UN13B_MOUSE
ID UN13B_MOUSE Reviewed; 1602 AA.
AC Q9Z1N9; A2AG43; B2RXT0; B2RXY6; Q6BCX2;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Protein unc-13 homolog B;
DE AltName: Full=Munc13-2 {ECO:0000303|PubMed:23229896};
DE Short=munc13;
GN Name=Unc13b {ECO:0000312|MGI:MGI:1342278}; Synonyms=Unc13a;
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 [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 2).
RC STRAIN=BALB/cJ;
RX PubMed=15330860; DOI=10.1111/j.1365-2443.2004.00767.x;
RA Fukuda M.;
RT "Alternative splicing in the first alpha-helical region of the Rab-binding
RT domain of Rim regulates Rab3A binding activity: is Rim a Rab3 effector
RT protein during evolution?";
RL Genes Cells 9:831-842(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RA Song Y., Silverman M.;
RT "Cloning of the mouse renal isoform of munc13s.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
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 [5]
RP FUNCTION.
RX PubMed=12070347; DOI=10.1073/pnas.122623799;
RA Varoqueaux F., Sigler A., Rhee J.-S., Brose N., Enk C., Reim K.,
RA Rosenmund C.;
RT "Total arrest of spontaneous and evoked synaptic transmission but normal
RT synaptogenesis in the absence of Munc13-mediated vesicle priming.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9037-9042(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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 FUNCTION.
RX PubMed=23229896; DOI=10.1083/jcb.201208024;
RA van de Bospoort R., Farina M., Schmitz S.K., de Jong A., de Wit H.,
RA Verhage M., Toonen R.F.;
RT "Munc13 controls the location and efficiency of dense-core vesicle release
RT in neurons.";
RL J. Cell Biol. 199:883-891(2012).
CC -!- FUNCTION: Plays a role in vesicle maturation during exocytosis as a
CC target of the diacylglycerol second messenger pathway. Is involved in
CC neurotransmitter release by acting in synaptic vesicle priming prior to
CC vesicle fusion and participates in the activity-depending refilling of
CC readily releasable vesicle pool (RRP) (By similarity). Essential for
CC synaptic vesicle maturation in a subset of excitatory/glutamatergic but
CC not inhibitory/GABA-mediated synapses. In collaboration with UNC13A,
CC facilitates neuronal dense core vesicles fusion as well as controls the
CC location and efficiency of their synaptic release (PubMed:23229896).
CC {ECO:0000250, ECO:0000269|PubMed:12070347,
CC ECO:0000269|PubMed:23229896}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBUNIT: Interacts with RIMS1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
CC Golgi apparatus. Synapse {ECO:0000250}. Note=Localized to synapses (By
CC similarity). Translocates to the Golgi in response to phorbol ester
CC binding. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Z1N9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z1N9-2; Sequence=VSP_039197;
CC Name=3;
CC IsoId=Q9Z1N9-3; Sequence=VSP_039198;
CC -!- DOMAIN: The C2 domains are not involved in calcium-dependent
CC phospholipid binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the unc-13 family. {ECO:0000305}.
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DR EMBL; AB162894; BAD32690.1; -; Genomic_DNA.
DR EMBL; AF115848; AAD13619.1; -; mRNA.
DR EMBL; AL672276; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL732504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL772176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC157967; AAI57968.1; -; mRNA.
DR EMBL; BC158025; AAI58026.1; -; mRNA.
DR CCDS; CCDS38738.1; -. [Q9Z1N9-3]
DR CCDS; CCDS51161.1; -. [Q9Z1N9-1]
DR CCDS; CCDS80089.1; -. [Q9Z1N9-2]
DR RefSeq; NP_001074882.1; NM_001081413.2. [Q9Z1N9-3]
DR RefSeq; NP_001297687.1; NM_001310758.1. [Q9Z1N9-2]
DR RefSeq; NP_067443.2; NM_021468.3. [Q9Z1N9-1]
DR AlphaFoldDB; Q9Z1N9; -.
DR SMR; Q9Z1N9; -.
DR BioGRID; 204444; 4.
DR IntAct; Q9Z1N9; 1.
DR MINT; Q9Z1N9; -.
DR STRING; 10090.ENSMUSP00000103586; -.
DR DrugBank; DB11752; Bryostatin 1.
DR iPTMnet; Q9Z1N9; -.
DR PhosphoSitePlus; Q9Z1N9; -.
DR MaxQB; Q9Z1N9; -.
DR PaxDb; Q9Z1N9; -.
DR PRIDE; Q9Z1N9; -.
DR ProteomicsDB; 300081; -. [Q9Z1N9-1]
DR ProteomicsDB; 300082; -. [Q9Z1N9-2]
DR ProteomicsDB; 300083; -. [Q9Z1N9-3]
DR Antibodypedia; 11512; 186 antibodies from 29 providers.
DR DNASU; 22249; -.
DR Ensembl; ENSMUST00000079978; ENSMUSP00000078894; ENSMUSG00000028456. [Q9Z1N9-2]
DR Ensembl; ENSMUST00000107952; ENSMUSP00000103586; ENSMUSG00000028456. [Q9Z1N9-1]
DR Ensembl; ENSMUST00000163653; ENSMUSP00000128608; ENSMUSG00000028456. [Q9Z1N9-3]
DR GeneID; 22249; -.
DR KEGG; mmu:22249; -.
DR UCSC; uc008spg.2; mouse. [Q9Z1N9-3]
DR UCSC; uc012dcy.1; mouse. [Q9Z1N9-1]
DR CTD; 10497; -.
DR MGI; MGI:1342278; Unc13b.
DR VEuPathDB; HostDB:ENSMUSG00000028456; -.
DR eggNOG; KOG1011; Eukaryota.
DR GeneTree; ENSGT00940000154929; -.
DR HOGENOM; CLU_001304_3_0_1; -.
DR InParanoid; Q9Z1N9; -.
DR OrthoDB; 117172at2759; -.
DR PhylomeDB; Q9Z1N9; -.
DR TreeFam; TF312844; -.
DR Reactome; R-MMU-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-MMU-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-MMU-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-264642; Acetylcholine Neurotransmitter Release Cycle.
DR BioGRID-ORCS; 22249; 1 hit in 40 CRISPR screens.
DR ChiTaRS; Unc13b; mouse.
DR PRO; PR:Q9Z1N9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9Z1N9; protein.
DR Bgee; ENSMUSG00000028456; Expressed in submandibular gland and 220 other tissues.
DR ExpressionAtlas; Q9Z1N9; baseline and differential.
DR Genevisible; Q9Z1N9; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044305; C:calyx of Held; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0032009; C:early phagosome; IDA:ParkinsonsUK-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0098793; C:presynapse; IDA:ParkinsonsUK-UCL.
DR GO; GO:0048786; C:presynaptic active zone; IDA:ParkinsonsUK-UCL.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
DR GO; GO:0097470; C:ribbon synapse; IDA:ParkinsonsUK-UCL.
DR GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR GO; GO:0019992; F:diacylglycerol binding; IEA:InterPro.
DR GO; GO:0030742; F:GTP-dependent protein binding; ISO:MGI.
DR GO; GO:0001566; F:non-kinase phorbol ester receptor activity; TAS:MGI.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR GO; GO:0017075; F:syntaxin-1 binding; ISO:MGI.
DR GO; GO:0060478; P:acrosomal vesicle exocytosis; ISO:MGI.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:0061789; P:dense core granule priming; ISO:MGI.
DR GO; GO:0060384; P:innervation; IGI:MGI.
DR GO; GO:0031914; P:negative regulation of synaptic plasticity; IGI:ParkinsonsUK-UCL.
DR GO; GO:0007528; P:neuromuscular junction development; IGI:MGI.
DR GO; GO:0099011; P:neuronal dense core vesicle exocytosis; IMP:UniProtKB.
DR GO; GO:0090382; P:phagosome maturation; IMP:ParkinsonsUK-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:ParkinsonsUK-UCL.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:MGI.
DR GO; GO:0097151; P:positive regulation of inhibitory postsynaptic potential; ISS:ParkinsonsUK-UCL.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR GO; GO:0010808; P:positive regulation of synaptic vesicle priming; ISS:ParkinsonsUK-UCL.
DR GO; GO:0099525; P:presynaptic dense core vesicle exocytosis; IMP:SynGO.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IMP:ParkinsonsUK-UCL.
DR GO; GO:0061669; P:spontaneous neurotransmitter secretion; ISO:MGI.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR GO; GO:0016081; P:synaptic vesicle docking; IGI:MGI.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:0016188; P:synaptic vesicle maturation; IBA:GO_Central.
DR GO; GO:0016082; P:synaptic vesicle priming; IMP:ParkinsonsUK-UCL.
DR CDD; cd00029; C1; 1.
DR CDD; cd04027; C2B_Munc13; 1.
DR Gene3D; 2.60.40.150; -; 3.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR010439; MUN_dom.
DR InterPro; IPR014770; Munc13_1.
DR InterPro; IPR014772; Munc13_dom-2.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR027080; Unc-13.
DR InterPro; IPR037302; Unc-13_C2B.
DR PANTHER; PTHR10480; PTHR10480; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00168; C2; 3.
DR Pfam; PF06292; MUN; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00239; C2; 3.
DR SMART; SM01145; DUF1041; 1.
DR SUPFAM; SSF49562; SSF49562; 3.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50004; C2; 3.
DR PROSITE; PS51258; MHD1; 1.
DR PROSITE; PS51259; MHD2; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Coiled coil; Cytoplasm; Exocytosis;
KW Golgi apparatus; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Synapse; Zinc; Zinc-finger.
FT CHAIN 1..1602
FT /note="Protein unc-13 homolog B"
FT /id="PRO_0000188576"
FT DOMAIN 1..97
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 595..719
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1024..1168
FT /note="MHD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00587"
FT DOMAIN 1275..1417
FT /note="MHD2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00588"
FT DOMAIN 1430..1557
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 489..539
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 189..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1210..1231
FT /evidence="ECO:0000255"
FT COMPBIAS 190..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 628
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 628
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 634
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 680
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 680
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 682
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 682
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 699
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14795"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14795"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14795"
FT VAR_SEQ 176..188
FT /note="CHWTYLGWGEHQT -> S (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_039197"
FT VAR_SEQ 962
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039198"
FT CONFLICT 31
FT /note="V -> E (in Ref. 2; AAD13619)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="S -> D (in Ref. 2; AAD13619)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="L -> W (in Ref. 1; BAD32690 and 2; AAD13619)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="R -> H (in Ref. 2; AAD13619)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="H -> Y (in Ref. 1; BAD32690 and 2; AAD13619)"
FT /evidence="ECO:0000305"
FT CONFLICT 512..513
FT /note="GL -> AV (in Ref. 1; BAD32690 and 2; AAD13619)"
FT /evidence="ECO:0000305"
FT CONFLICT 579..580
FT /note="EV -> RI (in Ref. 2; AAD13619)"
FT /evidence="ECO:0000305"
FT CONFLICT 804
FT /note="R -> A (in Ref. 2; AAD13619)"
FT /evidence="ECO:0000305"
FT CONFLICT 837
FT /note="L -> M (in Ref. 2; AAD13619)"
FT /evidence="ECO:0000305"
FT CONFLICT 1073
FT /note="P -> PG (in Ref. 2; AAD13619)"
FT /evidence="ECO:0000305"
FT CONFLICT 1279..1280
FT /note="PL -> GV (in Ref. 2; AAD13619)"
FT /evidence="ECO:0000305"
FT CONFLICT 1280
FT /note="L -> P (in Ref. 2; AAI58026)"
FT /evidence="ECO:0000305"
FT CONFLICT 1418
FT /note="R -> G (in Ref. 2; AAD13619)"
FT /evidence="ECO:0000305"
FT CONFLICT 1492
FT /note="K -> R (in Ref. 2; AAD13619)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1602 AA; 181813 MW; FED63BFE566554D2 CRC64;
MSLLCVRVKR AKFQGSPDKF NTYVTLKVQN VKSTTVAVRG DQPSWEQDFM FEISRLDLGL
SVEVWNKGLI WDTMVGTVWI ALKTIRQSDE EGPGEWSTLE AETLMKDDEI CGTKNPTPHK
ILLDTRFELP FDIPEEEARY WTYKLEQINA LADDNEYSSQ EESQRKPLPT AAAQCCHWTY
LGWGEHQTFE DPDSAVDDRD SDYRSETSNS APPPYHTTTQ PNASVHQFPV PVRLPQQLFL
QGSSHDSCND SMQSYDLDYP ERRALSPTSS SRYGSSCNVS QGSSLLSELD QYHEQDDDGR
ERDSIHSSHS YGSLSKDGQA GLGEQEKALE VTCESEKEKT GESKEMRDDA TIHPPSDLVL
HKDHVLGPQE SLPEETASSP FTQARAHWFR AVTKVRLQLQ EISDDGDPSL PQWLPEGPAG
GLYGIDSMPD LRRKKPLPLV SDLSLVQSRK AGITSAMATR TSLKDEELKS HVYKKTLQAL
IYPISCTTPH NFEVWSATTP TYCYECEGLL WGLARQGMRC SECGVKCHEK CQDLLNADCL
QRAAEKSSKH GAEDRTQNII MAMKDRMKIR ERNKPEIFEV IRDVFTVSKV AHVQQMKTVK
QSVLDGTSKW SAKITITVVC AQGLQAKDKT GSSDPYVTVQ VGKTKKRTKT IFGNLNPVWE
EKFHFECHNS SDRIKVRVWD EDDDIKSRVK QRLKRESDDF LGQTIIEVRT LSGEMDVWYN
LEKRTDKSAV SGAIRLQISV EIKGEEKVAP YHVQYTCLHE NLFHYLTDIQ GSGGVWIPEA
RGDDAWKVYF DETAQEIVDE FAMRYGIESI YQAMTHFACL SSKYMCPGVP AVMSTLLANI
NAYYAHTTAS TNVSASDRFA ASNFGKERFV KLLDQLHNSL RIDLSTYRNN FPAGSPERLQ
DLKSTVDLLT SITFFRMKVQ ELQSPPRASQ VVKDCVKACL NSTYEYIFNN CHDLYSHQYQ
LQEQPLEEPG PSIRNLDFWP KLITLIVSII EEDKNSYTPV LSQFPQELNV GKVSAEVMWH
LFAQDMKYAL EEHEKDRLCK SADYMNLHFK VKWLHNEYVR DLPALQGQVP EYPAWFEQFV
LQWLDENEDV SLEFLRGALE RDKKDGFQQT SEHALFSCSV VDVFTQLNQS FEIIRKLECP
DPNILAHYMR RFAKTIGKVL MQYADILSKN FPAYCTKERL PCILMNNMQQ LRVQLEKMFE
AMGGKELDSE AADSLKELQV KLNTVLDELS MVFGNSFQVR IDECVRQMAD ILGQVRGTGN
ASPNARASVA QDADSVLRPL MDFLDGNLTL FATVCEKTVL KRVLKELWRV VMNTMERVIV
LPPLTDQTGT QLILTAAKEL SQLSKLKDHM VREETRNLTP KQCAVLDLAL DTIKQYFHAG
GNGLKKTFLE KSPDLQSLRY ALSLYTQTTD TLIKTFVRSQ TAQGAGVDDP VGEVSIQVDL
FTHPGTGEHK VTVKVVAAND LKWQTAGMFR PFVEVTMVGP HQSDKKRKFT TKSKSNNWTP
KYNETFHFLL GNEEGPEAYE LQICVKDYCF AREDRVIGLA VMPLRDVAAK GSCACWCPLG
RKIHMDETGM TILRILSQRS NDEVAREFVK LKSESRSTEE GS
