MELK_MOUSE
ID MELK_MOUSE Reviewed; 643 AA.
AC Q61846; Q3TPU1; Q61804; Q6ZQH6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Maternal embryonic leucine zipper kinase;
DE EC=2.7.11.1;
DE AltName: Full=Protein kinase PK38;
DE Short=mPK38;
DE AltName: Full=Tyrosine-protein kinase MELK;
DE EC=2.7.10.2;
GN Name=Melk; Synonyms=Kiaa0175, Pk38;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Keratinocyte;
RX PubMed=9305775; DOI=10.1016/s0378-1119(97)00181-9;
RA Gil M., Yang Y., Lee Y., Choi I., Ha H.;
RT "Cloning and expression of a cDNA encoding a novel protein serine/threonine
RT kinase predominantly expressed in hematopoietic cells.";
RL Gene 195:295-301(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6 X DBA/2;
RX PubMed=9136115;
RX DOI=10.1002/(sici)1098-2795(199706)47:2<148::aid-mrd4>3.0.co;2-m;
RA Heyer B.S., Warsowe J., Solter D., Knowles B.B., Ackerman S.L.;
RT "New member of the Snf1/AMPK kinase family, Melk, is expressed in the mouse
RT egg and preimplantation embryo.";
RL Mol. Reprod. Dev. 47:148-156(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16061694; DOI=10.1083/jcb.200412115;
RA Nakano I., Paucar A.A., Bajpai R., Dougherty J.D., Zewail A., Kelly T.K.,
RA Kim K.J., Ou J., Groszer M., Imura T., Freije W.A., Nelson S.F.,
RA Sofroniew M.V., Wu H., Liu X., Terskikh A.V., Geschwind D.H.,
RA Kornblum H.I.;
RT "Maternal embryonic leucine zipper kinase (MELK) regulates multipotent
RT neural progenitor proliferation.";
RL J. Cell Biol. 170:413-427(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP FUNCTION IN PHOSPHORYLATION OF MAP3K5, AND MUTAGENESIS OF LYS-40.
RX PubMed=18948261; DOI=10.1074/jbc.m807219200;
RA Jung H., Seong H.A., Ha H.;
RT "Murine protein serine/threonine kinase 38 activates apoptosis signal-
RT regulating kinase 1 via Thr 838 phosphorylation.";
RL J. Biol. Chem. 283:34541-34553(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in various processes
CC such as cell cycle regulation, self-renewal of stem cells, apoptosis
CC and splicing regulation. Has a broad substrate specificity;
CC phosphorylates BCL2L14, CDC25B, MAP3K5/ASK1 and ZNF622. Acts as an
CC activator of apoptosis by phosphorylating and activating MAP3K5/ASK1.
CC Acts as a regulator of cell cycle, notably by mediating phosphorylation
CC of CDC25B, promoting localization of CDC25B to the centrosome and the
CC spindle poles during mitosis. Plays a key role in cell proliferation.
CC Required for proliferation of embryonic and postnatal multipotent
CC neural progenitors. Phosphorylates and inhibits BCL2L14. Also involved
CC in the inhibition of spliceosome assembly during mitosis by
CC phosphorylating ZNF622, thereby contributing to its redirection to the
CC nucleus. May also play a role in primitive hematopoiesis.
CC {ECO:0000269|PubMed:16061694, ECO:0000269|PubMed:18948261}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
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 -!- ACTIVITY REGULATION: Activated by autophosphorylation of the T-loop at
CC Thr-167 and Ser-171: in contrast to other members of the SNF1
CC subfamily, phosphorylation at Thr-167 is not mediated by STK11/LKB1 but
CC via autophosphorylation instead. Inhibited by calcium-binding. Kinase
CC activity is also regulated by reducing agents: dithiothreitol (DTT) or
CC reduced glutathione are required for kinase activity in vitro; such
CC dependence is however not due to the presence of disulfide bonds (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Interacts with ZNF622 and PPP1R8 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in testis, ovary, thymus, spleen and T-
CC cell. Expressed by neural progenitors: highly enriched in cultures
CC containing multipotent progenitors. {ECO:0000269|PubMed:16061694,
CC ECO:0000269|PubMed:9136115, ECO:0000269|PubMed:9305775}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the 2-cell-stage embryo, followed by
CC a strong expression at 8-cell-stage. {ECO:0000269|PubMed:9136115}.
CC -!- DOMAIN: The KA1 domain mediates binding to phospholipids and targeting
CC to membranes. {ECO:0000250}.
CC -!- PTM: Autophosphorylated: autophosphorylation of the T-loop at Thr-167
CC and Ser-171 is required for activation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
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DR EMBL; L76158; AAB72030.1; -; mRNA.
DR EMBL; X95351; CAA64641.1; -; mRNA.
DR EMBL; AK011932; BAB27923.1; -; mRNA.
DR EMBL; AK145316; BAE26362.1; -; mRNA.
DR EMBL; AK164138; BAE37644.1; -; mRNA.
DR EMBL; AK129076; BAC97886.1; -; mRNA.
DR EMBL; AL805952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL807399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS18124.1; -.
DR RefSeq; NP_034920.2; NM_010790.2.
DR PDB; 4BFM; X-ray; 2.35 A; A=1-326.
DR PDB; 4CQG; X-ray; 2.57 A; A=1-326.
DR PDBsum; 4BFM; -.
DR PDBsum; 4CQG; -.
DR AlphaFoldDB; Q61846; -.
DR SMR; Q61846; -.
DR BioGRID; 201390; 11.
DR STRING; 10090.ENSMUSP00000043806; -.
DR iPTMnet; Q61846; -.
DR PhosphoSitePlus; Q61846; -.
DR EPD; Q61846; -.
DR jPOST; Q61846; -.
DR MaxQB; Q61846; -.
DR PaxDb; Q61846; -.
DR PRIDE; Q61846; -.
DR ProteomicsDB; 295853; -.
DR Antibodypedia; 2095; 472 antibodies from 40 providers.
DR DNASU; 17279; -.
DR Ensembl; ENSMUST00000045607; ENSMUSP00000043806; ENSMUSG00000035683.
DR GeneID; 17279; -.
DR KEGG; mmu:17279; -.
DR UCSC; uc008srv.1; mouse.
DR CTD; 9833; -.
DR MGI; MGI:106924; Melk.
DR VEuPathDB; HostDB:ENSMUSG00000035683; -.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00940000154889; -.
DR HOGENOM; CLU_000288_157_8_1; -.
DR InParanoid; Q61846; -.
DR OMA; LRAHYNV; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q61846; -.
DR TreeFam; TF314032; -.
DR BRENDA; 2.7.11.1; 3474.
DR BioGRID-ORCS; 17279; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Melk; mouse.
DR PRO; PR:Q61846; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q61846; protein.
DR Bgee; ENSMUSG00000035683; Expressed in primitive streak and 218 other tissues.
DR ExpressionAtlas; Q61846; baseline and differential.
DR Genevisible; Q61846; MM.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISS:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:0030097; P:hemopoiesis; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IDA:MGI.
DR GO; GO:0061351; P:neural precursor cell proliferation; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR CDD; cd14078; STKc_MELK; 1.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR001772; KA1_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR034673; MELK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF02149; KA1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF103243; SSF103243; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50032; KA1; 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; Apoptosis; ATP-binding; Calcium; Cell cycle; Cell membrane;
KW Kinase; Lipid-binding; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..643
FT /note="Maternal embryonic leucine zipper kinase"
FT /id="PRO_0000086324"
FT DOMAIN 11..263
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 594..643
FT /note="KA1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00565"
FT REGION 282..321
FT /note="UBA-like"
FT /evidence="ECO:0000250"
FT REGION 326..643
FT /note="Autoinhibitory region"
FT /evidence="ECO:0000250"
FT ACT_SITE 132
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 17..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 56
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q14680"
FT MOD_RES 163
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q14680"
FT MOD_RES 167
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q14680"
FT MOD_RES 171
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q14680"
FT MOD_RES 253
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q14680"
FT MOD_RES 336
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q14680"
FT MOD_RES 343
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q14680"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 399
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q14680"
FT MOD_RES 423
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q14680"
FT MOD_RES 486
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q14680"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14680"
FT MOD_RES 497
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q14680"
FT MOD_RES 510
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14680"
FT MOD_RES 521
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319"
FT MOD_RES 531
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q14680"
FT MUTAGEN 40
FT /note="K->R: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:18948261"
FT CONFLICT 335
FT /note="L -> P (in Ref. 2; CAA64641 and 4; BAC97886)"
FT /evidence="ECO:0000305"
FT HELIX 3..7
FT /evidence="ECO:0007829|PDB:4BFM"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:4BFM"
FT STRAND 11..19
FT /evidence="ECO:0007829|PDB:4BFM"
FT STRAND 21..30
FT /evidence="ECO:0007829|PDB:4BFM"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:4BFM"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:4BFM"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:4BFM"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:4BFM"
FT HELIX 52..62
FT /evidence="ECO:0007829|PDB:4BFM"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:4BFM"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:4BFM"
FT HELIX 94..101
FT /evidence="ECO:0007829|PDB:4BFM"
FT HELIX 106..125
FT /evidence="ECO:0007829|PDB:4BFM"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:4BFM"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:4BFM"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:4BFM"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:4BFM"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:4BFM"
FT HELIX 188..204
FT /evidence="ECO:0007829|PDB:4BFM"
FT HELIX 214..223
FT /evidence="ECO:0007829|PDB:4BFM"
FT HELIX 234..243
FT /evidence="ECO:0007829|PDB:4BFM"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:4BFM"
FT HELIX 254..258
FT /evidence="ECO:0007829|PDB:4BFM"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:4BFM"
FT HELIX 284..294
FT /evidence="ECO:0007829|PDB:4BFM"
FT HELIX 298..305
FT /evidence="ECO:0007829|PDB:4BFM"
FT HELIX 312..326
FT /evidence="ECO:0007829|PDB:4BFM"
SQ SEQUENCE 643 AA; 72729 MW; 5637D2A4E8CFA216 CRC64;
MKDYDELLKY YELYETIGTG GFAKVKLACH VLTGEMVAIK IMDKNALGSD LPRVKTEIDA
LKSLRHQHIC QLYHVLETKN KIFMVLEYCP GGELFDYIIS QDRLSEEETR VVFRQILSAV
AYVHSQGYAH RDLKPENLLF DENHKLKLID FGLCAKPKGN KDYHLQTCCG SLAYAAPELI
QGKSYLGSEA DVWSMGILLY VLMCGFLPFD DDNVMALYKK IMRGKYEVPK WLSPSSILLL
QQMLQVDPKK RISMRNLLNH PWVMQDYSCP VEWQSKTPLT HLDEDCVTEL SVHHRSSRQT
MEDLISSWQY DHLTATYLLL LAKKARGKPA RLQLLSFSCG TASTTPKSKN LSLEDMSTSD
DNCVAGLIDY ELCEDKLLAP KTPQVTKHLA ESNHAASKSP APGVRRAVAN KLMDKENVCT
PKSSVKNEEQ FVFSEPKIPV SKNQYKREIP ASPTRFPTPA KARAQCLREA PVRTPGNSAG
ADTLTTGVIS PERRCRSMDV DLNQAHMEDT PKKKGTNVFG SLERGLDKVL TALTRNKKKG
SARDGPRKRK LHYNVTTTRL VNPDQLLSEI MAILPKKNVD FVQKGYTLKC QTQSDFGKVT
MQFELEVCQL QRPDVVGIRR QRLKGDAWVY KRLVEDILSG CKM
