AP3B1_MOUSE
ID AP3B1_MOUSE Reviewed; 1105 AA.
AC Q9Z1T1; E9QQ08; Q91YR4;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=AP-3 complex subunit beta-1;
DE AltName: Full=Adaptor protein complex AP-3 subunit beta-1;
DE AltName: Full=Adaptor-related protein complex 3 subunit beta-1;
DE AltName: Full=Beta-3A-adaptin;
DE AltName: Full=Clathrin assembly protein complex 3 beta-1 large chain;
GN Name=Ap3b1;
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], TISSUE SPECIFICITY, AND DISEASE.
RC STRAIN=C3H/HeJ;
RX PubMed=9931340; DOI=10.1093/hmg/8.2.323;
RA Feng L., Seymour A.B., Jiang S.Y., To A., Peden A.A., Novak E.K., Zhen L.,
RA Rusiniak M.E., Eicher E.M., Robinson M.S., Gorin M.B., Swank R.T.;
RT "The beta-3A subunit gene (Ap3b1) of the AP-3 adaptor complex is altered in
RT the mouse hypopigmentation mutant pearl, a model for Hermansky-Pudlak
RT syndrome and night blindness.";
RL Hum. Mol. Genet. 8:323-330(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=11056055; DOI=10.1006/geno.2000.6350;
RA Feng L., Rigatti B.W., Novak E.K., Gorin M.B., Swank R.T.;
RT "Genomic structure of the mouse ap3b1 gene in normal and pearl mice.";
RL Genomics 69:370-379(2000).
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].
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [8]
RP FUNCTION, AND ASSOCIATION WITH THE BLOC-1 COMPLEX.
RX PubMed=21998198; DOI=10.1091/mbc.e11-07-0592;
RA Larimore J., Tornieri K., Ryder P.V., Gokhale A., Zlatic S.A., Craige B.,
RA Lee J.D., Talbot K., Pare J.F., Smith Y., Faundez V.;
RT "The schizophrenia susceptibility factor dysbindin and its associated
RT complex sort cargoes from cell bodies to the synapse.";
RL Mol. Biol. Cell 22:4854-4867(2011).
RN [9]
RP PYROPHOSPHORYLATION.
RX PubMed=17873058; DOI=10.1073/pnas.0707338104;
RA Bhandari R., Saiardi A., Ahmadibeni Y., Snowman A.M., Resnick A.C.,
RA Kristiansen T.Z., Molina H., Pandey A., Werner J.K. Jr., Juluri K.R.,
RA Xu Y., Prestwich G.D., Parang K., Snyder S.H.;
RT "Protein pyrophosphorylation by inositol pyrophosphates is a
RT posttranslational event.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15305-15310(2007).
CC -!- FUNCTION: Subunit of non-clathrin- and clathrin-associated adaptor
CC protein complex 3 (AP-3) that plays a role in protein sorting in the
CC late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes
CC mediate both the recruitment of clathrin to membranes and the
CC recognition of sorting signals within the cytosolic tails of
CC transmembrane cargo molecules. AP-3 appears to be involved in the
CC sorting of a subset of transmembrane proteins targeted to lysosomes and
CC lysosome-related organelles. In concert with the BLOC-1 complex, AP-3
CC is required to target cargos into vesicles assembled at cell bodies for
CC delivery into neurites and nerve terminals.
CC {ECO:0000269|PubMed:21998198}.
CC -!- SUBUNIT: Adaptor protein complex 3 (AP-3) is a heterotetramer composed
CC of two large adaptins (delta-type subunit AP3D1 and beta-type subunit
CC AP3B1 or AP3B2), a medium adaptin (mu-type subunit AP3M1 or AP3M2) and
CC a small adaptin (sigma-type subunit APS1 or AP3S2) (PubMed:21998198).
CC AP-3 associates with the BLOC-1 complex (PubMed:21998198). Interacts
CC with KIF3A; interaction is direct; interaction is impaired by
CC pyrophosphorylation of AP3B1 (By similarity).
CC {ECO:0000250|UniProtKB:O00203, ECO:0000269|PubMed:21998198}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000250|UniProtKB:O00203}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O00203}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O00203}. Golgi apparatus
CC {ECO:0000250|UniProtKB:O00203}. Note=Component of the coat surrounding
CC the cytoplasmic face of coated vesicles located at the Golgi complex.
CC {ECO:0000250|UniProtKB:O00203}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:9931340}.
CC -!- PTM: Phosphorylated on serine residues. {ECO:0000250|UniProtKB:O00203}.
CC -!- PTM: Pyrophosphorylated by 5-diphosphoinositol pentakisphosphate (5-
CC IP7) (PubMed:17873058). Pyrophosphorylation impairs interaction with
CC KIF3A (By similarity). Serine pyrophosphorylation is achieved by
CC Mg(2+)-dependent, but enzyme independent transfer of a beta-phosphate
CC from a inositol pyrophosphate to a pre-phosphorylated serine residue
CC (PubMed:17873058). {ECO:0000250|UniProtKB:O00203,
CC ECO:0000269|PubMed:17873058}.
CC -!- DISEASE: Note=Defects in Ap3b1 are the cause of the autosomal recessive
CC phenotype 'pearl' (pe). Pearl mice exhibit hypopigmentation, lysosomal
CC secretion abnormalities, and platelet-dense granules with reduced
CC levels of adenine nucleotides and serotonin. The changes in platelets
CC lead to prolonged bleeding. Additionally, pearl mice exhibit reduced
CC sensitivity in the dark-adapted state (PubMed:9931340).
CC {ECO:0000269|PubMed:9931340}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
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DR EMBL; AF103809; AAC78338.1; -; mRNA.
DR EMBL; AF255589; AAG23622.1; -; Genomic_DNA.
DR EMBL; AF255566; AAG23622.1; JOINED; Genomic_DNA.
DR EMBL; AF255567; AAG23622.1; JOINED; Genomic_DNA.
DR EMBL; AF255568; AAG23622.1; JOINED; Genomic_DNA.
DR EMBL; AF255569; AAG23622.1; JOINED; Genomic_DNA.
DR EMBL; AF255570; AAG23622.1; JOINED; Genomic_DNA.
DR EMBL; AF255571; AAG23622.1; JOINED; Genomic_DNA.
DR EMBL; AF255572; AAG23622.1; JOINED; Genomic_DNA.
DR EMBL; AF255573; AAG23622.1; JOINED; Genomic_DNA.
DR EMBL; AF255574; AAG23622.1; JOINED; Genomic_DNA.
DR EMBL; AF255575; AAG23622.1; JOINED; Genomic_DNA.
DR EMBL; AF255576; AAG23622.1; JOINED; Genomic_DNA.
DR EMBL; AF255577; AAG23622.1; JOINED; Genomic_DNA.
DR EMBL; AF255578; AAG23622.1; JOINED; Genomic_DNA.
DR EMBL; AF255579; AAG23622.1; JOINED; Genomic_DNA.
DR EMBL; AF255580; AAG23622.1; JOINED; Genomic_DNA.
DR EMBL; AF255581; AAG23622.1; JOINED; Genomic_DNA.
DR EMBL; AF255582; AAG23622.1; JOINED; Genomic_DNA.
DR EMBL; AF255583; AAG23622.1; JOINED; Genomic_DNA.
DR EMBL; AF255584; AAG23622.1; JOINED; Genomic_DNA.
DR EMBL; AF255585; AAG23622.1; JOINED; Genomic_DNA.
DR EMBL; AF255586; AAG23622.1; JOINED; Genomic_DNA.
DR EMBL; AF255587; AAG23622.1; JOINED; Genomic_DNA.
DR EMBL; AF255588; AAG23622.1; JOINED; Genomic_DNA.
DR EMBL; AC122373; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC123043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015068; AAH15068.1; -; mRNA.
DR CCDS; CCDS26693.1; -.
DR PIR; T18295; T18295.
DR RefSeq; NP_033810.2; NM_009680.3.
DR AlphaFoldDB; Q9Z1T1; -.
DR SMR; Q9Z1T1; -.
DR BioGRID; 198132; 7.
DR ComplexPortal; CPX-5145; Ubiquitous AP-3 Adaptor complex, sigma3a variant.
DR ComplexPortal; CPX-5146; Ubiquitous AP-3 Adaptor complex, sigma3b variant.
DR CORUM; Q9Z1T1; -.
DR DIP; DIP-49018N; -.
DR IntAct; Q9Z1T1; 10.
DR MINT; Q9Z1T1; -.
DR STRING; 10090.ENSMUSP00000022196; -.
DR iPTMnet; Q9Z1T1; -.
DR PhosphoSitePlus; Q9Z1T1; -.
DR EPD; Q9Z1T1; -.
DR jPOST; Q9Z1T1; -.
DR MaxQB; Q9Z1T1; -.
DR PaxDb; Q9Z1T1; -.
DR PeptideAtlas; Q9Z1T1; -.
DR PRIDE; Q9Z1T1; -.
DR ProteomicsDB; 282132; -.
DR Antibodypedia; 24502; 150 antibodies from 30 providers.
DR DNASU; 11774; -.
DR Ensembl; ENSMUST00000022196; ENSMUSP00000022196; ENSMUSG00000021686.
DR GeneID; 11774; -.
DR KEGG; mmu:11774; -.
DR UCSC; uc007rlv.2; mouse.
DR CTD; 8546; -.
DR MGI; MGI:1333879; Ap3b1.
DR VEuPathDB; HostDB:ENSMUSG00000021686; -.
DR eggNOG; KOG1060; Eukaryota.
DR GeneTree; ENSGT00940000157603; -.
DR HOGENOM; CLU_006320_3_1_1; -.
DR InParanoid; Q9Z1T1; -.
DR OMA; ASSNEWK; -.
DR OrthoDB; 323029at2759; -.
DR PhylomeDB; Q9Z1T1; -.
DR TreeFam; TF314605; -.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR BioGRID-ORCS; 11774; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Ap3b1; mouse.
DR PRO; PR:Q9Z1T1; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9Z1T1; protein.
DR Bgee; ENSMUSG00000021686; Expressed in choroid plexus of fourth ventricle and 262 other tissues.
DR ExpressionAtlas; Q9Z1T1; baseline and differential.
DR Genevisible; Q9Z1T1; MM.
DR GO; GO:0030123; C:AP-3 adaptor complex; IC:ComplexPortal.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IC:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005802; C:trans-Golgi network; TAS:MGI.
DR GO; GO:0030742; F:GTP-dependent protein binding; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0008089; P:anterograde axonal transport; IMP:UniProtKB.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; IMP:UniProtKB.
DR GO; GO:0019882; P:antigen processing and presentation; IMP:MGI.
DR GO; GO:0048007; P:antigen processing and presentation, exogenous lipid antigen via MHC class Ib; IMP:MGI.
DR GO; GO:0007596; P:blood coagulation; IMP:MGI.
DR GO; GO:0000902; P:cell morphogenesis; IGI:MGI.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IMP:MGI.
DR GO; GO:0035654; P:clathrin-coated vesicle cargo loading, AP-3-mediated; IC:ComplexPortal.
DR GO; GO:0090152; P:establishment of protein localization to mitochondrial membrane involved in mitochondrial fission; IMP:MGI.
DR GO; GO:0030851; P:granulocyte differentiation; IMP:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IGI:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IMP:MGI.
DR GO; GO:0046907; P:intracellular transport; IC:ComplexPortal.
DR GO; GO:0030324; P:lung development; IGI:MGI.
DR GO; GO:0060425; P:lung morphogenesis; IGI:MGI.
DR GO; GO:0007040; P:lysosome organization; IMP:MGI.
DR GO; GO:1903232; P:melanosome assembly; IC:ComplexPortal.
DR GO; GO:0032438; P:melanosome organization; IMP:MGI.
DR GO; GO:0061024; P:membrane organization; IMP:MGI.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0043473; P:pigmentation; IMP:MGI.
DR GO; GO:0060155; P:platelet dense granule organization; IMP:MGI.
DR GO; GO:0051138; P:positive regulation of NK T cell differentiation; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0034394; P:protein localization to cell surface; IMP:MGI.
DR GO; GO:0036211; P:protein modification process; IMP:MGI.
DR GO; GO:0006622; P:protein targeting to lysosome; IMP:MGI.
DR GO; GO:0050790; P:regulation of catalytic activity; IMP:MGI.
DR GO; GO:0003016; P:respiratory system process; IGI:MGI.
DR GO; GO:0007338; P:single fertilization; IMP:MGI.
DR GO; GO:0098773; P:skin epidermis development; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0016182; P:synaptic vesicle budding from endosome; IDA:SynGO.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; IMP:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006829; P:zinc ion transport; TAS:BHF-UCL.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR026740; AP3_beta.
DR InterPro; IPR029394; AP3B1_Ser.
DR InterPro; IPR029390; AP3B_C.
DR InterPro; IPR026739; AP_beta.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015151; B-adaptin_app_sub_C.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR PANTHER; PTHR11134; PTHR11134; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF14796; AP3B1_C; 1.
DR Pfam; PF14797; SEEEED; 1.
DR PIRSF; PIRSF037096; AP3_complex_beta; 1.
DR SMART; SM01355; AP3B1_C; 1.
DR SMART; SM01020; B2-adapt-app_C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..1105
FT /note="AP-3 complex subunit beta-1"
FT /id="PRO_0000193747"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..707
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..776
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..824
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00203"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00203"
FT MOD_RES 763
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00203"
FT CONFLICT 275..277
FT /note="ESE -> DS (in Ref. 4; AAH15068)"
FT /evidence="ECO:0000305"
FT CONFLICT 439..444
FT /note="VTDTCL -> FTETCF (in Ref. 1; AAC78338 and 2;
FT AAG23622)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="L -> F (in Ref. 1; AAC78338 and 2; AAG23622)"
FT /evidence="ECO:0000305"
FT CONFLICT 691
FT /note="D -> DEE (in Ref. 4; AAH15068)"
FT /evidence="ECO:0000305"
FT CONFLICT 714
FT /note="G -> E (in Ref. 4; AAH15068)"
FT /evidence="ECO:0000305"
FT CONFLICT 724
FT /note="T -> TSN (in Ref. 4; AAH15068)"
FT /evidence="ECO:0000305"
FT CONFLICT 737
FT /note="S -> N (in Ref. 4; AAH15068)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1105 AA; 122740 MW; 59EB4A722B40E233 CRC64;
MSSNSFAYNE QSGGGEAAEL GQEATSTISP SGAFGLFSSD WKKNEDLKQM LESNKDSAKL
DAMKRIVGMI AKGKNASELF PAVVKNVASK NIEIKKLVYV YLVRYAEEQQ DLALLSISTF
QRALKDPNQL IRASALRVLS SIRVPIIVPV MMLAIKEASA DLSPYVRKNA AHAIQKLYSL
DPEQKEMLIE VIEKLLKDKS TLVAGSVVMA FEEVCPDRID LIHRNYRKLC NLLVDVEEWG
QVVIIHMLTR YARTQFVSPW REDGGLEDNE KNFYESEEEE EEKEKSSRKK SYAMDPDHRL
LIRNTKPLLQ SRNAAVVMAV AQLYWHISPK SEAGVISKSL VRLLRSNREV QYIVLQNIAT
MSIERKGMFE PYLKSFYVRS TDPTMIKTLK LEILTNLANE ANISTLLREF QTYVRSQDKQ
FAAATIQTIG RCATSISEVT DTCLNGLVCL LSNRDEIVVA ESVVVIKKLL QMQPAQHGEI
IRHMAKLLDS ITVPVARASI LWLIGENCER VPKIAPDVLR KMAKSFTSED DLVKLQILNL
AAKLYLTNSK QTKLLTQYIL NLGKYDQNYD IRDRTRFIRQ LIVPNEKSGA LSKYAKKIFL
APKPAPLLES PFKDRDRFQL GTLSHTLNIK ASGYLELSNW PEVAPDPSVR NVEVIESAKE
WTPLGKTKKE KPMKKFYSES EEEEDEDEDE DEEEEEKEDE DENPSDSSSD SESGSGSESG
DTGTEDSSED SSSGQDSETG SQAEAERQKV AKRNSKTKRK SDSENREKKN ENSKASESSS
EESSSMEDSS SESESESGSD SEPAPRNVAP AKERKPQQER HPPSKDVFLL DLDDFNPVST
PVALPTPALS PSLIADLEGL NLSTSSSVIN VSTPVFVPTK THELLHRMHG KGLAAHYCFP
RQPCIFSDKM VSVQITLTNT SDRKIENIHI GGKGLPVGMQ MHAFHPIDSL EPKGSVTVSV
GIDFCDSTQT ASFQLCTKDD CFNVTLQPPV GELLSPVAMS EKDFKKEQGT LTGMNETSAT
LIAAPQNFTP SMILQKVVNV ANLGAVPSSQ DNVHRFAART VHSGSLMLVT VELKEGSTAQ
LIINTEKTVI GSVLLRELKP VLSQG
