NBEA_MOUSE
ID NBEA_MOUSE Reviewed; 2936 AA.
AC Q9EPN1; Q8C931; Q9EPM9; Q9EPN0; Q9WVM9;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Neurobeachin;
DE AltName: Full=Lysosomal-trafficking regulator 2;
GN Name=Nbea; Synonyms=Lyst2;
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 {ECO:0000312|EMBL:CAC18811.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Brain {ECO:0000312|EMBL:CAC18811.1};
RX PubMed=11102458; DOI=10.1523/jneurosci.20-23-08551.2000;
RA Wang X., Herberg F.W., Laue M.M., Wullner C., Hu B., Petrasch-Parwez E.,
RA Kilimann M.W.;
RT "Neurobeachin: a protein kinase A-anchoring, beige/Chediak-Higashi protein
RT homolog implicated in neuronal membrane traffic.";
RL J. Neurosci. 20:8551-8565(2000).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Brain {ECO:0000269|PubMed:12160729};
RX PubMed=12160729; DOI=10.1006/geno.2002.6822;
RA Dyomin V.G., Chaganti S.R., Dyomina K., Palanisamy N., Murty V.V.V.S.,
RA Dalla-Favera R., Chaganti R.S.K.;
RT "BCL8 is a novel, evolutionarily conserved human gene family encoding
RT proteins with presumptive protein kinase A anchoring function.";
RL Genomics 80:158-165(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2220-2936.
RA Tchernev V.T., McMurtrie E.B., Nguyen Q.A., Mishra V.S., Barbosa M.D.F.S.,
RA McIndoe R., Kingsmore S.F.;
RT "Identification of LYST2, a brain-specific member of the Chediak-Higashi
RT syndrome gene family.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1001; SER-1004; SER-1519;
RP SER-1704; SER-1707; SER-2128 AND SER-2565, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC 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).
CC -!- FUNCTION: Binds to type II regulatory subunits of protein kinase A and
CC anchors/targets them to the membrane. May anchor the kinase to
CC cytoskeletal and/or organelle-associated proteins. May have a role in
CC membrane trafficking. {ECO:0000269|PubMed:11102458,
CC ECO:0000303|PubMed:11102458}.
CC -!- SUBUNIT: Interacts with RII subunit of PKA.
CC {ECO:0000269|PubMed:11102458}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11102458};
CC Peripheral membrane protein {ECO:0000269|PubMed:11102458}. Endomembrane
CC system {ECO:0000269|PubMed:11102458}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11102458}. Postsynaptic cell membrane
CC {ECO:0000269|PubMed:11102458}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11102458}. Note=Associated with pleomorphic
CC tubulovesicular endomembranes near the trans sides of Golgi stacks and
CC throughout the cell bodies and cell processes. Concentrated at the
CC postsynaptic plasma membrane of a subpopulation of synapses.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000269|PubMed:11102458};
CC IsoId=Q9EPN1-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q9EPN1-2; Sequence=VSP_050540;
CC Name=3 {ECO:0000269|PubMed:11102458};
CC IsoId=Q9EPN1-3; Sequence=VSP_050541;
CC Name=4 {ECO:0000269|PubMed:11102458};
CC IsoId=Q9EPN1-4; Sequence=VSP_050542;
CC -!- TISSUE SPECIFICITY: Forebrain, brainstem and cerebellum.
CC {ECO:0000269|PubMed:11102458}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in neonatal brain, levels decline
CC in adults. {ECO:0000269|PubMed:11102458}.
CC -!- DOMAIN: RII-alpha binding site, predicted to form an amphipathic helix,
CC could participate in protein-protein interactions with a complementary
CC surface on the R-subunit dimer. {ECO:0000303|PubMed:11102458}.
CC -!- SIMILARITY: Belongs to the WD repeat neurobeachin family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y18276; CAC18811.1; -; mRNA.
DR EMBL; Y18276; CAC18812.1; -; mRNA.
DR EMBL; Y18276; CAC18813.1; -; mRNA.
DR EMBL; AK043125; BAC31466.1; -; mRNA.
DR EMBL; AF072372; AAD41634.1; -; mRNA.
DR CCDS; CCDS50911.1; -. [Q9EPN1-1]
DR RefSeq; NP_085098.1; NM_030595.1. [Q9EPN1-1]
DR RefSeq; XP_006501586.1; XM_006501523.3. [Q9EPN1-4]
DR SMR; Q9EPN1; -.
DR BioGRID; 204974; 8.
DR IntAct; Q9EPN1; 10.
DR MINT; Q9EPN1; -.
DR STRING; 10090.ENSMUSP00000029374; -.
DR iPTMnet; Q9EPN1; -.
DR PhosphoSitePlus; Q9EPN1; -.
DR MaxQB; Q9EPN1; -.
DR PaxDb; Q9EPN1; -.
DR PeptideAtlas; Q9EPN1; -.
DR PRIDE; Q9EPN1; -.
DR ProteomicsDB; 287614; -. [Q9EPN1-1]
DR ProteomicsDB; 287615; -. [Q9EPN1-2]
DR ProteomicsDB; 287616; -. [Q9EPN1-3]
DR ProteomicsDB; 287617; -. [Q9EPN1-4]
DR Antibodypedia; 22966; 73 antibodies from 27 providers.
DR Ensembl; ENSMUST00000029374; ENSMUSP00000029374; ENSMUSG00000027799. [Q9EPN1-1]
DR GeneID; 26422; -.
DR KEGG; mmu:26422; -.
DR UCSC; uc008pgt.2; mouse. [Q9EPN1-2]
DR UCSC; uc033htk.1; mouse. [Q9EPN1-1]
DR CTD; 26960; -.
DR MGI; MGI:1347075; Nbea.
DR VEuPathDB; HostDB:ENSMUSG00000027799; -.
DR eggNOG; KOG1787; Eukaryota.
DR GeneTree; ENSGT00940000154934; -.
DR HOGENOM; CLU_000218_2_1_1; -.
DR InParanoid; Q9EPN1; -.
DR OMA; XRKVEIM; -.
DR OrthoDB; 153369at2759; -.
DR PhylomeDB; Q9EPN1; -.
DR TreeFam; TF313490; -.
DR BioGRID-ORCS; 26422; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Nbea; mouse.
DR PRO; PR:Q9EPN1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9EPN1; protein.
DR Bgee; ENSMUSG00000027799; Expressed in caudate-putamen and 240 other tissues.
DR ExpressionAtlas; Q9EPN1; baseline and differential.
DR Genevisible; Q9EPN1; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:CACAO.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; NAS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0051018; F:protein kinase A binding; NAS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IDA:MGI.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IMP:MGI.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; NAS:UniProtKB.
DR GO; GO:0008104; P:protein localization; IDA:MGI.
DR GO; GO:0006605; P:protein targeting; ISS:MGI.
DR CDD; cd06071; Beach; 1.
DR CDD; cd01201; PH_BEACH; 1.
DR Gene3D; 1.10.1540.10; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000409; BEACH_dom.
DR InterPro; IPR036372; BEACH_dom_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR010508; NBEA-like_DUF1088.
DR InterPro; IPR031570; NBEA/BDCP_DUF4704.
DR InterPro; IPR023362; PH-BEACH_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF02138; Beach; 1.
DR Pfam; PF06469; DUF1088; 1.
DR Pfam; PF15787; DUF4704; 1.
DR Pfam; PF14844; PH_BEACH; 1.
DR SMART; SM01026; Beach; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF81837; SSF81837; 1.
DR PROSITE; PS50197; BEACH; 1.
DR PROSITE; PS51783; PH_BEACH; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Synapse; WD repeat.
FT CHAIN 1..2936
FT /note="Neurobeachin"
FT /id="PRO_0000051090"
FT REPEAT 1316..1358
FT /note="WD 1"
FT /evidence="ECO:0000305"
FT DOMAIN 2137..2245
FT /note="BEACH-type PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01119"
FT DOMAIN 2264..2553
FT /note="BEACH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00026,
FT ECO:0000305"
FT REPEAT 2708..2751
FT /note="WD 2"
FT /evidence="ECO:0000305"
FT REPEAT 2768..2808
FT /note="WD 3"
FT /evidence="ECO:0000305"
FT REPEAT 2850..2889
FT /note="WD 4"
FT /evidence="ECO:0000305"
FT REPEAT 2892..2931
FT /note="WD 5"
FT /evidence="ECO:0000305"
FT REGION 961..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1203..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1480..1521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1639..1667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1701..1721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1830..1850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1490..1514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1001
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1004
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1519
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1704
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1707
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..2197
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_050540"
FT VAR_SEQ 1601..1632
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11102458"
FT /id="VSP_050541"
FT VAR_SEQ 2560..2564
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11102458"
FT /id="VSP_050542"
FT CONFLICT 2220..2221
FT /note="FM -> SR (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 2332
FT /note="D -> H (in Ref. 2; AAD41634)"
FT /evidence="ECO:0000305"
FT CONFLICT 2337
FT /note="I -> K (in Ref. 2; AAD41634)"
FT /evidence="ECO:0000305"
FT CONFLICT 2375
FT /note="A -> P (in Ref. 2; AAD41634)"
FT /evidence="ECO:0000305"
FT CONFLICT 2431
FT /note="L -> V (in Ref. 2; AAD41634)"
FT /evidence="ECO:0000305"
FT CONFLICT 2532
FT /note="E -> V (in Ref. 2; AAD41634)"
FT /evidence="ECO:0000305"
FT CONFLICT 2539
FT /note="G -> A (in Ref. 2; AAD41634)"
FT /evidence="ECO:0000305"
FT CONFLICT 2554
FT /note="S -> T (in Ref. 2; AAD41634)"
FT /evidence="ECO:0000305"
FT CONFLICT 2561
FT /note="F -> S (in Ref. 2; AAD41634)"
FT /evidence="ECO:0000305"
FT CONFLICT 2802
FT /note="D -> N (in Ref. 2; AAD41634)"
FT /evidence="ECO:0000305"
FT CONFLICT 2805
FT /note="R -> K (in Ref. 2; AAD41634)"
FT /evidence="ECO:0000305"
FT CONFLICT 2920..2936
FT /note="AFNIDFNRWHYEHQNRY -> LLI (in Ref. 2; AAD41634)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2936 AA; 326743 MW; A6CFD90CA666CEA4 CRC64;
MASDKPGPGL EPQPVALLAV GAGGGAGGGG AMGEPRGAAG SGPVVLPAGM INPSVPIRNI
RMKFAVLIGL IQVGEVSNRD IVETVLNLLV GGEFDLEMNF IIQDAESITC MTELLEHCDV
TCQAEIWSMF TAILRKSVRN LQTSTEVGLI EQVLLKMSAV DDMIADLLVD MLGVLASYSI
TVKELKLLFS MLRGESGIWP RHAVKLLSVL NQMPQRHGPD TFFNFPGCSA AAIALPPIAK
WPYQNGFTLN TWFRMDPLNN INVDKDKPYL YCFRTSKGVG YSAHFVGNCL IVTSLKSKGK
GFQHCVKYDF QPRKWYMISI VHIYNRWRNS EIRCYVNGQL VSYGDMAWHV NTNDSYDKCF
LGSSETADAN RVFCGQLGAV YVFSEALNPA QIFAVHQLGP GYKSTFKFKS ESDIHLAEHH
KQVLYDGKLA SSIAFSYNAK ATDAQLCLES SPKENASIFV HSPHALMLQD VKAIVTHSIH
SAIHSIGGIQ VLFPLFAQLD NRQLNDSQVE TTVCATLLAF LVELLKSSVA MQEQMLGGKG
FLVIGYLLEK SSRVHITRAV LEQFLSFAKY LDGLSHGAPL LKQLCDHILF NPAIWIHTPA
KVQLSLYTYL SAEFIGTATI YTTIRRVGTV LQLMHTLKYY YWVINPADSS GIAPKGLDGP
RPSQKEIISL RAFMLLFLKQ LILKDRGVKE DELQSILNYL LTMHEDENIH DVLQLLVALM
SEHPASMIPA FDQRNGIRVI YKLLASKSES IWVQALKVLG YFLKHLGHKR KVEIMHTHSL
FTLLGERLML HTNTVTVTTY NTLYEILTEQ VCTQVVHKPH PEPDSTVKIQ NPMILKVVAT
LLKNSTPSAE LMEVRRLFLS DMIKLFSNSR ENRRCLLQCS VWQDWMFSLG YINPKSSEEQ
KITEMVYNIF RILLYHAIKY EWGGWRVWVD TLSIAHSKVT YEAHKEYLAK MYEEYQRQEE
ENIKKGKKGN VSTISGLSSQ TAGAKGGMEI REIEDLSQSQ SPESETDYPV STDTRDLLMS
TKVSDDILGS SDRPGSGVHV EVHDLLVDIK AEKVEATEVK LDDMDLSPET LVGGENGALV
EVESLLDNVY SAAVEKLQNN VHGSVGIIKK NEEKDNGPLI TLADEKEELP NSSTPFLFDK
IPRQEEKLLP ELSSNHIIPN IQDTQVHLGV SDDLGLLAHM TASVELTCTS SIMEEKDFRI
HTTSDGVSSV SERELASSTK GLDYAEMTAT TLETESSNSK AVPNVDAGSI ISDTERSDDG
KESGKEIRKI QTTATTQAVQ GRSSTQQDRD LRVDLGFRGM PMTEEQRRQF SPGPRTTMFR
IPEFKWSPMH QRLLTDLLFA LETDVHVWRS HSTKSVMDFV NSNENIIFVH NTIHLISQMV
DNIIIACGGI LPLLSAATSP TGSKTELENI EVTQGMSAET AVTFLSRLMA MVDVLVFASS
LNFSEIEAEK NMSSGGLMRQ CLRLVCCVAV RNCLECRQRQ RDRGSKSSHG SSKPQEAPHS
VTAASASKTP LENVPGNLSP IKDPDRLLQD VDINRLRAVV FRDVDDSKQA QFLALAVVYF
ISVLMVSKYR DILEPQRETA RTGSQPGRNI RQEINSPTST VVVIPSIPHP SLNHGLLAKL
MPEQSFAHSF YKETPATFPD TVKEKETPTP GEDIQLESSV PHTDSGMGEE QVASILDGAE
LEPAAGPDAM SELLSTLSSE VKKSQESLTE HPSEMLKPAP SISSISQTKG INVKEILKSL
VAAPVEIAEC GPEPIPYPDP ALKREAHAIL PMQFHSFDRS VVVPVKKPPP GSLAVTTVGA
TAAGSGLPTG STSSIFAAPG ATPKSMINTT GAVDSGSSSS SSSSSFVNGA TSKNLPAVQT
VAPMPEDSAE NMSITAKLER ALEKVAPLLR EIFVDFAPFL SRTLLGSHGQ ELLIEGLVCM
KSSTSVVELV MLLCSQEWQN SIQKNAGLAF IELINEGRLL CHAMKDHIVR VANEAEFILN
RQRAEDVHKH AEFESQCAQY AADRREEEKM CDHLISAAKH RDHVTANQLK QKILNILTNK
HGAWGAVSHS QLHDFWRLDY WEDDLRRRRR FVRNAFGSTH AEALLKSAVE YGTEEDVVKS
KKAFRSQAIV NQNSETELML EGDDDAVSLL QEKEIDNLAG PVVLSTPAQL IAPVVVAKGT
LSITTTEIYF EVDEDDAAFK KIDTKVLAYT EGLHGKWMFS EIRAVFSRRY LLQNTALEVF
MANRTSVMFN FPDQATVKKV VYSLPRVGVG TSYGLPQARR ISLATPRQLY KSSNMTQRWQ
RREISNFEYL MFLNTIAGRT YNDLNQYPVF PWVLTNYESE ELDLTLPGNF RDLSKPIGAL
NPKRAVFYAE RYETWEEDQS PPFHYNTHYS TATSALSWLV RIEPFTTFFL NANDGKFDHP
DRTFSSIARS WRTSQRDTSD VKELIPEFYY LPEMFVNSNG YHLGVREDEV VVNDVDLPPW
AKKPEDFVRI NRMALESEFV SCQLHQWIDL IFGYKQRGPE AVRALNVFHY LTYEGSVNLD
SITDPVLREA MEAQIQNFGQ TPSQLLIEPH PPRSSAMHLC FLPQSPLMFK DQMQQDVIMV
LKFPSNSPVT HVAANTLPHL TIPAVVTVTC SRLFAVNRWH NTVGLRGAPG YSLDQAHHLP
IEMDPLIANN SGVNKRQITD LVDQSIQINA HCFVVTADNR YILICGFWDK SFRVYSTETG
KLTQIVFGHW DVVTCLARSE SYIGGDCYIV SGSRDATLLL WYWSGRHHII GDNPNSSDYP
APRAVLTGHD HEVVCVSVCA ELGLVISGAK EGPCLVHTIT GDLLRALEGP ENCLFPRLIS
VSSEGHCIIY YERGRFSNFS INGKLLAQME INDSTRAILL SSDGQNLVTG GDNGVVEVWQ
ACDFKQLYIY PGCDAGIRAM DLSHDQRTLI TGMASGSIVA FNIDFNRWHY EHQNRY
