MRCKA_RAT
ID MRCKA_RAT Reviewed; 1732 AA.
AC O54874;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Serine/threonine-protein kinase MRCK alpha;
DE EC=2.7.11.1;
DE AltName: Full=CDC42-binding protein kinase 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:0000250|UniProtKB:Q5VT25};
GN Synonyms=Pk428 {ECO:0000312|RGD:621406};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC02941.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF LYS-106.
RC TISSUE=Brain {ECO:0000312|EMBL:AAC02941.1};
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 [2] {ECO:0000305}
RP OLIGOMERIZATION.
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 [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1127, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [5]
RP FUNCTION, AND INTERACTION WITH MYO18A AND LURAP1.
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1651 AND SER-1721, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [8]
RP INTERACTION WITH FAM89B AND LURAP1.
RC TISSUE=Brain;
RX PubMed=25107909; DOI=10.1074/jbc.m114.588079;
RA Lee I.C., Leung T., Tan I.;
RT "Adaptor protein LRAP25 mediates myotonic dystrophy kinase-related Cdc42-
RT binding kinase (MRCK) regulation of LIMK1 protein in lamellipodial F-actin
RT dynamics.";
RL J. Biol. Chem. 289:26989-27003(2014).
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:9418861).
CC Regulates actin cytoskeletal reorganization via phosphorylation of
CC PPP1R12A and MYL9/MLC2 (PubMed:21457715). In concert with MYO18A and
CC LURAP1, is involved in modulating lamellar actomyosin retrograde flow
CC that is crucial to cell protrusion and migration (PubMed:18854160).
CC Phosphorylates: PPP1R12C, LIMK1 and LIMK2. May play a role in TFRC-
CC mediated iron uptake. In concert with FAM89B/LRAP25 mediates the
CC targeting of LIMK1 to the lamellipodium resulting in its activation and
CC subsequent phosphorylation of CFL1 which is important for lamellipodial
CC F-actin regulation (By similarity). Triggers the formation of an
CC extrusion apical actin ring required for epithelial extrusion of
CC apoptotic cells (By similarity). {ECO:0000250|UniProtKB:Q3UU96,
CC ECO:0000250|UniProtKB:Q5VT25, ECO:0000269|PubMed:18854160,
CC ECO:0000269|PubMed:21457715, 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:9418861};
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:9418861};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9418861};
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 (By similarity). Inhibited by chelerythrine
CC chloride. {ECO:0000250, 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 (By similarity). 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 LURAP1
CC (PubMed:25107909). Interacts (via AGC-kinase C-terminal domain) with
CC FAM89B/LRAP25 (via LRR repeat) (PubMed:25107909). Forms a tripartite
CC complex with FAM89B/LRAP25 and LIMK1 (By similarity).
CC {ECO:0000250|UniProtKB:Q3UU96, ECO:0000250|UniProtKB:Q5VT25,
CC ECO:0000269|PubMed:11283256, ECO:0000269|PubMed:18854160,
CC ECO:0000269|PubMed:25107909}.
CC -!- INTERACTION:
CC O54874; O54874: Cdc42bpa; NbExp=2; IntAct=EBI-689253, EBI-689253;
CC O54874; D4A8G3: Lurap1; NbExp=8; IntAct=EBI-689253, EBI-2015467;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9418861}. 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 (PubMed:9418861). Localizes in the
CC lamellipodium in a FAM89B/LRAP25-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:Q3UU96, ECO:0000269|PubMed:9418861}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=O54874-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O54874-2; Sequence=Not described;
CC Name=3;
CC IsoId=O54874-3; Sequence=Not described;
CC Name=4;
CC IsoId=O54874-4; Sequence=Not described;
CC Name=5;
CC IsoId=O54874-5; Sequence=Not described;
CC Name=6;
CC IsoId=O54874-6; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Highly expressed in the brain and lung and present
CC in lower levels in all other tissues tested.
CC {ECO:0000269|PubMed:9418861}.
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:0000250|UniProtKB:Q5VT25}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. DMPK subfamily. {ECO:0000305}.
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DR EMBL; AF021935; AAC02941.1; -; mRNA.
DR PIR; T14039; T14039.
DR RefSeq; NP_446109.1; NM_053657.1. [O54874-1]
DR PDB; 4AW2; X-ray; 1.70 A; A=2-424.
DR PDBsum; 4AW2; -.
DR AlphaFoldDB; O54874; -.
DR SMR; O54874; -.
DR IntAct; O54874; 8.
DR MINT; O54874; -.
DR STRING; 10116.ENSRNOP00000003837; -.
DR CarbonylDB; O54874; -.
DR iPTMnet; O54874; -.
DR PhosphoSitePlus; O54874; -.
DR jPOST; O54874; -.
DR PaxDb; O54874; -.
DR PRIDE; O54874; -.
DR GeneID; 114116; -.
DR KEGG; rno:114116; -.
DR UCSC; RGD:621406; rat. [O54874-1]
DR CTD; 8476; -.
DR RGD; 621406; Cdc42bpa.
DR eggNOG; KOG0612; Eukaryota.
DR InParanoid; O54874; -.
DR OrthoDB; 759391at2759; -.
DR PhylomeDB; O54874; -.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR Reactome; R-RNO-9013409; RHOJ GTPase cycle.
DR PRO; PR:O54874; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0042641; C:actomyosin; IDA:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
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:UniProtKB.
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:0007010; P:cytoskeleton organization; IDA:RGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD.
DR GO; GO:0007097; P:nuclear migration; ISO:RGD.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; 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 3D-structure; Alternative splicing; ATP-binding; Cell projection;
KW Coiled coil; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1732
FT /note="Serine/threonine-protein kinase MRCK alpha"
FT /id="PRO_0000086393"
FT DOMAIN 77..343
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:9418861"
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 973..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1592..1732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 437..670
FT /evidence="ECO:0000255"
FT COILED 713..820
FT /evidence="ECO:0000255"
FT COILED 880..943
FT /evidence="ECO:0000255"
FT COMPBIAS 1602..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:9418861"
FT SITE 478..479
FT /note="Cleavage; by CASP3 in vitro"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT SITE 984..985
FT /note="Cleavage; by CASP3 in vitro"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 222
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 234
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 240
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 1127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 1545
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 1611
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 1613
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 1629
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 1651
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1664
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 1669
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 1693
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 1719
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25"
FT MOD_RES 1721
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MUTAGEN 106
FT /note="K->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:9418861"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:4AW2"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:4AW2"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:4AW2"
FT HELIX 28..43
FT /evidence="ECO:0007829|PDB:4AW2"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:4AW2"
FT HELIX 51..70
FT /evidence="ECO:0007829|PDB:4AW2"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:4AW2"
FT STRAND 77..85
FT /evidence="ECO:0007829|PDB:4AW2"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:4AW2"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:4AW2"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:4AW2"
FT HELIX 110..115
FT /evidence="ECO:0007829|PDB:4AW2"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:4AW2"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:4AW2"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:4AW2"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:4AW2"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:4AW2"
FT HELIX 162..167
FT /evidence="ECO:0007829|PDB:4AW2"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:4AW2"
FT HELIX 175..194
FT /evidence="ECO:0007829|PDB:4AW2"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:4AW2"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:4AW2"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:4AW2"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:4AW2"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:4AW2"
FT HELIX 262..277
FT /evidence="ECO:0007829|PDB:4AW2"
FT HELIX 287..295
FT /evidence="ECO:0007829|PDB:4AW2"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:4AW2"
FT HELIX 312..319
FT /evidence="ECO:0007829|PDB:4AW2"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:4AW2"
FT TURN 329..334
FT /evidence="ECO:0007829|PDB:4AW2"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:4AW2"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:4AW2"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:4AW2"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:4AW2"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:4AW2"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:4AW2"
SQ SEQUENCE 1732 AA; 197064 MW; 65F62F7872ACCD3B CRC64;
MSGEVRLRQL EQFILDGPAQ TNGQCFSVET LLDILICLYD ECNNSPLRRE KNILEYLEWA
KPFTSKVKQM RLHREDFEIL KVIGRGAFGE VAVVKLKNAD KVFAMKILNK WEMLKRAETA
CFREERDVLV NGDSKWITTL HYAFQDDNNL YLVMDYYVGG DLLTLLSKFE DRLPEEMARF
YLAEMVIAID SVHQLHYVHR DIKPDNILMD MNGHIRLADF GSCLKLMEDG TVQSSVAVGT
PDYISPEILQ AMEDGKGRYG PECDWWSLGV CMYEMLYGET PFYAESLVET YGKIMNHKER
FQFPTQVTDV SENAKDLIRR LICSREHRLG QNGIEDFKKH PFFSGIDWDN IRNCEAPYIP
EVSSPTDTSN FDVDDDCLKN SETMPPPTHT AFSGHHLPFV GFTYTSSCVL SDRSCLRVTA
GPTSLDLDVN VQRTLDNNLA TEAYERRIKR LEQEKLELTR KLQESTQTVQ ALQYSTVDGP
LTASKDLEIK SLKEEIEKLR KQVAEVNHLE QQLEEANSVR RELDDAFRQI KAFEKQIKTL
QQEREELNKE LVQASERLKN QSKELKDAHC QRKLAMQEFM EINERLTELH TQKQKLARHV
RDKEEEVDLV MQKAESLRQE LRRAERAKKE LEVHTEALIA EASKDRKLRE QSRHYSKQLE
NELEGLKQKQ ISYSPGICSI EHQQEITKLK TDLEKKSIFY EEEISKREGI HASEIKNLKK
ELHDSEGQQL ALNKEIMVLK DKLEKTRRES QSEREEFENE FKQQYEREKV LLTEENKKLT
SELDKLTSLY ESLSLRNQHL EEEVKDLADK KESVAHWEAQ ITEIIQWVSD EKDARGYLQA
LASKMTEELE ALRNSSLGTR ATDMPWKMRR FAKLDMSARL ELQSALDAEI RAKQAIQEEL
NKVKASNIIT ECKLKDSEKK NLELLSEIEQ LIKDTEELRS EKGVEHRDSQ HSFLAFLNTP
TDALDQFERS PSCTPAGKGR RIADSAPLPV HTPTLRKKGC PASAGFPPKR KTHQFFVKSF
TAPTKCHQCT SLMVGLIRQG CSCEVCGFSC HITCVNKAPT TCPVPPEQTK GPLGIDPQKG
VGTAYEGHVR IPKPAGVKKG WQRALAVVCD FKLFLYDIAE GKASQPSSVI SQVIDMRDEE
FSVSSVLASD VIHASRKDIP CIFRVTASQL SAPSDKCSIL MLADSETERS KWVGVLSELH
KVLKKNKFRD RSVYVPKEAY DSTLPLIKTT QAAAIIDHER VALGNEEGLF VVHVTKDEII
RVGDNKKIHQ IELIPSDQLV AVISGRNRHV RLFPMSALDG RETDFYKLAE TKGCQTIAAG
KVRHGALSCL CVAMKRQVLC YELFQSKTRH RKFKEIQVPC NVQWMAIFSE HLCVGFQSGF
LRYPLNGEGS PCNMLHSNDH TLAFITHQPM DAICAVEISN KEYLLCFSSI GIYTDCQGRR
SRQQELMWPA NPSSCCYNAP YLSIYSENAV DIFDVNSMEW IQTLPLKKVR PLNTEGSLNL
LGLETIRLIY FKNKMAEGDE LVVPETSDNS RKQMVRNINN KRRYSFRVPE EERMQQRREM
LRDPEMRNKL ISNPTNFNHI AHMGPGDGIQ ILKDLPMNPR PQESRTVFSG SVSIPSITKS
RPEPGRSMSA SSGLSARSSA QNGSALKREF SGGSYNTKRQ PMPSPSEGSL SSGGVDQGSD
APVRDYDGED SDSPRHSTAS NSSNLSSPPS PVSPRKTKSL SLESTDRGSW DP
