BIN1_MOUSE
ID BIN1_MOUSE Reviewed; 588 AA.
AC O08539; Q62434;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Myc box-dependent-interacting protein 1;
DE AltName: Full=Amphiphysin II;
DE AltName: Full=Amphiphysin-like protein;
DE AltName: Full=Bridging integrator 1;
DE AltName: Full=SH3 domain-containing protein 9;
GN Name=Bin1; Synonyms=Amphl, Sh3p9;
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), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=9182529; DOI=10.1074/jbc.272.24.15101;
RA Leprince C., Romero F., Cussac D., Vayssiere B., Berger R., Tavitian A.,
RA Camonis J.H.;
RT "A new member of the amphiphysin family connecting endocytosis and signal
RT transduction pathways.";
RL J. Biol. Chem. 272:15101-15105(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Embryo;
RX PubMed=9630982; DOI=10.1038/nbt0696-741;
RA Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.;
RT "Cloning of ligand targets: systematic isolation of SH3 domain-containing
RT proteins.";
RL Nat. Biotechnol. 14:741-744(1996).
RN [3]
RP INTERACTION WITH MYC.
RC TISSUE=Skeletal muscle;
RX PubMed=8782822; DOI=10.1038/ng0996-69;
RA Sakamuro D., Elliott K.J., Wechsler-Reya R., Prendergast G.C.;
RT "BIN1 is a novel Myc-interacting protein with features of a tumour
RT suppressor.";
RL Nat. Genet. 14:69-76(1996).
RN [4]
RP FUNCTION.
RX PubMed=12183633; DOI=10.1126/science.1071362;
RA Lee E., Marcucci M., Daniell L., Pypaert M., Weisz O.A., Ochoa G.C.,
RA Farsad K., Wenk M.R., De Camilli P.;
RT "Amphiphysin 2 (Bin1) and T-tubule biogenesis in muscle.";
RL Science 297:1193-1196(2002).
RN [5]
RP INTERACTION WITH SH3GLB1.
RX PubMed=12456676; DOI=10.1074/jbc.m208568200;
RA Modregger J., Schmidt A.A., Ritter B., Huttner W.B., Plomann M.;
RT "Characterization of endophilin B1b, a brain-specific membrane-associated
RT lysophosphatidic acid acyl transferase with properties distinct from
RT endophilin A1.";
RL J. Biol. Chem. 278:4160-4167(2003).
RN [6]
RP INTERACTION WITH SNX4, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=12668730; DOI=10.1242/jcs.00403;
RA Leprince C., Le Scolan E., Meunier B., Fraisier V., Brandon N.,
RA De Gunzburg J., Camonis J.;
RT "Sorting nexin 4 and amphiphysin 2, a new partnership between endocytosis
RT and intracellular trafficking.";
RL J. Cell Sci. 116:1937-1948(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-298; SER-304 AND
RP THR-308, AND IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-298; SER-304;
RP THR-308 AND SER-324, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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 [13]
RP FUNCTION.
RX PubMed=27179792; DOI=10.1093/hmg/ddw146;
RA Miyagawa T., Ebinuma I., Morohashi Y., Hori Y., Young Chang M., Hattori H.,
RA Maehara T., Yokoshima S., Fukuyama T., Tsuji S., Iwatsubo T.,
RA Prendergast G.C., Tomita T.;
RT "BIN1 regulates BACE1 intracellular trafficking and amyloid-beta
RT production.";
RL Hum. Mol. Genet. 25:2948-2958(2016).
CC -!- FUNCTION: Is a key player in the control of plasma membrane curvature,
CC and membrane shaping and remodeling. Required in muscle cells for the
CC formation of T-tubules, tubular invaginations of the plasma membrane
CC that function in depolarization-contraction coupling. Required in
CC muscle cells for the formation of T-tubules, tubular invaginations of
CC the plasma membrane that function in depolarization-contraction
CC coupling (PubMed:12183633). Is a negative regulator of endocytosis (By
CC similarity). Is also involved in the regulation of intracellular
CC vesicles sorting, modulation of BACE1 trafficking and the control of
CC amyloid-beta production (PubMed:12668730, PubMed:27179792). In neuronal
CC circuits, endocytosis regulation may influence the internalization of
CC PHF-tau aggregates (By similarity). May be involved in the regulation
CC of MYC activity and the control cell proliferation (By similarity).
CC {ECO:0000250|UniProtKB:O00499, ECO:0000250|UniProtKB:O08839,
CC ECO:0000269|PubMed:12183633, ECO:0000269|PubMed:12668730,
CC ECO:0000269|PubMed:27179792}.
CC -!- SUBUNIT: Heterodimer with AMPH (By similarity). Binds SH3GLB1
CC (PubMed:12456676). Interacts (via SH3 domain) with DNM1. Interacts with
CC SYNJ1 (By similarity). Interacts (via SH3 domain) with DNM2. Interacts
CC with CLTC (By similarity). Interacts with AP2A2. Interacts with AP2B1
CC (By similarity). Interacts with MYC (via N-terminal transactivation
CC domain); the interaction requires the integrity of the conserved MYC
CC box regions 1 and 2 (PubMed:8782822). Interacts with BIN2 (By
CC similarity). Interacts with SNX4 (PubMed:12668730). Interacts (via BAR
CC domain) with BACE1 (By similarity). Binds (via BAR domain) F-actin (By
CC similarity). {ECO:0000250|UniProtKB:O00499,
CC ECO:0000250|UniProtKB:O08839, ECO:0000269|PubMed:12456676,
CC ECO:0000269|PubMed:12668730, ECO:0000269|PubMed:8782822}.
CC -!- INTERACTION:
CC O08539; P10637: Mapt; NbExp=2; IntAct=EBI-775152, EBI-774043;
CC O08539; Q9Z2C5: Mtm1; NbExp=3; IntAct=EBI-775152, EBI-6861578;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O00499}. Cytoplasm
CC {ECO:0000269|PubMed:12668730}. Endosome {ECO:0000269|PubMed:12668730}.
CC Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O08839}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=BRAMP2;
CC IsoId=O08539-1; Sequence=Displayed;
CC Name=2; Synonyms=SH3P9;
CC IsoId=O08539-2; Sequence=VSP_000254, VSP_000255;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed mainly in the brain. Isoform
CC 2 is widely expressed. {ECO:0000269|PubMed:9182529}.
CC -!- PTM: Phosphorylated by protein kinase C. {ECO:0000250}.
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DR EMBL; U86405; AAC53318.1; -; mRNA.
DR EMBL; U60884; AAC52661.1; -; mRNA.
DR CCDS; CCDS29119.1; -. [O08539-1]
DR RefSeq; NP_033798.1; NM_009668.2. [O08539-1]
DR RefSeq; XP_006526056.1; XM_006525993.3. [O08539-2]
DR AlphaFoldDB; O08539; -.
DR BMRB; O08539; -.
DR SMR; O08539; -.
DR BioGRID; 206025; 34.
DR ComplexPortal; CPX-744; c-MYC-BIN1 complex.
DR CORUM; O08539; -.
DR IntAct; O08539; 15.
DR MINT; O08539; -.
DR STRING; 10090.ENSMUSP00000025239; -.
DR iPTMnet; O08539; -.
DR PhosphoSitePlus; O08539; -.
DR EPD; O08539; -.
DR jPOST; O08539; -.
DR MaxQB; O08539; -.
DR PaxDb; O08539; -.
DR PeptideAtlas; O08539; -.
DR PRIDE; O08539; -.
DR ProteomicsDB; 265215; -. [O08539-1]
DR ProteomicsDB; 265216; -. [O08539-2]
DR Antibodypedia; 1297; 441 antibodies from 42 providers.
DR DNASU; 30948; -.
DR Ensembl; ENSMUST00000025239; ENSMUSP00000025239; ENSMUSG00000024381. [O08539-1]
DR Ensembl; ENSMUST00000234857; ENSMUSP00000157259; ENSMUSG00000024381. [O08539-2]
DR GeneID; 30948; -.
DR KEGG; mmu:30948; -.
DR UCSC; uc008ejh.1; mouse. [O08539-1]
DR UCSC; uc008ejj.1; mouse. [O08539-2]
DR CTD; 274; -.
DR MGI; MGI:108092; Bin1.
DR VEuPathDB; HostDB:ENSMUSG00000024381; -.
DR eggNOG; KOG3771; Eukaryota.
DR GeneTree; ENSGT00950000182882; -.
DR HOGENOM; CLU_017859_4_0_1; -.
DR InParanoid; O08539; -.
DR OrthoDB; 1366218at2759; -.
DR PhylomeDB; O08539; -.
DR TreeFam; TF313542; -.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 30948; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Bin1; mouse.
DR PRO; PR:O08539; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; O08539; protein.
DR Bgee; ENSMUSG00000024381; Expressed in hindlimb stylopod muscle and 260 other tissues.
DR ExpressionAtlas; O08539; baseline and differential.
DR Genevisible; O08539; MM.
DR GO; GO:0030424; C:axon; IDA:ARUK-UCL.
DR GO; GO:0043194; C:axon initial segment; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0044300; C:cerebellar mossy fiber; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:ARUK-UCL.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0031674; C:I band; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0060987; C:lipid tube; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0033268; C:node of Ranvier; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0030315; C:T-tubule; IDA:ARUK-UCL.
DR GO; GO:0043196; C:varicosity; ISO:MGI.
DR GO; GO:0031982; C:vesicle; IDA:ARUK-UCL.
DR GO; GO:0030018; C:Z disc; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; IMP:ARUK-UCL.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0051020; F:GTPase binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0070063; F:RNA polymerase binding; ISO:MGI.
DR GO; GO:0048156; F:tau protein binding; IPI:Alzheimers_University_of_Toronto.
DR GO; GO:0008333; P:endosome to lysosome transport; ISO:MGI.
DR GO; GO:0060988; P:lipid tube assembly; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0042692; P:muscle cell differentiation; IMP:MGI.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; IMP:ARUK-UCL.
DR GO; GO:1902960; P:negative regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; IMP:ARUK-UCL.
DR GO; GO:1904878; P:negative regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; IMP:ARUK-UCL.
DR GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; IMP:ARUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:1903946; P:negative regulation of ventricular cardiac muscle cell action potential; IMP:ARUK-UCL.
DR GO; GO:0051647; P:nucleus localization; IMP:WormBase.
DR GO; GO:0006997; P:nucleus organization; ISO:MGI.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:ARUK-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0048711; P:positive regulation of astrocyte differentiation; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0045807; P:positive regulation of endocytosis; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0010564; P:regulation of cell cycle process; ISO:MGI.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:ARUK-UCL.
DR GO; GO:0045664; P:regulation of neuron differentiation; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISO:MGI.
DR GO; GO:0033292; P:T-tubule organization; IMP:ARUK-UCL.
DR CDD; cd12139; SH3_Bin1; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR003005; Amphiphysin.
DR InterPro; IPR035471; Amphiphysin-2_SH3.
DR InterPro; IPR003023; Amphiphysin_2.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR46514:SF4; PTHR46514:SF4; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR01251; AMPHIPHYSIN.
DR PRINTS; PR01253; AMPHIPHYSIN2.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW Developmental protein; Differentiation; Endocytosis; Endosome; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; SH3 domain.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O00499"
FT CHAIN 2..588
FT /note="Myc box-dependent-interacting protein 1"
FT /id="PRO_0000192952"
FT DOMAIN 29..276
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 515..588
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 2..122
FT /note="Interaction with BIN2"
FT /evidence="ECO:0000250"
FT REGION 279..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..422
FT /note="Clathrin-binding"
FT /evidence="ECO:0000250"
FT REGION 448..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 15..42
FT /evidence="ECO:0000255"
FT COILED 193..274
FT /evidence="ECO:0000255"
FT COMPBIAS 279..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O00499"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 308
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT VAR_SEQ 174..204
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9630982"
FT /id="VSP_000254"
FT VAR_SEQ 335..457
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9630982"
FT /id="VSP_000255"
SQ SEQUENCE 588 AA; 64470 MW; 63CA362461500F38 CRC64;
MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR
LQKDLRTYLA SVKAMHEASK KLSECLQEVY EPEWPGRDEA NKIAENNDLL WMDYHQKLVD
QALLTMDTYL GQFPDIKSRI AKRGRKLVDY DSARHHYESL QTAKKKDEAK IAKPVSLLEK
AAPQWCQGKL QAHLVAQTNL LRNQAEEELI KAQKVFEEMN VDLQEELPSL WNSRVGFYVN
TFQSIAGLEE NFHKEMSKLN QNLNDVLVSL EKQHGSNTFT VKAQPSDNAP EKGNKSPSPP
PDGSPAATPE IRVNHEPEPA SGASPGATIP KSPSQLRKGP PVPPPPKHTP SKEMKQEQIL
SLFDDAFVPE ISVTTPSQFE APGPFSEQAS LLDLDFEPLP PVASPVKAPT PSGQSIPWDL
WEPTESQAGI LPSGEPSSAE GSFAVAWPSQ TAEPGPAQPA EASEVVGGAQ EPGETAASEA
TSSSLPAVVV ETFSATVNGA VEGSAGTGRL DLPPGFMFKV QAQHDYTATD TDELQLKAGD
VVLVIPFQNP EEQDEGWLMG VKESDWNQHK ELEKCRGVFP ENFTERVQ
