KKCC1_HUMAN
ID KKCC1_HUMAN Reviewed; 505 AA.
AC Q8N5S9; Q9BQH3;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Calcium/calmodulin-dependent protein kinase kinase 1;
DE Short=CaM-KK 1;
DE Short=CaM-kinase kinase 1;
DE Short=CaMKK 1;
DE EC=2.7.11.17;
DE AltName: Full=CaM-kinase IV kinase;
DE AltName: Full=Calcium/calmodulin-dependent protein kinase kinase alpha;
DE Short=CaM-KK alpha;
DE Short=CaM-kinase kinase alpha;
DE Short=CaMKK alpha;
GN Name=CAMKK1; Synonyms=CAMKKA;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Harvey M., Carra S., Tascedda F., Barden N.;
RT "Characterization of human CaMKK alpha gene structure.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP GLY-375.
RC TISSUE=Brain;
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 [4]
RP FUNCTION IN PHOSPHORYLATION OF CAMK1D.
RX PubMed=12935886; DOI=10.1016/s0014-5793(03)00817-2;
RA Ishikawa Y., Tokumitsu H., Inuzuka H., Murata-Hori M., Hosoya H.,
RA Kobayashi R.;
RT "Identification and characterization of novel components of a
RT Ca2+/calmodulin-dependent protein kinase cascade in HeLa cells.";
RL FEBS Lett. 550:57-63(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, AND IDENTIFICATION BY
RP 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67 AND SER-458, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND IDENTIFICATION BY
RP 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 [11]
RP VARIANT [LARGE SCALE ANALYSIS] GLY-375.
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: Calcium/calmodulin-dependent protein kinase that belongs to a
CC proposed calcium-triggered signaling cascade involved in a number of
CC cellular processes. Phosphorylates CAMK1, CAMK1D, CAMK1G and CAMK4.
CC Involved in regulating cell apoptosis. Promotes cell survival by
CC phosphorylating AKT1/PKB that inhibits pro-apoptotic BAD/Bcl2-
CC antagonist of cell death. {ECO:0000269|PubMed:12935886}.
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 -!- 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;
CC -!- ACTIVITY REGULATION: Activated by Ca(2+)/calmodulin. Binding of
CC calmodulin may relieve intrasteric autoinhibition. Partially inhibited
CC upon phosphorylation by PRCAKA/PKA (By similarity). May be regulated
CC through phosphorylation by CAMK1 and CAMK4. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CAMK4 and calmodulin. {ECO:0000250}.
CC -!- INTERACTION:
CC Q8N5S9; Q04917: YWHAH; NbExp=6; IntAct=EBI-6424030, EBI-306940;
CC Q8N5S9-2; P21333-2: FLNA; NbExp=3; IntAct=EBI-25850646, EBI-9641086;
CC Q8N5S9-2; P04792: HSPB1; NbExp=3; IntAct=EBI-25850646, EBI-352682;
CC Q8N5S9-2; P42858: HTT; NbExp=9; IntAct=EBI-25850646, EBI-466029;
CC Q8N5S9-2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-25850646, EBI-10975473;
CC Q8N5S9-2; P07196: NEFL; NbExp=3; IntAct=EBI-25850646, EBI-475646;
CC Q8N5S9-2; Q99497: PARK7; NbExp=3; IntAct=EBI-25850646, EBI-1164361;
CC Q8N5S9-2; Q8N2W9: PIAS4; NbExp=3; IntAct=EBI-25850646, EBI-473160;
CC Q8N5S9-2; P60891: PRPS1; NbExp=3; IntAct=EBI-25850646, EBI-749195;
CC Q8N5S9-2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-25850646, EBI-396669;
CC Q8N5S9-2; P37840: SNCA; NbExp=3; IntAct=EBI-25850646, EBI-985879;
CC Q8N5S9-2; P00441: SOD1; NbExp=3; IntAct=EBI-25850646, EBI-990792;
CC Q8N5S9-2; O76024: WFS1; NbExp=3; IntAct=EBI-25850646, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=A, Variant 3;
CC IsoId=Q8N5S9-1; Sequence=Displayed;
CC Name=2; Synonyms=B, Variant 1;
CC IsoId=Q8N5S9-2; Sequence=VSP_012140, VSP_012141;
CC -!- DOMAIN: The autoinhibitory domain overlaps with the calmodulin binding
CC region and may be involved in intrasteric autoinhibition.
CC -!- DOMAIN: The RP domain (arginine/proline-rich) is involved in the
CC recognition of CAMKI and CAMK4 as substrates. {ECO:0000250}.
CC -!- PTM: Appears to be autophosphorylated in a Ca(2+)/calmodulin-dependent
CC manner. Phosphorylated at multiple sites by PRCAKA/PKA. Phosphorylation
CC of Ser-458 is blocked upon binding to Ca(2+)/calmodulin. In vitro,
CC phosphorylated by CAMK1 and CAMK4 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AF425232; AAN37386.1; -; mRNA.
DR EMBL; AF425301; AAN37387.1; -; mRNA.
DR EMBL; AL136576; CAB66511.1; -; mRNA.
DR EMBL; BC031647; AAH31647.1; -; mRNA.
DR EMBL; BC043487; AAH43487.1; -; mRNA.
DR CCDS; CCDS11038.1; -. [Q8N5S9-1]
DR CCDS; CCDS11039.1; -. [Q8N5S9-2]
DR RefSeq; NP_115670.1; NM_032294.2. [Q8N5S9-1]
DR RefSeq; NP_757343.2; NM_172206.1.
DR RefSeq; NP_757344.2; NM_172207.2. [Q8N5S9-2]
DR RefSeq; XP_016880709.1; XM_017025220.1. [Q8N5S9-1]
DR PDB; 6CCF; X-ray; 2.10 A; A/B=124-411.
DR PDB; 6CD6; X-ray; 2.20 A; A/B/C/D=124-411.
DR PDBsum; 6CCF; -.
DR PDBsum; 6CD6; -.
DR AlphaFoldDB; Q8N5S9; -.
DR SMR; Q8N5S9; -.
DR BioGRID; 123981; 32.
DR IntAct; Q8N5S9; 43.
DR MINT; Q8N5S9; -.
DR STRING; 9606.ENSP00000158166; -.
DR BindingDB; Q8N5S9; -.
DR ChEMBL; CHEMBL5256; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q8N5S9; -.
DR GuidetoPHARMACOLOGY; 1956; -.
DR GlyGen; Q8N5S9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N5S9; -.
DR PhosphoSitePlus; Q8N5S9; -.
DR BioMuta; CAMKK1; -.
DR DMDM; 56404620; -.
DR EPD; Q8N5S9; -.
DR jPOST; Q8N5S9; -.
DR MassIVE; Q8N5S9; -.
DR MaxQB; Q8N5S9; -.
DR PeptideAtlas; Q8N5S9; -.
DR PRIDE; Q8N5S9; -.
DR ProteomicsDB; 72092; -. [Q8N5S9-1]
DR ProteomicsDB; 72093; -. [Q8N5S9-2]
DR TopDownProteomics; Q8N5S9-2; -. [Q8N5S9-2]
DR Antibodypedia; 3968; 216 antibodies from 33 providers.
DR DNASU; 84254; -.
DR Ensembl; ENST00000158166.5; ENSP00000158166.5; ENSG00000004660.15. [Q8N5S9-2]
DR Ensembl; ENST00000348335.7; ENSP00000323118.3; ENSG00000004660.15. [Q8N5S9-1]
DR GeneID; 84254; -.
DR KEGG; hsa:84254; -.
DR MANE-Select; ENST00000348335.7; ENSP00000323118.3; NM_032294.3; NP_115670.1.
DR UCSC; uc002fwu.4; human. [Q8N5S9-1]
DR CTD; 84254; -.
DR DisGeNET; 84254; -.
DR GeneCards; CAMKK1; -.
DR HGNC; HGNC:1469; CAMKK1.
DR HPA; ENSG00000004660; Tissue enhanced (brain).
DR MIM; 611411; gene.
DR neXtProt; NX_Q8N5S9; -.
DR OpenTargets; ENSG00000004660; -.
DR PharmGKB; PA26051; -.
DR VEuPathDB; HostDB:ENSG00000004660; -.
DR eggNOG; KOG0585; Eukaryota.
DR GeneTree; ENSGT00940000154890; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q8N5S9; -.
DR OMA; MACGPCM; -.
DR OrthoDB; 1044255at2759; -.
DR PhylomeDB; Q8N5S9; -.
DR TreeFam; TF313013; -.
DR PathwayCommons; Q8N5S9; -.
DR Reactome; R-HSA-111932; CaMK IV-mediated phosphorylation of CREB.
DR Reactome; R-HSA-442729; CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde.
DR Reactome; R-HSA-9619229; Activation of RAC1 downstream of NMDARs.
DR SignaLink; Q8N5S9; -.
DR SIGNOR; Q8N5S9; -.
DR BioGRID-ORCS; 84254; 16 hits in 1112 CRISPR screens.
DR ChiTaRS; CAMKK1; human.
DR GeneWiki; CAMKK1; -.
DR GenomeRNAi; 84254; -.
DR Pharos; Q8N5S9; Tchem.
DR PRO; PR:Q8N5S9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8N5S9; protein.
DR Bgee; ENSG00000004660; Expressed in right frontal lobe and 143 other tissues.
DR ExpressionAtlas; Q8N5S9; baseline and differential.
DR Genevisible; Q8N5S9; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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; IBA:GO_Central.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Cytoplasm; Kinase; Methylation; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..505
FT /note="Calcium/calmodulin-dependent protein kinase kinase
FT 1"
FT /id="PRO_0000086141"
FT DOMAIN 128..409
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 26..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..189
FT /note="RP domain"
FT REGION 435..440
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250"
FT REGION 438..463
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 460..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 275
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 134..142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VBY2"
FT MOD_RES 78
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8VBY2"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VBY2"
FT MOD_RES 108
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P97756"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97756"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 228
FT /note="L -> LALQNQAQNIQLDSTNIAKPHSLLPSEQQDSGSTWAARS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_012140"
FT VAR_SEQ 483..505
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_012141"
FT VARIANT 375
FT /note="E -> G (in dbSNP:rs7214723)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17344846"
FT /id="VAR_020531"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:6CCF"
FT STRAND 138..147
FT /evidence="ECO:0007829|PDB:6CCF"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:6CCF"
FT STRAND 152..160
FT /evidence="ECO:0007829|PDB:6CCF"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:6CCF"
FT HELIX 195..205
FT /evidence="ECO:0007829|PDB:6CCF"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:6CCF"
FT STRAND 223..231
FT /evidence="ECO:0007829|PDB:6CCF"
FT HELIX 249..268
FT /evidence="ECO:0007829|PDB:6CCF"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:6CCF"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:6CCF"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:6CCF"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:6CCF"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:6CCF"
FT HELIX 331..348
FT /evidence="ECO:0007829|PDB:6CCF"
FT HELIX 358..367
FT /evidence="ECO:0007829|PDB:6CCF"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:6CCF"
FT HELIX 380..389
FT /evidence="ECO:0007829|PDB:6CCF"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:6CCF"
FT HELIX 400..405
FT /evidence="ECO:0007829|PDB:6CCF"
FT HELIX 407..410
FT /evidence="ECO:0007829|PDB:6CCF"
SQ SEQUENCE 505 AA; 55735 MW; 92A055D20E487C86 CRC64;
MEGGPAVCCQ DPRAELVERV AAIDVTHLEE ADGGPEPTRN GVDPPPRARA ASVIPGSTSR
LLPARPSLSA RKLSLQERPA GSYLEAQAGP YATGPASHIS PRAWRRPTIE SHHVAISDAE
DCVQLNQYKL QSEIGKGAYG VVRLAYNESE DRHYAMKVLS KKKLLKQYGF PRRPPPRGSQ
AAQGGPAKQL LPLERVYQEI AILKKLDHVN VVKLIEVLDD PAEDNLYLVF DLLRKGPVME
VPCDKPFSEE QARLYLRDVI LGLEYLHCQK IVHRDIKPSN LLLGDDGHVK IADFGVSNQF
EGNDAQLSST AGTPAFMAPE AISDSGQSFS GKALDVWATG VTLYCFVYGK CPFIDDFILA
LHRKIKNEPV VFPEEPEISE ELKDLILKML DKNPETRIGV PDIKLHPWVT KNGEEPLPSE
EEHCSVVEVT EEEVKNSVRL IPSWTTVILV KSMLRKRSFG NPFEPQARRE ERSMSAPGNL
LVKEGFGEGG KSPELPGVQE DEAAS
