WDR81_MOUSE
ID WDR81_MOUSE Reviewed; 1934 AA.
AC Q5ND34; G5E8V0; Q3TA90; Q3TUS9; Q6KAR1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=WD repeat-containing protein 81 {ECO:0000312|MGI:MGI:2681828};
GN Name=Wdr81 {ECO:0000312|MGI:MGI:2681828};
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1042-1934 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1120-1934 (ISOFORM 3), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1228-1934 (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryonic liver, and Spleen;
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]
RP IDENTIFICATION BY 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, 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).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=21885617; DOI=10.1101/gr.126110.111;
RA Gulsuner S., Tekinay A.B., Doerschner K., Boyaci H., Bilguvar K., Unal H.,
RA Ors A., Onat O.E., Atalar E., Basak A.N., Topaloglu H., Kansu T., Tan M.,
RA Tan U., Gunel M., Ozcelik T.;
RT "Homozygosity mapping and targeted genomic sequencing reveal the gene
RT responsible for cerebellar hypoplasia and quadrupedal locomotion in a
RT consanguineous kindred.";
RL Genome Res. 21:1995-2003(2011).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP LEU-1349.
RX PubMed=23595742; DOI=10.1523/jneurosci.2394-12.2013;
RA Traka M., Millen K.J., Collins D., Elbaz B., Kidd G.J., Gomez C.M.,
RA Popko B.;
RT "WDR81 is necessary for Purkinje and photoreceptor cell survival.";
RL J. Neurosci. 33:6834-6844(2013).
RN [8]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=28404643; DOI=10.1083/jcb.201608039;
RA Liu X., Li Y., Wang X., Xing R., Liu K., Gan Q., Tang C., Gao Z., Jian Y.,
RA Luo S., Guo W., Yang C.;
RT "The BEACH-containing protein WDR81 coordinates p62 and LC3C to promote
RT aggrephagy.";
RL J. Cell Biol. 216:1301-1320(2017).
CC -!- FUNCTION: Functions as a negative regulator of the PI3 kinase/PI3K
CC activity associated with endosomal membranes via BECN1, a core subunit
CC of the PI3K complex. By modifying the phosphatidylinositol 3-
CC phosphate/PtdInsP3 content of endosomal membranes may regulate endosome
CC fusion, recycling, sorting and early to late endosome transport. It is
CC for instance, required for the delivery of cargos like BST2/tetherin
CC from early to late endosome and thereby participates indirectly to
CC their degradation by the lysosome. May also play a role in aggrephagy,
CC the macroautophagic degradation of ubiquitinated protein aggregates. In
CC this process, may regulate the interaction of SQSTM1 with ubiquitinated
CC proteins and also recruit MAP1LC3C (By similarity). May also be
CC involved in maintenance of normal mitochondrial structure and
CC organization (PubMed:23595742). {ECO:0000250|UniProtKB:Q562E7,
CC ECO:0000269|PubMed:23595742}.
CC -!- SUBUNIT: Interacts with WDR91; involved in early to late endosome cargo
CC transport. Interacts with BECN1; negatively regulates the PI3
CC kinase/PI3K activity associated with endosomal membranes. Interacts
CC with SQSTM1; the interaction is direct and regulates the interaction of
CC SQSTM1 with ubiquitinated proteins. Interacts with MAP1LC3C; recruits
CC MAP1LC3C to ubiquitinated protein aggregates in the aggrephagy process.
CC {ECO:0000250|UniProtKB:Q562E7}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000250|UniProtKB:Q562E7}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q562E7}. Late endosome membrane
CC {ECO:0000250|UniProtKB:Q562E7}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q562E7}. Cytoplasmic vesicle, autophagosome
CC membrane {ECO:0000250|UniProtKB:Q562E7}. Mitochondrion
CC {ECO:0000269|PubMed:23595742}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q562E7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5ND34-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5ND34-2; Sequence=VSP_019956;
CC Name=3;
CC IsoId=Q5ND34-3; Sequence=VSP_019957;
CC -!- TISSUE SPECIFICITY: Expressed in brain, Purkinje cells of cerebellum,
CC retinal photoreceptor cells and spinal cord (at protein level)
CC (PubMed:23595742). In brain, specifically expressed by neuronal cells
CC (at protein level). Detected in a wide range of tissues including
CC intestine, adipose tissue, liver, pancreas, thymus, spleen, kidney,
CC heart, eye, sciatic nerve, and testis (PubMed:21885617,
CC PubMed:23595742, PubMed:28404643). {ECO:0000269|PubMed:21885617,
CC ECO:0000269|PubMed:23595742, ECO:0000269|PubMed:28404643}.
CC -!- DISRUPTION PHENOTYPE: Brain-specific, conditional knockout mice are
CC born at the expected Mendelian frequency, but most of them die a few
CC hours after birth. If they show no overt brain morphological
CC abnormalities, a neuronal accumulation of SQSTM1 in foci is observed.
CC {ECO:0000269|PubMed:28404643}.
CC -!- SIMILARITY: Belongs to the WD repeat WDR81 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD21396.1; Type=Erroneous translation; Note=Incomplete prediction of CDS at the C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL591496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK131146; BAD21396.1; ALT_SEQ; mRNA.
DR EMBL; AK160585; BAE35892.1; -; mRNA.
DR EMBL; AK172019; BAE42779.1; -; mRNA.
DR CCDS; CCDS48849.1; -. [Q5ND34-1]
DR RefSeq; NP_620400.2; NM_138950.2. [Q5ND34-1]
DR RefSeq; XP_006532611.1; XM_006532548.3. [Q5ND34-3]
DR AlphaFoldDB; Q5ND34; -.
DR SMR; Q5ND34; -.
DR BioGRID; 228693; 3.
DR IntAct; Q5ND34; 1.
DR STRING; 10090.ENSMUSP00000134266; -.
DR iPTMnet; Q5ND34; -.
DR PhosphoSitePlus; Q5ND34; -.
DR CPTAC; non-CPTAC-3495; -.
DR EPD; Q5ND34; -.
DR jPOST; Q5ND34; -.
DR MaxQB; Q5ND34; -.
DR PaxDb; Q5ND34; -.
DR PeptideAtlas; Q5ND34; -.
DR PRIDE; Q5ND34; -.
DR ProteomicsDB; 299754; -. [Q5ND34-1]
DR ProteomicsDB; 299755; -. [Q5ND34-2]
DR ProteomicsDB; 299756; -. [Q5ND34-3]
DR Antibodypedia; 10606; 17 antibodies from 10 providers.
DR Ensembl; ENSMUST00000173320; ENSMUSP00000134266; ENSMUSG00000045374. [Q5ND34-1]
DR GeneID; 192652; -.
DR KEGG; mmu:192652; -.
DR UCSC; uc007kdu.2; mouse. [Q5ND34-3]
DR UCSC; uc011xzj.1; mouse. [Q5ND34-1]
DR CTD; 124997; -.
DR MGI; MGI:2681828; Wdr81.
DR VEuPathDB; HostDB:ENSMUSG00000045374; -.
DR eggNOG; KOG1786; Eukaryota.
DR eggNOG; KOG4190; Eukaryota.
DR GeneTree; ENSGT00930000151039; -.
DR HOGENOM; CLU_001454_0_0_1; -.
DR InParanoid; Q5ND34; -.
DR OMA; AYEQFTP; -.
DR OrthoDB; 101142at2759; -.
DR TreeFam; TF323353; -.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR BioGRID-ORCS; 192652; 6 hits in 73 CRISPR screens.
DR PRO; PR:Q5ND34; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5ND34; protein.
DR Bgee; ENSMUSG00000045374; Expressed in ileal epithelium and 227 other tissues.
DR ExpressionAtlas; Q5ND34; baseline and differential.
DR Genevisible; Q5ND34; MM.
DR GO; GO:0000421; C:autophagosome membrane; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0031313; C:extrinsic component of endosome membrane; ISS:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0035014; F:phosphatidylinositol 3-kinase regulator activity; ISS:UniProtKB.
DR GO; GO:0035973; P:aggrephagy; ISS:UniProtKB.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0043551; P:regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR CDD; cd06071; Beach; 1.
DR Gene3D; 1.10.1540.10; -; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR000409; BEACH_dom.
DR InterPro; IPR036372; BEACH_dom_sf.
DR InterPro; IPR011009; Kinase-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; PF00400; WD40; 1.
DR SMART; SM01026; Beach; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF81837; SSF81837; 1.
DR PROSITE; PS50197; BEACH; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle; Endosome; Lysosome;
KW Membrane; Mitochondrion; Reference proteome; Repeat; Transit peptide;
KW WD repeat.
FT CHAIN 1..1934
FT /note="WD repeat-containing protein 81"
FT /id="PRO_0000247245"
FT DOMAIN 335..612
FT /note="BEACH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00026"
FT REPEAT 1639..1678
FT /note="WD 1"
FT REPEAT 1685..1725
FT /note="WD 2"
FT REPEAT 1777..1816
FT /note="WD 3"
FT REPEAT 1819..1857
FT /note="WD 4"
FT REPEAT 1904..1934
FT /note="WD 5"
FT REGION 1..645
FT /note="Necessary and sufficient for the interaction with
FT SQSTM1"
FT /evidence="ECO:0000250|UniProtKB:Q562E7"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1018..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1515..1544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1562..1599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1169
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1562..1590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1457..1490
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15449545"
FT /id="VSP_019956"
FT VAR_SEQ 1769..1828
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019957"
FT MUTAGEN 1349
FT /note="L->P: Progressive ataxia associated with Purkinje
FT cell death. Retinal thinning due to photoreceptor cell
FT death."
FT /evidence="ECO:0000269|PubMed:23595742"
SQ SEQUENCE 1934 AA; 211945 MW; 8BE776A85B11C8AB CRC64;
MAQGSRRRKV VLTAGSEGWS PSSGPDMEEL LRSVERDLNI DARQLALAPG GTHVVALVST
RWLASLRERR LGPCPRAEGL GEAEVRTLLQ RSVQRLPPGW TRVEVHGLRK RRLSYPLGGG
VPFEEGSCSP ETLTRFMQEV AAQNYRNLWR HAYHTYGQPY SHSTAPSALP ALDSIRQALQ
RVYGCTFLPV GESIPCLSNV RDGPCPSRGS PACPSLLRAE ALLESPEMLY VVHPYVQFSL
HDVVTFSPAK LTNSQAKVLF LLFRVLRAMD ACHRQGLACG ALSLHHIAVD EKLCSELRLD
LSAYEMPSED ENQEGSEEKN GTGIKSEKEG EGRTECPTCQ KELRGLVLDW VHGRISNFHY
LMQLNRLAGR RQGDPNYHPV LPWVVDFTTP YGRFRDLRKS KFRLNKGDKQ LDFTYEMTRQ
AFVAGGAGSG EPPHVPHHIS DVLSDITYYV YKARRTPRSV LCGHVRAQWE PHEYPATMER
MQTWTPDECI PEFYTDPSIF CSIHPDMPDL DVPAWCSSNQ EFVAAHRALL ESWEVSQDLH
HWIDLTFGYK LQGKEAVKEK NVCLHLVDAH THLTSYGVVQ LFDQPHPQRL AGSPALAPEP
PLIPRLLVQP IREATGQEDI SGQLINGAGR LVVEATPCET GWTRDRPGTG EDDLEQATEA
LDSISLPGKA GDQPGSSSSQ ASPGLLSFSA PSGSRPGRRS KAAGLDPGEG EEGKIVLPEG
FSPIQALEEL EKVGNFLAKG LGSQLEEPEK PHAQPPVHLQ SLFHRDMQVL GVLLAEMVFA
TRVRILQPDA PLWVRFEAVR GLCIRHSKDI PVSLQPVLDT LLQLSGPKSP MVSKKGKLDP
LFEYRPVSQG LPPPSPAQLL SPFSSVVPFP PYFPALHKFI LLYQARRVED EVQGRELAFA
LWQQLGAVLN DITPEGLEIL LPFVLSLMSE EHTAVYTAWY LFEPVAKALG PKNANKYLLK
PLIGAYESPC RLHGRFYLYT DCFVAQLVVR LGLQAFLTHL LPHVLQVLAG VEASQEEGKG
LVGTTEDEES ELPVSGPGSC AFGEEIQMDG QPAASSGLGL PDYRSGVSFH DQADLPDTED
FQAGLYVAES PQPQEAEAVS LGQLSDKSST SEASQGEERG GDDGGAPADK NSVKSGDSSQ
DLKQSEGSEE EEEEEGCVVL EEDQEDEVTG TSELTLSDTM LSMETVVAPG DGRDREEEEE
PLTEQTEGKE QKILLDTACK MVRWLSAKLG PTVASRHVAR NLLRLLTSCY VGPTRQQFTV
SSDDTPPLNA GNIYQKRPVL GDIVSGPVLS CLLHIAYLYG EPVLTYQYLP YISYLVAPGS
NSNPSRLNSR KEAGLLAAVT LTQKIIVYLS DTTLMDILPR ISHEVLLPVL GFLTSFVTGF
PSGAQARTVL CVKTISLIAL ICLRIGQEMV QQHLSEPVAT FFQVFSHLHE LRQQDLPLDP
KGCTEGQLPE ATFSDGQRRP VDPTLLEELQ KVFTLEMAYT IYVPFSCLLG DIIRKIIPNH
ELVGELAGLY LESMSPSSRN PASMEPTMAS AGPEWDPQSG SCLQDDGHSG TFGSVLVGNR
IQIPDSQPQS PGPLGSLSGV GSSGGLSNRN EDNALKRELP RSAHGLSGNW LAYWQYEIGV
SQQDAHFHFH QIRLQSFPGH TGAVKCVAAL SSEDFFLSGS KDRTVRLWPL YNYGDGTNET
ASRLIYAQHR KSVFYVGQLE APQYVVSCDG AVHVWDPFTG KTLRTVDPSD SRVPLTAVAV
MPAPHTSITM ASSDSTLRFV DCRKPGLQHE FRLGGGLNPG LVRSLAVSPS GRSVVAGFSS
GFMVLLDTRT GLVLRGWPAH EGDILQIKAV EGSVLISSSS DHSLTVWKEL EQKPTHHYKS
ASDPIHTFDL YGSEVVTGTV ANKIGVCSLL EPPSQATTKL SSENFRGTLT SLALLPTKRH
LLLGSDNGII RLLA
