MP2K5_MOUSE
ID MP2K5_MOUSE Reviewed; 448 AA.
AC Q9WVS7; Q8CFM3; Q8K360; Q9D222;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Dual specificity mitogen-activated protein kinase kinase 5;
DE Short=MAP kinase kinase 5;
DE Short=MAPKK 5;
DE EC=2.7.12.2;
DE AltName: Full=MAPK/ERK kinase 5;
DE Short=MEK 5;
GN Name=Map2k5; Synonyms=Mek5, Mkk5, Prkmk5;
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] (ISOFORM 1), FUNCTION, AND MUTAGENESIS OF
RP SER-311 AND THR-315.
RC TISSUE=Brain;
RX PubMed=10473620; DOI=10.1074/jbc.274.37.26563;
RA Kamakura S., Moriguchi T., Nishida E.;
RT "Activation of the protein kinase ERK5/BMK1 by receptor tyrosine kinases.
RT Identification and characterization of a signaling pathway to the
RT nucleus.";
RL J. Biol. Chem. 274:26563-26571(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Head, and Hypothalamus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 INTERACTION WITH SQSTM1; PRKCZ; PRKCI; PARD6A AND MAP3K3, AND DOMAIN.
RX PubMed=12813044; DOI=10.1074/jbc.m303221200;
RA Lamark T., Perander M., Outzen H., Kristiansen K., Oevervatn A.,
RA Michaelsen E., Bjoerkoey G., Johansen T.;
RT "Interaction codes within the family of mammalian Phox and Bem1p domain-
RT containing proteins.";
RL J. Biol. Chem. 278:34568-34581(2003).
RN [5]
RP FUNCTION, DOMAIN, INTERACTION WITH MAP3K2 AND MAPK7, AND MUTAGENESIS OF
RP ARG-20; ILE-21; ASP-64; GLU-65; GLY-67 AND ASP-68.
RX PubMed=16507987; DOI=10.1128/mcb.26.6.2065-2079.2006;
RA Nakamura K., Uhlik M.T., Johnson N.L., Hahn K.M., Johnson G.L.;
RT "PB1 domain-dependent signaling complex is required for extracellular
RT signal-regulated kinase 5 activation.";
RL Mol. Cell. Biol. 26:2065-2079(2006).
RN [6]
RP IDENTIFICATION BY 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).
RN [7]
RP STRUCTURE BY NMR OF 7-107.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PB1 domain of mouse mitogen activated protein
RT kinase kinase 5 (MAP2K5).";
RL Submitted (JAN-2006) to the PDB data bank.
CC -!- FUNCTION: Acts as a scaffold for the formation of a ternary
CC MAP3K2/MAP3K3-MAP3K5-MAPK7 signaling complex. Activation of this
CC pathway appears to play a critical role in protecting cells from
CC stress-induced apoptosis, neuronal survival and cardiac development and
CC angiogenesis. {ECO:0000269|PubMed:10473620,
CC ECO:0000269|PubMed:16507987}.
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=2.7.12.2;
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=2.7.12.2;
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=2.7.12.2;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- SUBUNIT: Interacts with PARD6A, MAP3K3 and MAPK7. Forms a complex with
CC SQSTM1 and PRKCZ or PRKCI. {ECO:0000269|PubMed:12813044,
CC ECO:0000269|PubMed:16507987}.
CC -!- INTERACTION:
CC Q9WVS7; Q61083: Map3k2; NbExp=4; IntAct=EBI-446144, EBI-446134;
CC Q9WVS7; Q61084: Map3k3; NbExp=15; IntAct=EBI-446144, EBI-446250;
CC Q9WVS7; P28656: Nap1l1; NbExp=20; IntAct=EBI-446144, EBI-645055;
CC Q9WVS7; Q64337: Sqstm1; NbExp=3; IntAct=EBI-446144, EBI-645025;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9WVS7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9WVS7-2; Sequence=VSP_015840;
CC Name=3;
CC IsoId=Q9WVS7-3; Sequence=VSP_015838, VSP_015839;
CC Name=4;
CC IsoId=Q9WVS7-4; Sequence=VSP_015836, VSP_015837;
CC -!- DOMAIN: Binds MAP3K2/MAP3K3 and MAPK7 via non-overlapping residues of
CC the PB1 domain. This domain also mediates interactions with SQSTM1 and
CC PARD6A. {ECO:0000269|PubMed:12813044, ECO:0000269|PubMed:16507987}.
CC -!- PTM: Activated by phosphorylation on Ser/Thr by MAP kinase kinase
CC kinases. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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DR EMBL; AB019374; BAA82040.1; -; mRNA.
DR EMBL; AK020716; BAB32187.1; -; mRNA.
DR EMBL; BC013697; AAH13697.1; -; mRNA.
DR EMBL; BC028260; AAH28260.1; -; mRNA.
DR CCDS; CCDS23269.1; -. [Q9WVS7-1]
DR RefSeq; NP_035970.1; NM_011840.2. [Q9WVS7-1]
DR RefSeq; XP_006511208.1; XM_006511145.2.
DR PDB; 1WI0; NMR; -; A=8-107.
DR PDBsum; 1WI0; -.
DR AlphaFoldDB; Q9WVS7; -.
DR SMR; Q9WVS7; -.
DR CORUM; Q9WVS7; -.
DR IntAct; Q9WVS7; 11.
DR STRING; 10090.ENSMUSP00000034920; -.
DR iPTMnet; Q9WVS7; -.
DR PhosphoSitePlus; Q9WVS7; -.
DR EPD; Q9WVS7; -.
DR MaxQB; Q9WVS7; -.
DR PaxDb; Q9WVS7; -.
DR PRIDE; Q9WVS7; -.
DR ProteomicsDB; 290291; -. [Q9WVS7-1]
DR ProteomicsDB; 290292; -. [Q9WVS7-2]
DR ProteomicsDB; 290293; -. [Q9WVS7-3]
DR ProteomicsDB; 290294; -. [Q9WVS7-4]
DR Antibodypedia; 26267; 609 antibodies from 37 providers.
DR DNASU; 23938; -.
DR Ensembl; ENSMUST00000034920; ENSMUSP00000034920; ENSMUSG00000058444. [Q9WVS7-1]
DR GeneID; 23938; -.
DR KEGG; mmu:23938; -.
DR UCSC; uc009qaw.1; mouse. [Q9WVS7-1]
DR UCSC; uc009qaz.1; mouse. [Q9WVS7-4]
DR UCSC; uc012guv.1; mouse. [Q9WVS7-2]
DR CTD; 5607; -.
DR MGI; MGI:1346345; Map2k5.
DR VEuPathDB; HostDB:ENSMUSG00000058444; -.
DR eggNOG; KOG0581; Eukaryota.
DR GeneTree; ENSGT00940000157505; -.
DR HOGENOM; CLU_000288_2_0_1; -.
DR InParanoid; Q9WVS7; -.
DR OMA; ILANGQX; -.
DR OrthoDB; 688282at2759; -.
DR PhylomeDB; Q9WVS7; -.
DR TreeFam; TF106468; -.
DR BioGRID-ORCS; 23938; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Map2k5; mouse.
DR EvolutionaryTrace; Q9WVS7; -.
DR PRO; PR:Q9WVS7; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9WVS7; protein.
DR Bgee; ENSMUSG00000058444; Expressed in internal carotid artery and 257 other tissues.
DR Genevisible; Q9WVS7; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005819; C:spindle; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0004708; F:MAP kinase kinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISO:MGI.
DR GO; GO:0070375; P:ERK5 cascade; ISO:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0000165; P:MAPK cascade; IMP:MGI.
DR GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:2000342; P:negative regulation of chemokine (C-X-C motif) ligand 2 production; ISO:MGI.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:MGI.
DR GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0032717; P:negative regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0060761; P:negative regulation of response to cytokine stimulus; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:MGI.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR CDD; cd06395; PB1_Map2k5; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR034851; PB1_MAP2K5.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51745; PB1; 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 Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..448
FT /note="Dual specificity mitogen-activated protein kinase
FT kinase 5"
FT /id="PRO_0000086384"
FT DOMAIN 18..109
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DOMAIN 166..419
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 18..25
FT /note="Interaction with MAPK7"
FT /evidence="ECO:0000269|PubMed:16507987"
FT REGION 64..68
FT /note="Interaction with MAP3K2/MAP3K3"
FT /evidence="ECO:0000269|PubMed:12813044,
FT ECO:0000269|PubMed:16507987"
FT REGION 116..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..131
FT /note="Interaction with MAPK7"
FT /evidence="ECO:0000269|PubMed:16507987"
FT COMPBIAS 123..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 283
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 172..180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13163"
FT MOD_RES 315
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13163"
FT VAR_SEQ 108..118
FT /note="ACKPPGERNIH -> GYRRGSRLREY (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015836"
FT VAR_SEQ 119..448
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015837"
FT VAR_SEQ 183..186
FT /note="AHHV -> LLHI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015838"
FT VAR_SEQ 187..448
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015839"
FT VAR_SEQ 359..367
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015840"
FT MUTAGEN 20
FT /note="R->A: Loss of MAPK7 binding; when associated with A-
FT 21."
FT /evidence="ECO:0000269|PubMed:16507987"
FT MUTAGEN 21
FT /note="I->A: Loss of MAPK7 binding; when associated with A-
FT 20."
FT /evidence="ECO:0000269|PubMed:16507987"
FT MUTAGEN 64
FT /note="D->A: Loss of MAP3K2/MAP3K3 binding; when associated
FT with A-65."
FT /evidence="ECO:0000269|PubMed:16507987"
FT MUTAGEN 65
FT /note="E->A: Loss of MAP3K2/MAP3K3 binding; when associated
FT with A-64."
FT /evidence="ECO:0000269|PubMed:16507987"
FT MUTAGEN 67
FT /note="G->A: Loss of MAP3K2/MAP3K3 binding; when associated
FT with A-68."
FT /evidence="ECO:0000269|PubMed:16507987"
FT MUTAGEN 68
FT /note="D->A: Loss of MAP3K2/MAP3K3 binding; when associated
FT with A-67."
FT /evidence="ECO:0000269|PubMed:16507987"
FT MUTAGEN 311
FT /note="S->A: Dominant negative form; when associated with
FT V-315."
FT /evidence="ECO:0000269|PubMed:10473620"
FT MUTAGEN 311
FT /note="S->D: Dominant active form; when associated with D-
FT 315."
FT /evidence="ECO:0000269|PubMed:10473620"
FT MUTAGEN 315
FT /note="T->D: Dominant active form; when associated with D-
FT 311."
FT /evidence="ECO:0000269|PubMed:10473620"
FT MUTAGEN 315
FT /note="T->V: Dominant negative form; when associated with
FT A-311."
FT /evidence="ECO:0000269|PubMed:10473620"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:1WI0"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:1WI0"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1WI0"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:1WI0"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1WI0"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:1WI0"
FT HELIX 75..95
FT /evidence="ECO:0007829|PDB:1WI0"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:1WI0"
SQ SEQUENCE 448 AA; 50105 MW; 50C50E8F0F712BE7 CRC64;
MLWLALGPFC AMENQVLVIR IKIPNSGAVD WTVHSGPQLL FRDVLDVIGQ VLPEATTTAF
EYEDEDGDRI TVRSDEEMKA MLSYYYSTVM EQQVNGQLIE PLQIFPRACK PPGERNIHGL
KVNTRAGPSQ HTSPVVSDSL PSNSLKKSSA ELRKILANGQ MNEQDIRYRD TLGHGNGGTV
YKAHHVPSGK ILAVKVILLD ITLELQKQIM SELEILYKCD SSYIIGFYGA FFVENRISIC
TEFMDGGSLD VYRKIPEHVL GRIAVAVVKG LTYLWSLKIL HRDVKPSNML VNTGGQVKLC
DFGVSTQLVN SIAKTYVGTN AYMAPERISG EQYGIHSDVW SLGISFMELA LGRFPYPQIQ
KNQGSLMPLQ LLQCIVDEDS PVLPLGEFSE PFVHFITQCM RKQPKERPAP EELMGHPFIV
QFNDGNSTVV SMWVCRALEE RRSQQGPP
