KCC1A_RAT
ID KCC1A_RAT Reviewed; 374 AA.
AC Q63450; Q63084;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Calcium/calmodulin-dependent protein kinase type 1;
DE EC=2.7.11.17 {ECO:0000269|PubMed:8631893, ECO:0000269|PubMed:8702851};
DE AltName: Full=CaM kinase I;
DE Short=CaM-KI;
DE AltName: Full=CaM kinase I alpha;
DE Short=CaMKI-alpha;
GN Name=Camk1;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8253780; DOI=10.1016/s0021-9258(19)74343-9;
RA Picciotto M.R., Czernik A.J., Nairn A.C.;
RT "Calcium/calmodulin-dependent protein kinase I. cDNA cloning and
RT identification of autophosphorylation site.";
RL J. Biol. Chem. 268:26512-26521(1993).
RN [2]
RP ERRATUM OF PUBMED:8253780.
RA Picciotto M.R., Czernik A.J., Nairn A.C.;
RL J. Biol. Chem. 270:10358-10358(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Lung;
RX PubMed=7948038; DOI=10.1016/0167-4889(94)90123-6;
RA Cho F.S., Phillips K.S., Bogucki B., Weaver T.E.;
RT "Characterization of a rat cDNA clone encoding calcium/calmodulin-dependent
RT protein kinase I.";
RL Biochim. Biophys. Acta 1224:156-160(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [5]
RP PROTEIN SEQUENCE OF 12-37; 158-167; 233-241 AND 285-295.
RX PubMed=8386178; DOI=10.1016/s0021-9258(18)52989-6;
RA Mochizuki H., Ito T., Hidaka H.;
RT "Purification and characterization of Ca2+/calmodulin-dependent protein
RT kinase V from rat cerebrum.";
RL J. Biol. Chem. 268:9143-9147(1993).
RN [6]
RP FUNCTION IN PHOSPHORYLATION OF CREB1.
RX PubMed=1646483; DOI=10.1126/science.1646483;
RA Sheng M., Thompson M.A., Greenberg M.E.;
RT "CREB: a Ca(2+)-regulated transcription factor phosphorylated by
RT calmodulin-dependent kinases.";
RL Science 252:1427-1430(1991).
RN [7]
RP SUBSTRATE RECOGNITION MOTIF.
RX PubMed=7698321; DOI=10.1016/0014-5793(95)00172-6;
RA Dale S., Wilson W.A., Edelman A.M., Hardie D.G.;
RT "Similar substrate recognition motifs for mammalian AMP-activated protein
RT kinase, higher plant HMG-CoA reductase kinase-A, yeast SNF1, and mammalian
RT calmodulin-dependent protein kinase I.";
RL FEBS Lett. 361:191-195(1995).
RN [8]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=7624832; DOI=10.1002/syn.890200111;
RA Picciotto M.R., Zoli M., Bertuzzi G., Nairn A.C.;
RT "Immunochemical localization of calcium/calmodulin-dependent protein kinase
RT I.";
RL Synapse 20:75-84(1995).
RN [9]
RP FUNCTION IN PHOSPHORYLATION OF ATF1 AND CREB1.
RX PubMed=8621702; DOI=10.1074/jbc.271.6.3066;
RA Sun P., Lou L., Maurer R.A.;
RT "Regulation of activating transcription factor-1 and the cAMP response
RT element-binding protein by Ca2+/calmodulin-dependent protein kinases type
RT I, II, and IV.";
RL J. Biol. Chem. 271:3066-3073(1996).
RN [10]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, PHOSPHORYLATION AT THR-177 BY
RP CAMKK1 AND CAMKK2, AND MUTAGENESIS OF THR-177.
RX PubMed=8631893; DOI=10.1074/jbc.271.18.10806;
RA Edelman A.M., Mitchelhill K.I., Selbert M.A., Anderson K.A., Hook S.S.,
RA Stapleton D., Goldstein E.G., Means A.R., Kemp B.E.;
RT "Multiple Ca(2+)-calmodulin-dependent protein kinase kinases from rat
RT brain. Purification, regulation by Ca(2+)-calmodulin, and partial amino
RT acid sequence.";
RL J. Biol. Chem. 271:10806-10810(1996).
RN [11]
RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=8702851; DOI=10.1074/jbc.271.34.20930;
RA Aletta J.M., Selbert M.A., Nairn A.C., Edelman A.M.;
RT "Activation of a calcium-calmodulin-dependent protein kinase I cascade in
RT PC12 cells.";
RL J. Biol. Chem. 271:20930-20934(1996).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=10936699; DOI=10.1016/s0304-3940(00)01347-1;
RA Ahmed B.Y., Yamaguchi F., Tsumura T., Gotoh T., Sugimoto K., Tai Y.,
RA Konishi R., Kobayashi R., Tokuda M.;
RT "Expression and subcellular localization of multifunctional calmodulin-
RT dependent protein kinases-I, -II and -IV are altered in rat hippocampal CA1
RT neurons after induction of long-term potentiation.";
RL Neurosci. Lett. 290:149-153(2000).
RN [13]
RP SUBCELLULAR LOCATION, AND FUNCTION IN PHOSPHORYLATION OF MYL9.
RX PubMed=12081505; DOI=10.1042/bj20020536;
RA Suizu F., Fukuta Y., Ueda K., Iwasaki T., Tokumitsu H., Hosoya H.;
RT "Characterization of Ca2+/calmodulin-dependent protein kinase I as a myosin
RT II regulatory light chain kinase in vitro and in vivo.";
RL Biochem. J. 367:335-345(2002).
RN [14]
RP SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNAL, MUTAGENESIS OF
RP 319-LEU--LEU-321 AND 263-LYS-ARG-264, AND INTERACTION WITH XPO1.
RX PubMed=15147908; DOI=10.1016/j.febslet.2004.04.042;
RA Stedman D.R., Uboha N.V., Stedman T.T., Nairn A.C., Picciotto M.R.;
RT "Cytoplasmic localization of calcium/calmodulin-dependent protein kinase I-
RT alpha depends on a nuclear export signal in its regulatory domain.";
RL FEBS Lett. 566:275-280(2004).
RN [15]
RP FUNCTION IN AXONAL OUTGROWTH.
RX PubMed=15084659; DOI=10.1523/jneurosci.3294-03.2004;
RA Wayman G.A., Kaech S., Grant W.F., Davare M., Impey S., Tokumitsu H.,
RA Nozaki N., Banker G., Soderling T.R.;
RT "Regulation of axonal extension and growth cone motility by calmodulin-
RT dependent protein kinase I.";
RL J. Neurosci. 24:3786-3794(2004).
RN [16]
RP FUNCTION IN LONG-TERM POTENTIATION.
RX PubMed=15689566; DOI=10.1523/jneurosci.4086-04.2005;
RA Schmitt J.M., Guire E.S., Saneyoshi T., Soderling T.R.;
RT "Calmodulin-dependent kinase kinase/calmodulin kinase I activity gates
RT extracellular-regulated kinase-dependent long-term potentiation.";
RL J. Neurosci. 25:1281-1290(2005).
RN [17]
RP FUNCTION IN PHOSPHORYLATION OF NUMB.
RX PubMed=17022975; DOI=10.1016/j.febslet.2006.09.043;
RA Tokumitsu H., Hatano N., Yokokura S., Sueyoshi Y., Nozaki N., Kobayashi R.;
RT "Phosphorylation of Numb regulates its interaction with the clathrin-
RT associated adaptor AP-2.";
RL FEBS Lett. 580:5797-5801(2006).
RN [18]
RP FUNCTION IN DENDRITIC GROWTH.
RX PubMed=16772171; DOI=10.1016/j.neuron.2006.05.008;
RA Wayman G.A., Impey S., Marks D., Saneyoshi T., Grant W.F., Derkach V.,
RA Soderling T.R.;
RT "Activity-dependent dendritic arborization mediated by CaM-kinase I
RT activation and enhanced CREB-dependent transcription of Wnt-2.";
RL Neuron 50:897-909(2006).
RN [19]
RP FUNCTION IN MEDULLOBLASTOMA CELLS MIGRATION.
RX PubMed=21107644; DOI=10.1007/s11060-010-0472-6;
RA Davare M.A., Saneyoshi T., Soderling T.R.;
RT "Calmodulin-kinases regulate basal and estrogen stimulated medulloblastoma
RT migration via Rac1.";
RL J. Neurooncol. 104:65-82(2011).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RC TISSUE=Brain;
RX PubMed=8601311; DOI=10.1016/s0092-8674(00)81066-1;
RA Goldberg J., Nairn A.C., Kuriyan J.;
RT "Structural basis for the autoinhibition of calcium/calmodulin-dependent
RT protein kinase I.";
RL Cell 84:875-887(1996).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 294-318 IN COMPLEX WITH
RP CALMODULIN, AND DOMAIN.
RX PubMed=12475216; DOI=10.1021/bi026660t;
RA Clapperton J.A., Martin S.R., Smerdon S.J., Gamblin S.J., Bayley P.M.;
RT "Structure of the complex of calmodulin with the target sequence of
RT calmodulin-dependent protein kinase I: studies of the kinase activation
RT mechanism.";
RL Biochemistry 41:14669-14679(2002).
CC -!- FUNCTION: Calcium/calmodulin-dependent protein kinase that operates in
CC the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium
CC influx, regulates transcription activators activity, cell cycle,
CC hormone production, cell differentiation, actin filament organization
CC and neurite outgrowth. Recognizes the substrate consensus sequence
CC [MVLIF]-x-R-x(2)-[ST]-x(3)-[MVLIF]. Regulates axonal extension and
CC growth cone motility in hippocampal and cerebellar nerve cells. Upon
CC NMDA receptor-mediated Ca(2+) elevation, promotes dendritic growth in
CC hippocampal neurons and is essential in synapses for full long-term
CC potentiation (LTP) and ERK2-dependent translational activation.
CC Downstream of NMDA receptors, promotes the formation of spines and
CC synapses in hippocampal neurons by phosphorylating ARHGEF7/BETAPIX on
CC 'Ser-516', which results in the enhancement of ARHGEF7 activity and
CC activation of RAC1. Promotes neuronal differentiation and neurite
CC outgrowth by activation and phosphorylation of MARK2 on 'Ser-91', 'Ser-
CC 92', 'Ser-93' and 'Ser-294'. Promotes nuclear export of HDAC5 and
CC binding to 14-3-3 by phosphorylation of 'Ser-259' and 'Ser-498' in the
CC regulation of muscle cell differentiation (By similarity). Regulates
CC NUMB-mediated endocytosis by phosphorylation of NUMB on 'Ser-275' and
CC 'Ser-294'. Involved in the regulation of basal and estrogen-stimulated
CC migration of medulloblastoma cells through ARHGEF7/BETAPIX
CC phosphorylation (By similarity). Is required for proper activation of
CC cyclin-D1/CDK4 complex during G1 progression in diploid fibroblasts.
CC Plays a role in K(+) and ANG2-mediated regulation of the aldosterone
CC synthase (CYP11B2) to produce aldosterone in the adrenal cortex.
CC Phosphorylates EIF4G3/eIF4GII. In vitro phosphorylates CREB1, ATF1,
CC CFTR, MYL9 and SYN1/synapsin I. {ECO:0000250,
CC ECO:0000269|PubMed:12081505, ECO:0000269|PubMed:15084659,
CC ECO:0000269|PubMed:15689566, ECO:0000269|PubMed:1646483,
CC ECO:0000269|PubMed:16772171, ECO:0000269|PubMed:17022975,
CC ECO:0000269|PubMed:21107644, ECO:0000269|PubMed:8621702}.
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=2.7.11.17;
CC Evidence={ECO:0000269|PubMed:8631893, ECO:0000269|PubMed:8702851};
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=2.7.11.17; Evidence={ECO:0000269|PubMed:8631893,
CC ECO:0000269|PubMed:8702851};
CC -!- ACTIVITY REGULATION: Activated by Ca(2+)/calmodulin. Binding of
CC calmodulin results in conformational change that relieves intrasteric
CC autoinhibition and allows phosphorylation of Thr-177 within the
CC activation loop by CaMKK1 or CaMKK2. Phosphorylation of Thr-177 results
CC in several fold increase in total activity. Unlike CaMK4, is unable to
CC exhibit autonomous activity after Ca(2+)/calmodulin activation.
CC {ECO:0000269|PubMed:8631893, ECO:0000269|PubMed:8702851}.
CC -!- SUBUNIT: Monomer. Interacts with XPO1. {ECO:0000269|PubMed:12475216,
CC ECO:0000269|PubMed:15147908}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly
CC cytoplasmic.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:7624832}.
CC -!- DOMAIN: The autoinhibitory domain overlaps with the calmodulin binding
CC region and interacts in the inactive folded state with the catalytic
CC domain as a pseudosubstrate. {ECO:0000269|PubMed:12475216}.
CC -!- PTM: Phosphorylated by CaMKK1 and CaMKK2 on Thr-177.
CC {ECO:0000269|PubMed:8631893}.
CC -!- PTM: Polybiquitinated by the E3 ubiquitin-protein ligase complex
CC SCF(FBXL12), leading to proteasomal degradation. {ECO:0000250}.
CC -!- MISCELLANEOUS: Dendrite development is blocked in hippocampal neurons
CC silencing CAKM1.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA19670.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L24907; AAA19670.1; ALT_FRAME; mRNA.
DR EMBL; L26288; AAA66944.1; -; mRNA.
DR EMBL; BC071177; AAH71177.1; -; mRNA.
DR PIR; S50193; S50193.
DR RefSeq; NP_604463.1; NM_134468.1.
DR RefSeq; XP_006237065.1; XM_006237003.3.
DR PDB; 1A06; X-ray; 2.50 A; A=1-329.
DR PDB; 1MXE; X-ray; 1.70 A; E/F=294-318.
DR PDB; 2L7L; NMR; -; B=299-320.
DR PDBsum; 1A06; -.
DR PDBsum; 1MXE; -.
DR PDBsum; 2L7L; -.
DR AlphaFoldDB; Q63450; -.
DR BMRB; Q63450; -.
DR SMR; Q63450; -.
DR BioGRID; 251279; 4.
DR IntAct; Q63450; 5.
DR MINT; Q63450; -.
DR STRING; 10116.ENSRNOP00000033456; -.
DR iPTMnet; Q63450; -.
DR PhosphoSitePlus; Q63450; -.
DR jPOST; Q63450; -.
DR PaxDb; Q63450; -.
DR PRIDE; Q63450; -.
DR GeneID; 171503; -.
DR KEGG; rno:171503; -.
DR UCSC; RGD:629473; rat.
DR CTD; 8536; -.
DR RGD; 629473; Camk1.
DR VEuPathDB; HostDB:ENSRNOG00000021781; -.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q63450; -.
DR OMA; RPKVQPC; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q63450; -.
DR BRENDA; 2.7.11.17; 5301.
DR Reactome; R-RNO-9619229; Activation of RAC1 downstream of NMDARs.
DR EvolutionaryTrace; Q63450; -.
DR PRO; PR:Q63450; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000021781; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; Q63450; RN.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0006913; P:nucleocytoplasmic transport; ISO:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISS:UniProtKB.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:1901985; P:positive regulation of protein acetylation; ISO:RGD.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; ISO:RGD.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0051835; P:positive regulation of synapse structural plasticity; ISS:UniProtKB.
DR GO; GO:0060143; P:positive regulation of syncytium formation by plasma membrane fusion; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0051147; P:regulation of muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:0043393; P:regulation of protein binding; ISS:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB.
DR GO; GO:0050807; P:regulation of synapse organization; IDA:SynGO.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
DR DisProt; DP01958; -.
DR IDEAL; IID50054; -.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
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 3D-structure; Allosteric enzyme; ATP-binding; Calmodulin-binding;
KW Cell cycle; Cytoplasm; Developmental protein; Differentiation;
KW Direct protein sequencing; Isopeptide bond; Kinase; Neurogenesis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT CHAIN 1..374
FT /note="Calcium/calmodulin-dependent protein kinase type 1"
FT /id="PRO_0000086078"
FT DOMAIN 20..276
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 276..316
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000269|PubMed:8601311,
FT ECO:0007744|PDB:1A06"
FT REGION 296..317
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000269|PubMed:12475216,
FT ECO:0007744|PDB:1MXE, ECO:0007744|PDB:2L7L"
FT MOTIF 263..264
FT /note="Involved in nuclear import"
FT /evidence="ECO:0000305"
FT MOTIF 315..321
FT /note="Nuclear export signal"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT BINDING 26..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 177
FT /note="Phosphothreonine; by CaMKK1 and CaMKK2"
FT /evidence="ECO:0000269|PubMed:8631893"
FT CROSSLNK 59
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14012"
FT MUTAGEN 177
FT /note="T->A: Loss of activation by CaMKK1 and CaMKK2."
FT /evidence="ECO:0000269|PubMed:8631893"
FT MUTAGEN 263..264
FT /note="KR->AA: Partially excluded from the nucleus; when
FT associated with 319-AQA-321."
FT /evidence="ECO:0000269|PubMed:15147908"
FT MUTAGEN 319..321
FT /note="LQL->AQA: Retention in the nucleus. Partially
FT excluded from the nucleus; when associated with 263-AA-
FT 264."
FT /evidence="ECO:0000269|PubMed:15147908"
FT CONFLICT 37
FT /note="A -> T (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="F -> G (in Ref. 1; AAA19670)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="A -> R (in Ref. 1; AAA19670)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="S -> V (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="A -> R (in Ref. 1; AAA19670)"
FT /evidence="ECO:0000305"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:1A06"
FT STRAND 20..28
FT /evidence="ECO:0007829|PDB:1A06"
FT HELIX 29..33
FT /evidence="ECO:0007829|PDB:1A06"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:1A06"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:1A06"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:1A06"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:1A06"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1A06"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:1A06"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:1A06"
FT HELIX 115..134
FT /evidence="ECO:0007829|PDB:1A06"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1A06"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:1A06"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1A06"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:1A06"
FT HELIX 198..213
FT /evidence="ECO:0007829|PDB:1A06"
FT HELIX 223..231
FT /evidence="ECO:0007829|PDB:1A06"
FT TURN 239..244
FT /evidence="ECO:0007829|PDB:1A06"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:1A06"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:1A06"
FT HELIX 267..272
FT /evidence="ECO:0007829|PDB:1A06"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:1A06"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:1A06"
FT HELIX 287..297
FT /evidence="ECO:0007829|PDB:1A06"
FT HELIX 298..317
FT /evidence="ECO:0007829|PDB:1MXE"
SQ SEQUENCE 374 AA; 41638 MW; 37889B3DEF033AB2 CRC64;
MPGAVEGPRW KQAEDIRDIY DFRDVLGTGA FSEVILAEDK RTQKLVAIKC IAKKALEGKE
GSMENEIAVL HKIKHPNIVA LDDIYESGGH LYLIMQLVSG GELFDRIVEK GFYTERDASR
LIFQVLDAVK YLHDLGIVHR DLKPENLLYY SLDEDSKIMI SDFGLSKMED PGSVLSTACG
TPGYVAPEVL AQKPYSKAVD CWSIGVIAYI LLCGYPPFYD ENDAKLFEQI LKAEYEFDSP
YWDDISDSAK DFIRHLMEKD PEKRFTCEQA LQHPWIAGDT ALDKNIHQSV SEQIKKNFAK
SKWKQAFNAT AVVRHMRKLQ LGTSQEGQGQ TASHGELLTP TAGGPAAGCC CRDCCVEPGS
ELPPAPPPSS RAMD
