CDKL1_HUMAN
ID CDKL1_HUMAN Reviewed; 358 AA.
AC Q00532; J3KMW1; Q2M3A4; Q6QUA0; Q8WXQ5;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 6.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Cyclin-dependent kinase-like 1 {ECO:0000305};
DE EC=2.7.11.22;
DE AltName: Full=Protein kinase p42 KKIALRE;
DE AltName: Full=Serine/threonine-protein kinase KKIALRE {ECO:0000303|Ref.2};
GN Name=CDKL1 {ECO:0000312|HGNC:HGNC:1781};
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 1), AND VARIANT GLU-275.
RX PubMed=1639063; DOI=10.1002/j.1460-2075.1992.tb05360.x;
RA Meyerson M., Enders G.H., Wu C.-L., Su L.-K., Gorka C., Nelson C.,
RA Harlow E., Tsai L.-H.;
RT "A family of human cdc2-related protein kinases.";
RL EMBO J. 11:2909-2917(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Hu W.-X., Tang L.-J., Shi Y.-W.;
RT "The cloning of 2nd splicing version of human serine/threonine-protein
RT kinase KKIALRE (cyclin-dependent kinase like-1).";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS PRO-67;
RP GLU-275; VAL-330 AND ASN-342.
RG NIEHS SNPs program;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
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 [7]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=9000130;
RA Taglienti C.A., Wysk M., Davis R.J.;
RT "Molecular cloning of the epidermal growth factor-stimulated protein kinase
RT p56 KKIAMRE.";
RL Oncogene 13:2563-2574(1996).
RN [8] {ECO:0007744|PDB:4AGU}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-300 OF VARIANT GLU-275 IN
RP COMPLEX WITH SYNTHETIC INHIBITOR.
RX PubMed=29420175; DOI=10.1016/j.celrep.2017.12.083;
RA Canning P., Park K., Goncalves J., Li C., Howard C.J., Sharpe T.D.,
RA Holt L.J., Pelletier L., Bullock A.N., Leroux M.R.;
RT "CDKL Family Kinases Have Evolved Distinct Structural Features and Ciliary
RT Function.";
RL Cell Rep. 22:885-894(2018).
RN [9]
RP VARIANTS [LARGE SCALE ANALYSIS] GLU-275 AND VAL-330.
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 -!- 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=2.7.11.22;
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=2.7.11.22;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9000130}. Nucleus
CC {ECO:0000269|PubMed:9000130}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q00532-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q00532-2; Sequence=VSP_041239, VSP_041240, VSP_041241,
CC VSP_041242;
CC Name=3;
CC IsoId=Q00532-3; Sequence=VSP_059391, VSP_059392;
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, and to a lower extent
CC in ovary. {ECO:0000269|PubMed:9000130}.
CC -!- DOMAIN: The [NKR]KIAxRE motif seems to be a cyclin-binding region.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/cdkl1/";
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DR EMBL; X66358; CAA47002.1; -; mRNA.
DR EMBL; X66359; CAA47002.1; JOINED; mRNA.
DR EMBL; AF390028; AAL58838.1; -; mRNA.
DR EMBL; AY525548; AAS00095.1; -; Genomic_DNA.
DR EMBL; AL118556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK308732; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC104977; AAI04978.1; -; mRNA.
DR CCDS; CCDS73637.1; -. [Q00532-3]
DR PIR; S22745; S22745.
DR PIR; S23383; S23383.
DR RefSeq; NP_004187.2; NM_004196.4.
DR RefSeq; XP_005268214.1; XM_005268157.2.
DR RefSeq; XP_016877218.1; XM_017021729.1.
DR PDB; 4AGU; X-ray; 2.40 A; A/B/C=1-300.
DR PDBsum; 4AGU; -.
DR AlphaFoldDB; Q00532; -.
DR SMR; Q00532; -.
DR BioGRID; 114341; 16.
DR IntAct; Q00532; 22.
DR MINT; Q00532; -.
DR STRING; 9606.ENSP00000379176; -.
DR BindingDB; Q00532; -.
DR ChEMBL; CHEMBL5789; -.
DR DrugBank; DB12010; Fostamatinib.
DR GuidetoPHARMACOLOGY; 1982; -.
DR GlyGen; Q00532; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q00532; -.
DR PhosphoSitePlus; Q00532; -.
DR BioMuta; CDKL1; -.
DR DMDM; 229463050; -.
DR MassIVE; Q00532; -.
DR PaxDb; Q00532; -.
DR PeptideAtlas; Q00532; -.
DR PRIDE; Q00532; -.
DR ProteomicsDB; 57849; -. [Q00532-1]
DR ProteomicsDB; 57850; -. [Q00532-2]
DR Antibodypedia; 23644; 355 antibodies from 28 providers.
DR DNASU; 8814; -.
DR Ensembl; ENST00000395834.6; ENSP00000379176.2; ENSG00000100490.10.
DR GeneID; 8814; -.
DR KEGG; hsa:8814; -.
DR UCSC; uc001wxz.5; human. [Q00532-1]
DR UCSC; uc032bbp.2; human.
DR CTD; 8814; -.
DR DisGeNET; 8814; -.
DR GeneCards; CDKL1; -.
DR HGNC; HGNC:1781; CDKL1.
DR HPA; ENSG00000100490; Low tissue specificity.
DR MIM; 603441; gene.
DR neXtProt; NX_Q00532; -.
DR PharmGKB; PA26317; -.
DR VEuPathDB; HostDB:ENSG00000100490; -.
DR eggNOG; KOG0593; Eukaryota.
DR InParanoid; Q00532; -.
DR OrthoDB; 398098at2759; -.
DR PhylomeDB; Q00532; -.
DR TreeFam; TF101031; -.
DR BRENDA; 2.7.11.22; 2681.
DR PathwayCommons; Q00532; -.
DR SignaLink; Q00532; -.
DR BioGRID-ORCS; 8814; 8 hits in 1114 CRISPR screens.
DR ChiTaRS; CDKL1; human.
DR GenomeRNAi; 8814; -.
DR Pharos; Q00532; Tchem.
DR PRO; PR:Q00532; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q00532; protein.
DR Bgee; ENSG00000100490; Expressed in right uterine tube and 118 other tissues.
DR ExpressionAtlas; Q00532; baseline and differential.
DR Genevisible; Q00532; HS.
DR GO; GO:0035869; C:ciliary transition zone; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:1902017; P:regulation of cilium assembly; ISS:UniProtKB.
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; Cytoplasm; Kinase;
KW Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..358
FT /note="Cyclin-dependent kinase-like 1"
FT /id="PRO_0000085810"
FT DOMAIN 5..288
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 46..52
FT /note="[NKR]KIAxRE"
FT ACT_SITE 127
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 11..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 2
FT /note="M -> MELSTDTGWNQKSNFPPCDSRVSKEEAQLPFPTPSSYGADSSNQTYA
FT HKSQSEREQHKEVRAVLNHCSGLDGGEESGLCGTSTRIDAGTGNGTDDKVTDQHRHRRC
FT LQGTKGNNRGSEVWGLLLQGNVDRSGGAPSAGVLLRRRGYSCALHGLRKFANLAGLLSR
FT QQDSARGVSHHSRLKIHFKKIYSSMM (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_041239"
FT VAR_SEQ 57
FT /note="K -> KAPSPYAAEPSLCGMKMVRRGKKEFLPAVAEKVDAPSGVGGQGQDSV
FT TVGSLGRRSTYGRKQEKQVRQREGIIYCYVAVLLRIYYFDQGCVAREEEQFQELVFGPF
FT CHIGSYFTGHRTNVRPYILLLSRPSPFKTAAGTYEAGLVILECSYFLAEQEPYCPTQAL
FT QQPHPIIGPWALEGGGVESKEDRHPPPKEAPASCEGFLRSAVPKQAYTPFKTSPDKRLS
FT DCVATPPWAPPTPLIISSGVLVAICSMIDPVPEFHSEGLLAKATSGSAGILVWIFLCND
FT AFIYGKYILRSGVLWVRGLPGFKSEAAALCHKCYSSADPKREQQQDLLQRVKEQSFHSV
FT NGAQARHKGSPSPHQTQEPSWPHPVDPTPGHRWSCLPVPCRAPALLSPWVVDGTGCCGA
FT GGGSDRGGSAAQEPT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_041240"
FT VAR_SEQ 99..122
FT /note="VPEHLVKSITWQTLQAVNFCHKHN -> ICNIFVCTGRRLGEHTEALSKKKK
FT KGGGGPFLKLRAASCRITLFKNVGCGLETTGDLSLNSGGGAASRGVAAALRALVCGTEL
FT TSSDSPQR (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_041241"
FT VAR_SEQ 248..358
FT /note="EPLELKFPNISYPALGLLKGCLHMDPTQRLTCEQLLHHPYFENIREIEDLAK
FT EHNKPTRKTLRKSRKHHCFTETSKLQYLPQLTGSSILPALDNKKYYCDTKKLNYRFPNI
FT -> SLCLSVTLTEGGLLASGAVKRSQMGSSVSQATSWPHPDIVAETAELDDIAMARQTP
FT VMLRFNRQKEQEKYLSYGA (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_041242"
FT VAR_SEQ 268..276
FT /note="CLHMDPTQR -> RVPIASRTE (in isoform 3)"
FT /id="VSP_059391"
FT VAR_SEQ 277..358
FT /note="Missing (in isoform 3)"
FT /id="VSP_059392"
FT VARIANT 67
FT /note="L -> P (in dbSNP:rs11570814)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_020576"
FT VARIANT 275
FT /note="Q -> E (in dbSNP:rs7161563)"
FT /evidence="ECO:0000269|PubMed:1639063,
FT ECO:0000269|PubMed:17344846, ECO:0000269|PubMed:29420175,
FT ECO:0000269|Ref.3"
FT /id="VAR_020577"
FT VARIANT 330
FT /note="L -> V (in dbSNP:rs9323183)"
FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.3"
FT /id="VAR_020578"
FT VARIANT 342
FT /note="K -> N (in dbSNP:rs770928060)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_020579"
FT CONFLICT 153
FT /note="A -> T (in Ref. 1; CAA47002, 2; AAL58838, 3;
FT AAS00095, 6; AAI04978 and 5; AK308732)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="N -> D (in Ref. 1; CAA47002)"
FT /evidence="ECO:0000305"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:4AGU"
FT STRAND 15..24
FT /evidence="ECO:0007829|PDB:4AGU"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:4AGU"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:4AGU"
FT HELIX 43..58
FT /evidence="ECO:0007829|PDB:4AGU"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:4AGU"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:4AGU"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:4AGU"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:4AGU"
FT HELIX 101..120
FT /evidence="ECO:0007829|PDB:4AGU"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:4AGU"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:4AGU"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:4AGU"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:4AGU"
FT HELIX 171..175
FT /evidence="ECO:0007829|PDB:4AGU"
FT HELIX 183..198
FT /evidence="ECO:0007829|PDB:4AGU"
FT HELIX 208..219
FT /evidence="ECO:0007829|PDB:4AGU"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:4AGU"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:4AGU"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:4AGU"
FT HELIX 259..268
FT /evidence="ECO:0007829|PDB:4AGU"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:4AGU"
FT HELIX 279..283
FT /evidence="ECO:0007829|PDB:4AGU"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:4AGU"
SQ SEQUENCE 358 AA; 41803 MW; 83C14DC5935B0DBC CRC64;
MMEKYEKIGK IGEGSYGVVF KCRNRDTGQI VAIKKFLESE DDPVIKKIAL REIRMLKQLK
HPNLVNLLEV FRRKRRLHLV FEYCDHTVLH ELDRYQRGVP EHLVKSITWQ TLQAVNFCHK
HNCIHRDVKP ENILITKHSV IKLCDFGFAR LLAGPSDYYT DYVATRWYRS PELLVGDTQY
GPPVDVWAIG CVFAELLSGV PLWPGKSDVD QLYLIRKTLG DLIPRHQQVF STNQYFSGVK
IPDPEDMEPL ELKFPNISYP ALGLLKGCLH MDPTQRLTCE QLLHHPYFEN IREIEDLAKE
HNKPTRKTLR KSRKHHCFTE TSKLQYLPQL TGSSILPALD NKKYYCDTKK LNYRFPNI
