M4K2_HUMAN
ID M4K2_HUMAN Reviewed; 820 AA.
AC Q12851; Q86VU3;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase kinase 2;
DE EC=2.7.11.1;
DE AltName: Full=B lymphocyte serine/threonine-protein kinase;
DE AltName: Full=Germinal center kinase;
DE Short=GC kinase;
DE AltName: Full=MAPK/ERK kinase kinase kinase 2;
DE Short=MEK kinase kinase 2;
DE Short=MEKKK 2;
DE AltName: Full=Rab8-interacting protein;
GN Name=MAP4K2; Synonyms=GCK, RAB8IP;
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 {ECO:0000312|EMBL:AAA20968.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-820 (ISOFORM 1), FUNCTION, DOMAIN, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Tonsil;
RX PubMed=7515885; DOI=10.1016/s0021-9258(19)89463-2;
RA Katz P., Whalen G., Kehrl J.H.;
RT "Differential expression of a novel protein kinase in human B lymphocytes.
RT Preferential localization in the germinal center.";
RL J. Biol. Chem. 269:16802-16809(1994).
RN [5]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=7477268; DOI=10.1038/377750a0;
RA Pombo C.M., Kehrl J.H., Sanchez I., Katz P., Avruch J., Zon L.I.,
RA Woodgett J.R., Force T., Kyriakis J.M.;
RT "Activation of the SAPK pathway by the human STE20 homologue germinal
RT centre kinase.";
RL Nature 377:750-754(1995).
RN [6]
RP FUNCTION, AUTOPHOSPHORYLATION, AND INTERACTION WITH MAP3K1/MEKK1 AND TRAF2.
RX PubMed=9712898; DOI=10.1074/jbc.273.35.22681;
RA Yuasa T., Ohno S., Kehrl J.H., Kyriakis J.M.;
RT "Tumor necrosis factor signaling to stress-activated protein kinase
RT (SAPK)/Jun NH2-terminal kinase (JNK) and p38. Germinal center kinase
RT couples TRAF2 to mitogen-activated protein kinase/ERK kinase kinase 1 and
RT SAPK while receptor interacting protein associates with a mitogen-activated
RT protein kinase kinase kinase upstream of MKK6 and p38.";
RL J. Biol. Chem. 273:22681-22692(1998).
RN [7] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH TRAF2 AND MAP3K1.
RX PubMed=11784851; DOI=10.1128/mcb.22.3.737-749.2002;
RA Chadee D.N., Yuasa T., Kyriakis J.M.;
RT "Direct activation of mitogen-activated protein kinase kinase kinase MEKK1
RT by the Ste20p homologue GCK and the adapter protein TRAF2.";
RL Mol. Cell. Biol. 22:737-749(2002).
RN [8]
RP ACTIVITY REGULATION, FUNCTION, UBIQUITINATION, AND INTERACTION WITH TRAF6.
RX PubMed=15456887; DOI=10.1128/mcb.24.20.9165-9175.2004;
RA Zhong J., Kyriakis J.M.;
RT "Germinal center kinase is required for optimal Jun N-terminal kinase
RT activation by Toll-like receptor agonists and is regulated by the ubiquitin
RT proteasome system and agonist-induced, TRAF6-dependent stabilization.";
RL Mol. Cell. Biol. 24:9165-9175(2004).
RN [9]
RP FUNCTION, AND INTERACTION WITH MAP3K11/MLK3.
RX PubMed=17584736; DOI=10.1074/jbc.m703422200;
RA Zhong J., Kyriakis J.M.;
RT "Dissection of a signaling pathway by which pathogen-associated molecular
RT patterns recruit the JNK and p38 MAPKs and trigger cytokine release.";
RL J. Biol. Chem. 282:24246-24254(2007).
RN [10]
RP REVIEW ON FUNCTION.
RX PubMed=10026130; DOI=10.1074/jbc.274.9.5259;
RA Kyriakis J.M.;
RT "Signaling by the germinal center kinase family of protein kinases.";
RL J. Biol. Chem. 274:5259-5262(1999).
RN [11]
RP REVIEW ON FUNCTION.
RX PubMed=11316611; DOI=10.1016/s0962-8924(01)01980-8;
RA Dan I., Watanabe N.M., Kusumi A.;
RT "The Ste20 group kinases as regulators of MAP kinase cascades.";
RL Trends Cell Biol. 11:220-230(2001).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328 AND SER-394, 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 [16]
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Serine/threonine-protein kinase which acts as an essential
CC component of the MAP kinase signal transduction pathway. Acts as a MAPK
CC kinase kinase kinase (MAP4K) and is an upstream activator of the
CC stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK)
CC signaling pathway and to a lesser extent of the p38 MAPKs signaling
CC pathway. Required for the efficient activation of JNKs by TRAF6-
CC dependent stimuli, including pathogen-associated molecular patterns
CC (PAMPs) such as polyinosine-polycytidine (poly(IC)),
CC lipopolysaccharides (LPS), lipid A, peptidoglycan (PGN), or bacterial
CC flagellin. To a lesser degree, IL-1 and engagement of CD40 also
CC stimulate MAP4K2-mediated JNKs activation. The requirement for
CC MAP4K2/GCK is most pronounced for LPS signaling, and extends to LPS
CC stimulation of c-Jun phosphorylation and induction of IL-8. Enhances
CC MAP3K1 oligomerization, which may relieve N-terminal mediated MAP3K1
CC autoinhibition and lead to activation following autophosphorylation.
CC Mediates also the SAP/JNK signaling pathway and the p38 MAPKs signaling
CC pathway through activation of the MAP3Ks MAP3K10/MLK2 and MAP3K11/MLK3.
CC May play a role in the regulation of vesicle targeting or fusion.
CC regulation of vesicle targeting or fusion.
CC {ECO:0000269|PubMed:11784851, ECO:0000269|PubMed:15456887,
CC ECO:0000269|PubMed:17584736, ECO:0000269|PubMed:7477268,
CC ECO:0000269|PubMed:7515885, ECO:0000269|PubMed:9712898}.
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 Evidence={ECO:0000269|PubMed:7515885};
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; Evidence={ECO:0000269|PubMed:7515885};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:7515885};
CC -!- ACTIVITY REGULATION: The tumor necrosis factor (TNF), as well as
CC endotoxins and pro-inflammatory stimuli such as polyinosine-
CC polycytidine (poly(IC)), lipopolysaccharides (LPS), peptidoglycan
CC (PGN), flagellin, or lipid A activate MAP4K2 by promoting its
CC autophosphorylation. {ECO:0000269|PubMed:15456887,
CC ECO:0000269|PubMed:7477268}.
CC -!- SUBUNIT: Interacts with TRAF2, TRAF6, MAP3K1/MEKK1 and MAP3K11/MLK3.
CC Interacts with RAB8A (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q12851; Q13233: MAP3K1; NbExp=2; IntAct=EBI-49783, EBI-49776;
CC Q12851; Q9NUX5: POT1; NbExp=2; IntAct=EBI-49783, EBI-752420;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Basolateral cell
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q12851-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12851-2; Sequence=VSP_054134;
CC -!- TISSUE SPECIFICITY: Highly expressed in germinal center but not mantle
CC zone B-cells. Also expressed in lung, brain and placenta and at lower
CC levels in other tissues examined. {ECO:0000269|PubMed:7515885}.
CC -!- DOMAIN: The PEST domains are Pro-, Glu-, Ser-, and Thr-rich domains.
CC Proteins with PEST domains are frequently targets of degradation by the
CC ubiquitin proteasome. {ECO:0000269|PubMed:7515885}.
CC -!- PTM: Polyubiquitinated through 'Lys-48'-polyubiquitin chains, allowing
CC proteasomal turnover. Ubiquitination requires the kinase activity of
CC MAP4K2/GCK. {ECO:0000269|PubMed:15456887}.
CC -!- PTM: Autophosphorylated in response to tumor necrosis factor (TNF),
CC endotoxins or pro-inflammatory stimuli. Autophosphorylation leads to
CC activation.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA20968.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR EMBL; AP001462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW74302.1; -; Genomic_DNA.
DR EMBL; BC047865; AAH47865.1; -; mRNA.
DR EMBL; U07349; AAA20968.1; ALT_SEQ; mRNA.
DR CCDS; CCDS8082.1; -. [Q12851-1]
DR CCDS; CCDS81582.1; -. [Q12851-2]
DR PIR; A53714; A53714.
DR RefSeq; NP_001294919.1; NM_001307990.1. [Q12851-2]
DR RefSeq; NP_004570.2; NM_004579.4. [Q12851-1]
DR AlphaFoldDB; Q12851; -.
DR SMR; Q12851; -.
DR BioGRID; 111809; 93.
DR IntAct; Q12851; 17.
DR MINT; Q12851; -.
DR STRING; 9606.ENSP00000294066; -.
DR BindingDB; Q12851; -.
DR ChEMBL; CHEMBL5330; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q12851; -.
DR GuidetoPHARMACOLOGY; 2086; -.
DR iPTMnet; Q12851; -.
DR PhosphoSitePlus; Q12851; -.
DR BioMuta; MAP4K2; -.
DR DMDM; 215274019; -.
DR CPTAC; CPTAC-862; -.
DR CPTAC; CPTAC-863; -.
DR EPD; Q12851; -.
DR jPOST; Q12851; -.
DR MassIVE; Q12851; -.
DR MaxQB; Q12851; -.
DR PaxDb; Q12851; -.
DR PeptideAtlas; Q12851; -.
DR PRIDE; Q12851; -.
DR ProteomicsDB; 58984; -. [Q12851-1]
DR ProteomicsDB; 70069; -.
DR Antibodypedia; 2060; 250 antibodies from 28 providers.
DR DNASU; 5871; -.
DR Ensembl; ENST00000294066.7; ENSP00000294066.2; ENSG00000168067.12. [Q12851-1]
DR Ensembl; ENST00000377350.7; ENSP00000366567.3; ENSG00000168067.12. [Q12851-2]
DR GeneID; 5871; -.
DR KEGG; hsa:5871; -.
DR MANE-Select; ENST00000294066.7; ENSP00000294066.2; NM_004579.5; NP_004570.2.
DR UCSC; uc001obh.4; human. [Q12851-1]
DR CTD; 5871; -.
DR DisGeNET; 5871; -.
DR GeneCards; MAP4K2; -.
DR HGNC; HGNC:6864; MAP4K2.
DR HPA; ENSG00000168067; Low tissue specificity.
DR MIM; 603166; gene.
DR neXtProt; NX_Q12851; -.
DR OpenTargets; ENSG00000168067; -.
DR PharmGKB; PA30610; -.
DR VEuPathDB; HostDB:ENSG00000168067; -.
DR eggNOG; KOG0576; Eukaryota.
DR GeneTree; ENSGT00940000162250; -.
DR InParanoid; Q12851; -.
DR OMA; DTANNPE; -.
DR OrthoDB; 996262at2759; -.
DR PhylomeDB; Q12851; -.
DR TreeFam; TF105121; -.
DR PathwayCommons; Q12851; -.
DR SignaLink; Q12851; -.
DR SIGNOR; Q12851; -.
DR BioGRID-ORCS; 5871; 31 hits in 1083 CRISPR screens.
DR GeneWiki; MAP4K2; -.
DR GenomeRNAi; 5871; -.
DR Pharos; Q12851; Tchem.
DR PRO; PR:Q12851; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q12851; protein.
DR Bgee; ENSG00000168067; Expressed in granulocyte and 116 other tissues.
DR ExpressionAtlas; Q12851; baseline and differential.
DR Genevisible; Q12851; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; TAS:ProtInc.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0008349; F:MAP kinase kinase kinase kinase activity; IBA:GO_Central.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:UniProtKB.
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:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR GO; GO:0007254; P:JNK cascade; TAS:ProtInc.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:UniProtKB.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0006903; P:vesicle targeting; IEA:Ensembl.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR021160; MAPKKKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF038172; MAPKKKK; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Cytoplasm;
KW Golgi apparatus; Immunity; Innate immunity; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Stress response; Transferase;
KW Ubl conjugation.
FT CHAIN 1..820
FT /note="Mitogen-activated protein kinase kinase kinase
FT kinase 2"
FT /id="PRO_0000086275"
FT DOMAIN 16..273
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 482..793
FT /note="CNH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT REGION 294..314
FT /note="PEST1"
FT REGION 344..360
FT /note="PEST2"
FT REGION 387..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..448
FT /note="PEST3"
FT COMPBIAS 409..438
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 22..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 426..433
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054134"
FT CONFLICT 120
FT /note="A -> R (in Ref. 4; AAA20968)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 820 AA; 91556 MW; A59C1E99BFFAEF41 CRC64;
MALLRDVSLQ DPRDRFELLQ RVGAGTYGDV YKARDTVTSE LAAVKIVKLD PGDDISSLQQ
EITILRECRH PNVVAYIGSY LRNDRLWICM EFCGGGSLQE IYHATGPLEE RQIAYVCREA
LKGLHHLHSQ GKIHRDIKGA NLLLTLQGDV KLADFGVSGE LTASVAKRRS FIGTPYWMAP
EVAAVERKGG YNELCDVWAL GITAIELGEL QPPLFHLHPM RALMLMSKSS FQPPKLRDKT
RWTQNFHHFL KLALTKNPKK RPTAEKLLQH PFTTQQLPRA LLTQLLDKAS DPHLGTPSPE
DCELETYDMF PDTIHSRGQH GPAERTPSEI QFHQVKFGAP RRKETDPLNE PWEEEWTLLG
KEELSGSLLQ SVQEALEERS LTIRSASEFQ ELDSPDDTMG TIKRAPFLGP LPTDPPAEEP
LSSPPGTLPP PPSGPNSSPL LPTAWATMKQ REDPERSSCH GLPPTPKVHM GACFSKVFNG
CPLRIHAAVT WIHPVTRDQF LVVGAEEGIY TLNLHELHED TLEKLISHRC SWLYCVNNVL
LSLSGKSTHI WAHDLPGLFE QRRLQQQVPL SIPTNRLTQR IIPRRFALST KIPDTKGCLQ
CRVVRNPYTG ATFLLAALPT SLLLLQWYEP LQKFLLLKNF SSPLPSPAGM LEPLVLDGKE
LPQVCVGAEG PEGPGCRVLF HVLPLEAGLT PDILIPPEGI PGSAQQVIQV DRDTILVSFE
RCVRIVNMQG EPTATLAPEL TFDFPIETVV CLQDSVLAFW SHGMQGRSLD TNEVTQEITD
ETRIFRVLGA HRDIILESIP TDNPEAHSNL YILTGHQSTY
