ROCK2_BOVIN
ID ROCK2_BOVIN Reviewed; 1388 AA.
AC Q28021;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Rho-associated protein kinase 2;
DE EC=2.7.11.1;
DE AltName: Full=Rho-associated, coiled-coil-containing protein kinase 2;
DE AltName: Full=Rho-associated, coiled-coil-containing protein kinase II;
DE Short=ROCK-II;
DE AltName: Full=p164 ROCK-2;
GN Name=ROCK2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 10-18; 30-44; 58-64;
RP 133-140; 248-252; 291-305; 327-348; 350-360; 366-384; 392-400; 506-511;
RP 527-535; 590-604; 633-652; 670-681; 829-842; 861-872; 913-921; 947-950;
RP 979-988; 1066-1070; 1087-1091; 1114-1120; 1131-1141; 1145-1151; 1158-1166;
RP 1182-1191; 1198-1218 AND 1318-1325, FUNCTION, INTERACTION WITH RHOA,
RP PHOSPHORYLATION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=8641286; DOI=10.1002/j.1460-2075.1996.tb00574.x;
RA Matsui T., Amano M., Yamamoto T., Chihara K., Nakafuku M., Ito M.,
RA Nakano T., Okawa K., Iwamatsu A., Kaibuchi K.;
RT "Rho-associated kinase, a novel serine/threonine kinase, as a putative
RT target for small GTP binding protein Rho.";
RL EMBO J. 15:2208-2216(1996).
RN [2]
RP FUNCTION.
RX PubMed=8702756; DOI=10.1074/jbc.271.34.20246;
RA Amano M., Ito M., Kimura K., Fukata Y., Chihara K., Nakano T., Matsuura Y.,
RA Kaibuchi K.;
RT "Phosphorylation and activation of myosin by Rho-associated kinase (Rho-
RT kinase).";
RL J. Biol. Chem. 271:20246-20249(1996).
RN [3]
RP FUNCTION.
RX PubMed=9565595; DOI=10.1074/jbc.273.19.11728;
RA Goto H., Kosako H., Tanabe K., Yanagida M., Sakurai M., Amano M.,
RA Kaibuchi K., Inagaki M.;
RT "Phosphorylation of vimentin by Rho-associated kinase at a unique amino-
RT terminal site that is specifically phosphorylated during cytokinesis.";
RL J. Biol. Chem. 273:11728-11736(1998).
RN [4]
RP FUNCTION.
RX PubMed=9456324; DOI=10.1083/jcb.140.3.647;
RA Matsui T., Maeda M., Doi Y., Yonemura S., Amano M., Kaibuchi K.,
RA Tsukita S., Tsukita S.;
RT "Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin
RT (ERM) proteins and regulates their head-to-tail association.";
RL J. Cell Biol. 140:647-657(1998).
RN [5]
RP FUNCTION.
RX PubMed=10209029; DOI=10.1083/jcb.145.2.347;
RA Fukata Y., Oshiro N., Kinoshita N., Kawano Y., Matsuoka Y., Bennett V.,
RA Matsuura Y., Kaibuchi K.;
RT "Phosphorylation of adducin by Rho-kinase plays a crucial role in cell
RT motility.";
RL J. Cell Biol. 145:347-361(1999).
RN [6]
RP FUNCTION.
RX PubMed=10873572; DOI=10.1006/bbrc.2000.2901;
RA Kaneko T., Amano M., Maeda A., Goto H., Takahashi K., Ito M., Kaibuchi K.;
RT "Identification of calponin as a novel substrate of Rho-kinase.";
RL Biochem. Biophys. Res. Commun. 273:110-116(2000).
RN [7]
RP FUNCTION.
RX PubMed=10818093; DOI=10.1074/jbc.m001032200;
RA Arimura N., Inagaki N., Chihara K., Menager C., Nakamura N., Amano M.,
RA Iwamatsu A., Goshima Y., Kaibuchi K.;
RT "Phosphorylation of collapsin response mediator protein-2 by Rho-kinase.
RT Evidence for two separate signaling pathways for growth cone collapse.";
RL J. Biol. Chem. 275:23973-23980(2000).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 979-1047 IN COMPLEX WITH RHOA, AND
RP HOMODIMERIZATION.
RX PubMed=12954645; DOI=10.1074/jbc.m306458200;
RA Shimizu T., Ihara K., Maesaki R., Amano M., Kaibuchi K., Hakoshima T.;
RT "Parallel coiled-coil association of the RhoA-binding domain in Rho-
RT kinase.";
RL J. Biol. Chem. 278:46046-46051(2003).
CC -!- FUNCTION: Protein kinase which is a key regulator of actin cytoskeleton
CC and cell polarity. Involved in regulation of smooth muscle contraction,
CC actin cytoskeleton organization, stress fiber and focal adhesion
CC formation, neurite retraction, cell adhesion and motility via
CC phosphorylation of ADD1, BRCA2, CNN1, EZR, DPYSL2, EP300, MSN,
CC MYL9/MLC2, NPM1, RDX, PPP1R12A and VIM. Phosphorylates SORL1 and IRF4.
CC Acts as a negative regulator of VEGF-induced angiogenic endothelial
CC cell activation. Positively regulates the activation of p42/MAPK1-
CC p44/MAPK3 and of p90RSK/RPS6KA1 during myogenic differentiation. Plays
CC an important role in the timely initiation of centrosome duplication.
CC Inhibits keratinocyte terminal differentiation. May regulate closure of
CC the eyelids and ventral body wall through organization of actomyosin
CC bundles. Plays a critical role in the regulation of spine and synaptic
CC properties in the hippocampus. Plays an important role in generating
CC the circadian rhythm of the aortic myofilament Ca(2+) sensitivity and
CC vascular contractility by modulating the myosin light chain
CC phosphorylation. {ECO:0000269|PubMed:10209029,
CC ECO:0000269|PubMed:10818093, ECO:0000269|PubMed:10873572,
CC ECO:0000269|PubMed:8641286, ECO:0000269|PubMed:8702756,
CC ECO:0000269|PubMed:9456324, ECO:0000269|PubMed:9565595}.
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 -!- 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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by RHOA binding. Inhibited by Y-27632.
CC -!- SUBUNIT: Homodimer (PubMed:12954645). Interacts with IRS1 (By
CC similarity). Interacts with RAF1 (By similarity). Interacts with RHOA
CC (activated by GTP) (PubMed:12954645). Interacts with RHOB and RHOC (By
CC similarity). Interacts with PPP1R12A (By similarity). Interacts with
CC EP300 (By similarity). Interacts with CHORDC1 (By similarity).
CC Interacts with BRCA2 (By similarity). Interacts with NPM1; this
CC interaction enhances ROCK2 activity (By similarity). Interacts with
CC SORL1 (By similarity). Interacts with PJVK (By similarity).
CC {ECO:0000250|UniProtKB:O75116, ECO:0000250|UniProtKB:P70336,
CC ECO:0000250|UniProtKB:Q62868, ECO:0000269|PubMed:12954645}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8641286}. Cell
CC membrane {ECO:0000269|PubMed:8641286}; Peripheral membrane protein
CC {ECO:0000269|PubMed:8641286}. Nucleus {ECO:0000250}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
CC Note=Cytoplasmic, and associated with actin microfilaments and the
CC plasma membrane.
CC -!- TISSUE SPECIFICITY: Highly expressed in whole brain and in cerebellum,
CC and at lower levels in heart and lung. Detected at low levels in
CC skeletal muscle, spleen, liver, kidney and pancreas.
CC {ECO:0000269|PubMed:8641286}.
CC -!- DOMAIN: An interaction between Thr-414 and Asp-48 is essential for
CC kinase activity and dimerization. {ECO:0000250}.
CC -!- PTM: Autophosphorylated. Phosphorylation at Tyr-722 reduces its binding
CC to RHOA and is crucial for focal adhesion dynamics. Dephosphorylation
CC by PTPN11 stimulates its RHOA binding activity (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Cleaved by granzyme B during apoptosis. This leads to constitutive
CC activation of the kinase and membrane blebbing (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U36909; AAC48567.1; -; mRNA.
DR PIR; S70633; S70633.
DR RefSeq; NP_776877.1; NM_174452.2.
DR PDB; 1UIX; X-ray; 1.80 A; A/B=979-1047.
DR PDB; 2F2U; X-ray; 2.40 A; A/B=18-417.
DR PDB; 2H9V; X-ray; 3.10 A; A=18-417.
DR PDBsum; 1UIX; -.
DR PDBsum; 2F2U; -.
DR PDBsum; 2H9V; -.
DR AlphaFoldDB; Q28021; -.
DR SMR; Q28021; -.
DR DIP; DIP-29038N; -.
DR IntAct; Q28021; 1.
DR MINT; Q28021; -.
DR STRING; 9913.ENSBTAP00000007691; -.
DR BindingDB; Q28021; -.
DR iPTMnet; Q28021; -.
DR PaxDb; Q28021; -.
DR PRIDE; Q28021; -.
DR GeneID; 282041; -.
DR KEGG; bta:282041; -.
DR CTD; 9475; -.
DR eggNOG; KOG0612; Eukaryota.
DR InParanoid; Q28021; -.
DR OrthoDB; 759391at2759; -.
DR EvolutionaryTrace; Q28021; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
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:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0072518; F:Rho-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:AgBase.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0048598; P:embryonic morphogenesis; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0010825; P:positive regulation of centrosome duplication; IEA:InterPro.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:1901888; P:regulation of cell junction assembly; IBA:GO_Central.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0006939; P:smooth muscle contraction; IEA:InterPro.
DR CDD; cd00029; C1; 1.
DR CDD; cd11638; HR1_ROCK2; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR020684; ROCK1/ROCK2.
DR InterPro; IPR037311; ROCK2_HR1.
DR InterPro; IPR015008; ROCK_Rho-bd_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08912; Rho_Binding; 1.
DR PIRSF; PIRSF037568; Rho_kinase; 1.
DR SMART; SM00109; C1; 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; 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; PS51860; REM_1; 1.
DR PROSITE; PS51859; RHO_BD; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Biological rhythms; Cell membrane; Coiled coil;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Kinase; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..1388
FT /note="Rho-associated protein kinase 2"
FT /id="PRO_0000086624"
FT DOMAIN 92..354
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 357..425
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 497..573
FT /note="REM-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 979..1047
FT /note="RhoBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01206"
FT DOMAIN 1150..1349
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 1260..1315
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..784
FT /note="Interaction with PPP1R12A"
FT /evidence="ECO:0000250"
FT REGION 373..420
FT /note="Interaction with NPM1"
FT /evidence="ECO:0000250"
FT REGION 512..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1047
FT /note="RHOA binding"
FT REGION 1345..1388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 439..1025
FT /evidence="ECO:0000255"
FT COILED 1053..1131
FT /evidence="ECO:0000255"
FT COMPBIAS 1363..1388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 214
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 98..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 1131..1132
FT /note="Cleavage; by granzyme B"
FT /evidence="ECO:0000250"
FT MOD_RES 414
FT /note="Phosphothreonine; by ROCK2"
FT /evidence="ECO:0000250|UniProtKB:Q62868"
FT MOD_RES 722
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:O75116"
FT MOD_RES 1137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75116"
FT MOD_RES 1212
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75116"
FT MOD_RES 1362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75116"
FT MOD_RES 1374
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75116"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:2F2U"
FT HELIX 43..57
FT /evidence="ECO:0007829|PDB:2F2U"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:2F2U"
FT HELIX 66..82
FT /evidence="ECO:0007829|PDB:2F2U"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2F2U"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2F2U"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:2F2U"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:2F2U"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:2F2U"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:2F2U"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:2F2U"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:2F2U"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:2F2U"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:2F2U"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:2F2U"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:2F2U"
FT HELIX 188..206
FT /evidence="ECO:0007829|PDB:2F2U"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:2F2U"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:2F2U"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:2F2U"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:2F2U"
FT STRAND 241..247
FT /evidence="ECO:0007829|PDB:2F2U"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:2F2U"
FT HELIX 259..263
FT /evidence="ECO:0007829|PDB:2F2U"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:2F2U"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:2F2U"
FT HELIX 274..289
FT /evidence="ECO:0007829|PDB:2F2U"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:2F2U"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:2F2U"
FT HELIX 323..332
FT /evidence="ECO:0007829|PDB:2F2U"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:2F2U"
FT TURN 340..343
FT /evidence="ECO:0007829|PDB:2F2U"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:2F2U"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:2F2U"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:2F2U"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:2F2U"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:2F2U"
FT HELIX 979..1043
FT /evidence="ECO:0007829|PDB:1UIX"
SQ SEQUENCE 1388 AA; 160800 MW; CA83CE7D3860465D CRC64;
MSRPPPTGKM PGAPEAVSGD GAGASRQRKL EALIRDPRSP INVESLLDGL NPLVLDLDFP
ALRKNKNIDN FLNRYEKIVK KIRGLQMKAE DYDVVKVIGR GAFGEVQLVR HKASQKVYAM
KLLSKFEMIK RSDSAFFWEE RDIMAFANSP WVVQLFCAFQ DDKYLYMVME YMPGGDLVNL
MSNYDVPEKW AKFYTAEVVL ALDAIHSMGL IHRDVKPDNM LLDKHGHLKL ADFGTCMKMD
ETGMVHCDTA VGTPDYISPE VLKSQGGDGY YGRECDWWSV GVFLFEMLVG DTPFYADSLV
GTYSKIMDHK NSLCFPEDAE ISKHAKNLIC AFLTDREVRL GRNGVEEIKQ HPFFKNDQWN
WDNIRETAAP VVPELSSDID SSNFDDIEDD KGDVETFPIP KAFVGNQLPF IGFTYYRENL
LLSDSPSCKE NDSIQSRKNE ESQEIQKKLY TLEEHLSTEI QAKEELEQKC KSVNTRLEKV
AKELEEEITL RKNVESTLRQ LEREKALLQH KNAEYQRKAD HEADKKRNLE NDVNSLKDQL
EDLKKRNQNS QISTEKVNQL QRQLDETNAL LRTESDTAAR LRKTQAESSK QIQQLESNNR
DLQDKNCLLE TAKLKLEKEF INLQSVLESE RRDRTHGSEI INDLQGRISG LEEDVKNGKI
LLAKVELEKR QLQERFTDLE KEKNNMEIDM TYQLKVIQQS LEQEETEHKA TKARLADKNK
IYESIEEAKS EAMKEMEKKL SEERTLKQKV ENLLLEAEKR CSILDCDLKQ SQQKINELLK
QKDVLNEDVR NLTLKIEQET QKRCLTQNDL KMQTQQVNTL KMSEKQLKQE NNHLLEMKMS
LEKQNAELRK ERQDADGQMK ELQDQLEAEQ YFSTLYKTQV RELKEECEEK TKLCKELQQK
KQELQDERDS LAAQLEITLT KADSEQLARS IAEEQYSDLE KEKIMKELEI KEMMARHKQE
LTEKDATIAS LEETNRTLTS DVANLANEKE ELNNKLKEAQ EQLSRLKDEE ISAAAIKAQF
EKQLLTERTL KTQAVNKLAE IMNRKEPVKR GNDTDVRRKE KENRKLHMEL KSEREKLTQQ
MIKYQKELNE MQAQIAEESQ IRIELQMTLD SKDSDIEQLR SQLQALHIGL DSSSIGSGPG
DTEADDGFPE SRLEGWLSLP VRNNTKKFGW VKKYVIVSSK KILFYDSEQD KEQSNPYMVL
DIDKLFHVRP VTQTDVYRAD AKEIPRIFQI LYANEGESKK EQEFPVEPVG EKSNYICHKG
HEFIPTLYHF PTNCEACMKP LWHMFKPPPA LECRRCHIKC HKDHMDKKEE IIAPCKVYYD
ISSAKNLLLL ANSTEEQQKW VSRLVKKIPK KPPAPDPFAR SSPRTSMKIQ QNQSIRRPSR
QLAPNKPS
