. [Q5VT25-3]
DR   ProteomicsDB; 65294; -. [Q5VT25-4]
DR   ProteomicsDB; 65295; -. [Q5VT25-5]
DR   ProteomicsDB; 65296; -. [Q5VT25-6]
DR   Antibodypedia; 34655; 246 antibodies from 36 providers.
DR   DNASU; 8476; -.
DR   Ensembl; ENST00000334218.9; ENSP00000335341.6; ENSG00000143776.20. [Q5VT25-1]
DR   Ensembl; ENST00000366766.8; ENSP00000355728.5; ENSG00000143776.20. [Q5VT25-2]
DR   Ensembl; ENST00000366767.7; ENSP00000355729.3; ENSG00000143776.20. [Q5VT25-3]
DR   Ensembl; ENST00000366769.7; ENSP00000355731.3; ENSG00000143776.20. [Q5VT25-5]
DR   GeneID; 8476; -.
DR   KEGG; hsa:8476; -.
DR   MANE-Select; ENST00000366766.8; ENSP00000355728.5; NM_001394014.1; NP_001380943.1. [Q5VT25-2]
DR   UCSC; uc001hqr.4; human. [Q5VT25-1]
DR   CTD; 8476; -.
DR   DisGeNET; 8476; -.
DR   GeneCards; CDC42BPA; -.
DR   HGNC; HGNC:1737; CDC42BPA.
DR   HPA; ENSG00000143776; Low tissue specificity.
DR   MIM; 603412; gene.
DR   neXtProt; NX_Q5VT25; -.
DR   OpenTargets; ENSG00000143776; -.
DR   PharmGKB; PA26267; -.
DR   VEuPathDB; HostDB:ENSG00000143776; -.
DR   eggNOG; KOG0612; Eukaryota.
DR   GeneTree; ENSGT01030000234517; -.
DR   HOGENOM; CLU_000288_140_3_1; -.
DR   InParanoid; Q5VT25; -.
DR   OMA; EFTIGYM; -.
DR   OrthoDB; 759391at2759; -.
DR   PhylomeDB; Q5VT25; -.
DR   TreeFam; TF313551; -.
DR   PathwayCommons; Q5VT25; -.
DR   Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR   Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR   Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR   Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR   SignaLink; Q5VT25; -.
DR   SIGNOR; Q5VT25; -.
DR   BioGRID-ORCS; 8476; 5 hits in 1114 CRISPR screens.
DR   ChiTaRS; CDC42BPA; human.
DR   GeneWiki; CDC42BPA; -.
DR   GenomeRNAi; 8476; -.
DR   Pharos; Q5VT25; Tchem.
DR   PRO; PR:Q5VT25; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q5VT25; protein.
DR   Bgee; ENSG00000143776; Expressed in medial globus pallidus and 209 other tissues.
DR   ExpressionAtlas; Q5VT25; baseline and differential.
DR   Genevisible; Q5VT25; HS.
DR   GO; GO:0042641; C:actomyosin; IDA:UniProtKB.
DR   GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR   GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:UniProtKB.
DR   GO; GO:0031032; P:actomyosin structure organization; IMP:UniProtKB.
DR   GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   CDD; cd00029; C1; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR001180; CNH_dom.
DR   InterPro; IPR000095; CRIB_dom.
DR   InterPro; IPR031597; KELK.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR014930; Myotonic_dystrophy_kinase_coil.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR026611; Ser/Thr_kinase_MRCK_alpha.
DR   PANTHER; PTHR22988:SF31; PTHR22988:SF31; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF08826; DMPK_coil; 1.
DR   Pfam; PF15796; KELK; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00285; PBD; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   SUPFAM; SSF57889; SSF57889; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell projection; Coiled coil; Cytoplasm;
KW   Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..1732
FT                   /note="Serine/threonine-protein kinase MRCK alpha"
FT                   /id="PRO_0000086392"
FT   DOMAIN          77..343
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000269|PubMed:9092543"
FT   DOMAIN          344..414
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   DOMAIN          1082..1201
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          1227..1499
FT                   /note="CNH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT   DOMAIN          1571..1584
FT                   /note="CRIB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT   ZN_FING         1012..1062
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   REGION          968..1003
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1591..1732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          437..820
FT                   /evidence="ECO:0000255"
FT   COILED          880..943
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        968..992
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1602..1649
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1657..1676
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1695..1732
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        201
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P54265,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT                   ProRule:PRU10027"
FT   BINDING         83..91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P54265,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         106
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000269|PubMed:11283256"
FT   SITE            478..479
FT                   /note="Cleavage; by CASP3 in vitro"
FT                   /evidence="ECO:0000269|PubMed:29162624"
FT   SITE            984..985
FT                   /note="Cleavage; by CASP3 in vitro"
FT                   /evidence="ECO:0000269|PubMed:29162624"
FT   MOD_RES         222
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:11283256"
FT   MOD_RES         234
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:11283256"
FT   MOD_RES         240
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:11283256"
FT   MOD_RES         1127
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O54874"
FT   MOD_RES         1545
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1611
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1613
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1629
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1651
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1664
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1669
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         1693
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         1719
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1721
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         550..630
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15723050"
FT                   /id="VSP_051859"
FT   VAR_SEQ         969..1009
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16710414, ECO:0000303|Ref.2"
FT                   /id="VSP_051862"
FT   VAR_SEQ         969..981
FT                   /note="Missing (in isoform 3, isoform 5 and isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:15723050,
FT                   ECO:0000303|PubMed:9455484"
FT                   /id="VSP_051860"
FT   VAR_SEQ         969
FT                   /note="R -> TDPVENTYVWNPSVKFHIQSRST (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_051861"
FT   VAR_SEQ         973..981
FT                   /note="CTPASKGRR -> TSSEAEPVK (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_051863"
FT   VAR_SEQ         1597
FT                   /note="M -> MPGFPYPSPHHHSGLISSPINFEHIYHMTVNSAEKFLSPDSINPEYS
FT                   PSLRSVPGTPSFMTLR (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:9455484"
FT                   /id="VSP_035286"
FT   VARIANT         50
FT                   /note="E -> K (in a lung neuroendocrine carcinoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040830"
FT   VARIANT         231
FT                   /note="T -> M (in dbSNP:rs34614709)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040831"
FT   VARIANT         537
FT                   /note="I -> T (in dbSNP:rs56364976)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040832"
FT   VARIANT         780
FT                   /note="T -> M (in dbSNP:rs56119119)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_045583"
FT   VARIANT         790
FT                   /note="Y -> C (in dbSNP:rs34943764)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_045584"
FT   VARIANT         1148
FT                   /note="A -> T (in dbSNP:rs56219089)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_045585"
FT   VARIANT         1211
FT                   /note="R -> H (in dbSNP:rs961490)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_045586"
FT   VARIANT         1317
FT                   /note="V -> I (in dbSNP:rs1929860)"
FT                   /evidence="ECO:0000269|PubMed:17344846,
FT                   ECO:0000269|PubMed:17974005"
FT                   /id="VAR_045587"
FT   VARIANT         1418
FT                   /note="I -> K"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040833"
FT   VARIANT         1469
FT                   /note="A -> V (in dbSNP:rs55687355)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_045588"
FT   VARIANT         1618
FT                   /note="T -> A (in dbSNP:rs2297417)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_045589"
FT   VARIANT         1699
FT                   /note="A -> V (in dbSNP:rs2802269)"
FT                   /id="VAR_045590"
FT   VARIANT         1712
FT                   /note="A -> V (in dbSNP:rs2802269)"
FT                   /evidence="ECO:0000269|PubMed:17974005,
FT                   ECO:0000269|PubMed:9455484, ECO:0000269|Ref.2"
FT                   /id="VAR_057104"
FT   MUTAGEN         106
FT                   /note="K->A: Loss of kinase activity."
FT                   /evidence="ECO:0000269|PubMed:11283256"
FT   MUTAGEN         222
FT                   /note="S->L: Increase in autophosphorylation but not kinase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:11283256"
FT   MUTAGEN         234
FT                   /note="S->A: Loss of autophosphorylation and kinase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:11283256"
FT   MUTAGEN         240
FT                   /note="T->A: Loss of autophosphorylation and kinase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:11283256"
FT   MUTAGEN         403
FT                   /note="T->A: Loss of autophosphorylation and kinase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:11283256"
FT   MUTAGEN         478
FT                   /note="D->A: Prevents cleavage by CASP3, impairs the
FT                   increase of its kinase activity and impairs extrusion
FT                   apical actin ring assembly."
FT                   /evidence="ECO:0000269|PubMed:29162624"
FT   MUTAGEN         984
FT                   /note="D->A: Prevents cleavage by CASP3."
FT                   /evidence="ECO:0000269|PubMed:29162624"
FT   MUTAGEN         1579
FT                   /note="H->A: Loss of CDC42 binding; when associated with A-
FT                   1582."
FT                   /evidence="ECO:0000269|PubMed:9418861"
FT   MUTAGEN         1582
FT                   /note="H->A: Loss of CDC42 binding; when associated with A-
FT                   1579."
FT                   /evidence="ECO:0000269|PubMed:9418861"
FT   CONFLICT        25
FT                   /note="C -> Y (in Ref. 5; AAB37126)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        809
FT                   /note="D -> N (in Ref. 3; CAI46252)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1521
FT                   /note="L -> V (in Ref. 8)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1688
FT                   /note="G -> K (in Ref. 6; BAA32296)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1732 AA;  197307 MW;  48B10F81B5405A0A CRC64;
     MSGEVRLRQL EQFILDGPAQ TNGQCFSVET LLDILICLYD ECNNSPLRRE KNILEYLEWA
     KPFTSKVKQM RLHREDFEIL KVIGRGAFGE VAVVKLKNAD KVFAMKILNK WEMLKRAETA
     CFREERDVLV NGDNKWITTL HYAFQDDNNL YLVMDYYVGG DLLTLLSKFE DRLPEDMARF
     YLAEMVIAID SVHQLHYVHR DIKPDNILMD MNGHIRLADF GSCLKLMEDG TVQSSVAVGT
     PDYISPEILQ AMEDGKGRYG PECDWWSLGV CMYEMLYGET PFYAESLVET YGKIMNHKER
     FQFPAQVTDV SENAKDLIRR LICSREHRLG QNGIEDFKKH PFFSGIDWDN IRNCEAPYIP
     EVSSPTDTSN FDVDDDCLKN SETMPPPTHT AFSGHHLPFV GFTYTSSCVL SDRSCLRVTA
     GPTSLDLDVN VQRTLDNNLA TEAYERRIKR LEQEKLELSR KLQESTQTVQ ALQYSTVDGP
     LTASKDLEIK NLKEEIEKLR KQVTESSHLE QQLEEANAVR QELDDAFRQI KAYEKQIKTL
     QQEREDLNKE LVQASERLKN QSKELKDAHC QRKLAMQEFM EINERLTELH TQKQKLARHV
     RDKEEEVDLV MQKVESLRQE LRRTERAKKE LEVHTEALAA EASKDRKLRE QSEHYSKQLE
     NELEGLKQKQ ISYSPGVCSI EHQQEITKLK TDLEKKSIFY EEELSKREGI HANEIKNLKK
     ELHDSEGQQL ALNKEIMILK DKLEKTRRES QSEREEFESE FKQQYEREKV LLTEENKKLT
     SELDKLTTLY ENLSIHNQQL EEEVKDLADK KESVAHWEAQ ITEIIQWVSD EKDARGYLQA
     LASKMTEELE ALRNSSLGTR ATDMPWKMRR FAKLDMSARL ELQSALDAEI RAKQAIQEEL
     NKVKASNIIT ECKLKDSEKK NLELLSEIEQ LIKDTEELRS EKGIEHQDSQ HSFLAFLNTP
     TDALDQFERS PSCTPASKGR RTVDSTPLSV HTPTLRKKGC PGSTGFPPKR KTHQFFVKSF
     TTPTKCHQCT SLMVGLIRQG CSCEVCGFSC HITCVNKAPT TCPVPPEQTK GPLGIDPQKG
     IGTAYEGHVR IPKPAGVKKG WQRALAIVCD FKLFLYDIAE GKASQPSVVI SQVIDMRDEE
     FSVSSVLASD VIHASRKDIP CIFRVTASQL SASNNKCSIL MLADTENEKN KWVGVLSELH
     KILKKNKFRD RSVYVPKEAY DSTLPLIKTT QAAAIIDHER IALGNEEGLF VVHVTKDEII
     RVGDNKKIHQ IELIPNDQLV AVISGRNRHV RLFPMSALDG RETDFYKLSE TKGCQTVTSG
     KVRHGALTCL CVAMKRQVLC YELFQSKTRH RKFKEIQVPY NVQWMAIFSE QLCVGFQSGF
     LRYPLNGEGN PYSMLHSNDH TLSFIAHQPM DAICAVEISS KEYLLCFNSI GIYTDCQGRR
     SRQQELMWPA NPSSCCYNAP YLSVYSENAV DIFDVNSMEW IQTLPLKKVR PLNNEGSLNL
     LGLETIRLIY FKNKMAEGDE LVVPETSDNS RKQMVRNINN KRRYSFRVPE EERMQQRREM
     LRDPEMRNKL ISNPTNFNHI AHMGPGDGIQ ILKDLPMNPR PQESRTVFSG SVSIPSITKS
     RPEPGRSMSA SSGLSARSSA QNGSALKREF SGGSYSAKRQ PMPSPSEGSL SSGGMDQGSD
     APARDFDGED SDSPRHSTAS NSSNLSSPPS PASPRKTKSL SLESTDRGSW DP
 
 
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