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 27-MAR-2024, entry version 185. 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}; 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; 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 GlyGen; Q63450; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q63450; -. DR PhosphoSitePlus; Q63450; -. DR jPOST; Q63450; -. DR PaxDb; 10116-ENSRNOP00000033456; -. DR Ensembl; ENSRNOT00055013194; ENSRNOP00055010570; ENSRNOG00055007856. DR Ensembl; ENSRNOT00060023204; ENSRNOP00060018403; ENSRNOG00060013595. DR Ensembl; ENSRNOT00065047693; ENSRNOP00065039116; ENSRNOG00065027661. DR GeneID; 171503; -. DR KEGG; rno:171503; -. DR UCSC; RGD:629473; rat. DR AGR; RGD:629473; -. 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 OrthoDB; 1121238at2759; -. 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 cell types or tissues. 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:0035556; P:intracellular signal transduction; 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: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: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 CDD; cd14167; STKc_CaMKI_alpha; 1. DR DisProt; DP01958; -. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR24347:SF197; CALCIUM_CALMODULIN-DEPENDENT PROTEIN KINASE TYPE 1; 1. DR PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; Q63450; RN. 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 FT 263-AA-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 //