DLG5_MOUSE
ID DLG5_MOUSE Reviewed; 1921 AA.
AC E9Q9R9; Q3UGX5;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Disks large homolog 5;
GN Name=Dlg5;
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 MRNA].
RC STRAIN=C57BL/6J;
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 [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264; THR-984 AND SER-1263,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Kidney;
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH CTNB1,
RP AND VARIANT PRO-1642.
RX PubMed=25232112; DOI=10.1523/jneurosci.1280-14.2014;
RA Wang S.H., Celic I., Choi S.Y., Riccomagno M., Wang Q., Sun L.O.,
RA Mitchell S.P., Vasioukhin V., Huganir R.L., Kolodkin A.L.;
RT "Dlg5 regulates dendritic spine formation and synaptogenesis by controlling
RT subcellular N-cadherin localization.";
RL J. Neurosci. 34:12745-12761(2014).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KIF7 AND SMO.
RX PubMed=25644602; DOI=10.1101/gad.252676.114;
RA Chong Y.C., Mann R.K., Zhao C., Kato M., Beachy P.A.;
RT "Bifurcating action of Smoothened in Hedgehog signaling is mediated by
RT Dlg5.";
RL Genes Dev. 29:262-276(2015).
RN [6]
RP FUNCTION, AND INTERACTION WITH STK3; STK4 AND MARK3.
RX PubMed=28087714; DOI=10.1101/gad.284539.116;
RA Kwan J., Sczaniecka A., Arash E.H., Nguyen L., Chen C.C., Ratkovic S.,
RA Klezovitch O., Attisano L., McNeill H., Emili A., Vasioukhin V.;
RT "DLG5 connects cell polarity and Hippo signaling protein networks by
RT linking PAR-1 with MST1/2.";
RL Genes Dev. 30:2696-2709(2016).
CC -!- FUNCTION: Acts as a regulator of the Hippo signaling pathway.
CC Negatively regulates the Hippo signaling pathway by mediating the
CC interaction of MARK3 with STK3/4, bringing them together to promote
CC MARK3-dependent hyperphosphorylation and inactivation of STK3 kinase
CC activity toward LATS1 (PubMed:28087714). Positively regulates the Hippo
CC signaling by mediating the interaction of SCRIB with STK4/MST1 and
CC LATS1 which is important for the activation of the Hippo signaling
CC pathway. Involved in regulating cell proliferation, maintenance of
CC epithelial polarity, epithelial-mesenchymal transition (EMT), cell
CC migration and invasion (By similarity). Plays an important role in
CC dendritic spine formation and synaptogenesis in cortical neurons;
CC regulates synaptogenesis by enhancing the cell surface localization of
CC N-cadherin (PubMed:25232112). Acts as a positive regulator of hedgehog
CC (Hh) signaling pathway. Plays a critical role in the early point of the
CC SMO activity cycle by interacting with SMO at the ciliary base to
CC induce the accumulation of KIF7 and GLI2 at the ciliary tip for GLI2
CC activation (PubMed:25644602). {ECO:0000250|UniProtKB:Q8TDM6,
CC ECO:0000269|PubMed:25232112, ECO:0000269|PubMed:25644602,
CC ECO:0000269|PubMed:28087714}.
CC -!- SUBUNIT: Interacts with MPP1. Interacts with CTNNB1 and with the third
CC SH3 domain of SORBS3 to form a ternary complex (By similarity).
CC Interacts (via coiled-coil domain) with MARK3. Interacts (via PDZ
CC domain 3) with STK3/MST2 and STK4/MST1 (PubMed:28087714). Interacts
CC with SCRIB (By similarity). Interacts with CTNB1 (PubMed:25232112).
CC Interacts with SMO and (via PDZ4 or guanylate kinase-like domain) with
CC KIF7 (PubMed:25644602). {ECO:0000250|UniProtKB:Q8TDM6,
CC ECO:0000269|PubMed:25232112, ECO:0000269|PubMed:25644602,
CC ECO:0000269|PubMed:28087714}.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000250|UniProtKB:Q8TDM6}.
CC Cell membrane {ECO:0000250|UniProtKB:Q8TDM6}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q8TDM6}. Postsynaptic density
CC {ECO:0000269|PubMed:25232112}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:25644602}. Note=Localized at sites of cell-
CC cell contact. {ECO:0000250|UniProtKB:Q8TDM6}.
CC -!- TISSUE SPECIFICITY: Brain (at protein level).
CC {ECO:0000269|PubMed:25232112}.
CC -!- DOMAIN: The guanylate kinase-like domain interacts with the SH3 domain.
CC {ECO:0000269|PubMed:25232112}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; AK147699; BAE28082.1; -; mRNA.
DR EMBL; AC163638; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS49417.1; -.
DR RefSeq; NP_001156985.1; NM_001163513.1.
DR RefSeq; NP_082002.1; NM_027726.1.
DR AlphaFoldDB; E9Q9R9; -.
DR SMR; E9Q9R9; -.
DR STRING; 10090.ENSMUSP00000087879; -.
DR iPTMnet; E9Q9R9; -.
DR PhosphoSitePlus; E9Q9R9; -.
DR MaxQB; E9Q9R9; -.
DR PaxDb; E9Q9R9; -.
DR PRIDE; E9Q9R9; -.
DR ProteomicsDB; 279724; -.
DR Antibodypedia; 618; 103 antibodies from 18 providers.
DR DNASU; 71228; -.
DR Ensembl; ENSMUST00000090398; ENSMUSP00000087879; ENSMUSG00000021782.
DR GeneID; 71228; -.
DR KEGG; mmu:71228; -.
DR UCSC; uc007sqg.1; mouse.
DR CTD; 9231; -.
DR MGI; MGI:1918478; Dlg5.
DR VEuPathDB; HostDB:ENSMUSG00000021782; -.
DR eggNOG; KOG0708; Eukaryota.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00940000155303; -.
DR HOGENOM; CLU_002448_1_0_1; -.
DR InParanoid; E9Q9R9; -.
DR OMA; QEHYMAD; -.
DR OrthoDB; 123652at2759; -.
DR PhylomeDB; E9Q9R9; -.
DR TreeFam; TF323171; -.
DR Reactome; R-MMU-9013420; RHOU GTPase cycle.
DR Reactome; R-MMU-9013424; RHOV GTPase cycle.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 71228; 4 hits in 70 CRISPR screens.
DR ChiTaRS; Dlg5; mouse.
DR PRO; PR:E9Q9R9; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; E9Q9R9; protein.
DR Bgee; ENSMUSG00000021782; Expressed in placenta labyrinth and 245 other tissues.
DR ExpressionAtlas; E9Q9R9; baseline and differential.
DR Genevisible; E9Q9R9; MM.
DR GO; GO:0005912; C:adherens junction; IDA:MGI.
DR GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
DR GO; GO:0045176; P:apical protein localization; IMP:MGI.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IMP:MGI.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IMP:MGI.
DR GO; GO:0030011; P:maintenance of cell polarity; ISS:UniProtKB.
DR GO; GO:0072205; P:metanephric collecting duct development; IMP:MGI.
DR GO; GO:0030901; P:midbrain development; IMP:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0035331; P:negative regulation of hippo signaling; IMP:UniProtKB.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISS:UniProtKB.
DR GO; GO:0060563; P:neuroepithelial cell differentiation; IMP:MGI.
DR GO; GO:0030859; P:polarized epithelial cell differentiation; IMP:MGI.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:UniProtKB.
DR GO; GO:0035332; P:positive regulation of hippo signaling; ISS:UniProtKB.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IMP:UniProtKB.
DR GO; GO:0071896; P:protein localization to adherens junction; IMP:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0045186; P:zonula adherens assembly; IMP:MGI.
DR CDD; cd11860; SH3_DLG5; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 2.30.42.10; -; 4.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR035537; DLG5_SH3.
DR InterPro; IPR006907; DUF622.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 3.
DR Pfam; PF04822; Takusan; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 4.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 4.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50209; CARD; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 4.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Membrane; Phosphoprotein; Reference proteome; SH3 domain;
KW Synapse.
FT CHAIN 1..1921
FT /note="Disks large homolog 5"
FT /id="PRO_0000440556"
FT DOMAIN 1..90
FT /note="CARD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT DOMAIN 620..710
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 705..796
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1350..1429
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1504..1585
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1596..1664
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1724..1907
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 116..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1204..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1243..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1280..1343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1434..1501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 139..601
FT /evidence="ECO:0000255"
FT COMPBIAS 866..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1060
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1434..1462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1481..1496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDM6"
FT MOD_RES 900
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDM6"
FT MOD_RES 984
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1000
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDM6"
FT MOD_RES 1011
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDM6"
FT MOD_RES 1021
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDM6"
FT MOD_RES 1183
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDM6"
FT MOD_RES 1209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDM6"
FT MOD_RES 1263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDM6"
FT MOD_RES 1669
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDM6"
FT VARIANT 1642
FT /note="L -> P (in allele LP; loss of neuronal function and
FT disruption of interactions between the SH3 and guanylate
FT kinase-like domains)"
FT /evidence="ECO:0000269|PubMed:25232112"
FT CONFLICT 946
FT /note="T -> P (in Ref. 1; BAE28082)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1921 AA; 214386 MW; 0B2C62F913B3B26E CRC64;
MEPQRRELLA QCQQSLAQAM TEVEAVLGLL EAAGALSPGE RRQLDEEAGG AKAELLLQLL
LAKEQDHFQD LRAALEKTQP HLLPILYLNG VVGPPQSTEG AGSTYSVLSI MPSDSESSSS
LSSVGTTGKA PSPPPLLTEQ QANDTVENLS IQLRLMTRER NELRKRLAFA THGATFDKRP
YHRLNPDYER LKIQCVRAMS DLQSLQNQHT NALKRCEEVA KETDFYHTLH SRLLSDQTQL
KDDVDMLRRE NGKLRRERNL LQQSWEDMKR LREEDQKEIG DLRAQQQQVL KHNGSSEILN
KLYDTAMDKL EVVKKDYDAL RKRYSEKVAM HNSDLSRLEQ LGEENQRLQK QTEMLTQQRD
TAIQLQHQCA LSLRRFETIH HELSKATAQN KDLQWEMELL QSELTELRSK QVKTAKESEK
YKEERDAVYS EYKLIMSERD QVISELDKLQ TEVELAESKL KSSTSEKKAA SEEMEALRQI
KDTVTMDAGR ANKEVEILRK QCKALCQELK EALQEADVAK CRRDWAFQER DKIVAERDSI
RTLCDNLRRE RDRAVSELAE ALRSLDDTRK QKNDVSRELK ELKEQMECQL EKEARFRQLM
AHSSHDSAID TDSMEWETEV VEFERETEDI DLKALGFDMA EGVNEPCFPG DCGIFVTKVD
KGSIADGRLR VNDWLLRIND VDLINKDKKQ AIKALLNGEG AINMVVRRRK SLGGKVVTPL
HINLSGQKDS GISLENGVYA AAVVPGSPAA KEGSLAVGDR IVAINGIALD NKSLNECESL
LRSCQDSLTL SLLKVFPQSS SWSGQNIFEN IKDSDRMLSC RAHGPEVQAH NKRNLLQHNN
STQTDIFYTD RLEDRKELGH SGGSSSFLHK PFSGSSSPVS PQACPSTSER SLNSFRSDTS
AERGYGLVDM RSQRPLLSFE TEVGPCGAVE VPLDKIDPEG SNSGGTWPKA VLGSTSGPEK
LSVYKKPKQR KSIFDPNTFK RPQTPPKIDY LLPGPGLTHS PQPSKRVGSL TPPKPPRRSD
SIKFQHRLET SSESEATLVG SSPSTSPPSA PPPSMDPSEP THASPPRKAR VRIASSYHSE
GDGDTSYLPA KKPCDEDLTS QKVDELGQKR RRPKSAPSFR PKISPVVIPA QCLEEQECVP
AIGELSPEGQ EWSPYSPGHA SRHGNPLLYP NRPSVGTVPR SMTPGTTVGS ILRNPIYTVR
SHRVLPCGSP PVPRDAGSQS LSPSVQHQGR LSLDLSHRAC SDYSEMRASQ GSNSLPSSAR
LGSSSNLQFK AERIKIPLTP RYPRSVMGSD RGSLSHSECS TPPRSPLNID TLSSCSQPQT
TASTLPRIAV NPSSHGERRK DRPFVEEPRH VKVQKGSEPL GISIVSGEKG GVYVSKVTLG
SIAHQAGLEY GDQLLEFNGI NLRSATEQQA RLIIGQQCDT ITILAQYNPH IHQLNSHSRS
SSHLDPAATP HSTLQGSSAG TPEHPSVIDP LMEQDEGPGT PPAKQSASST RSVGDTTKKT
PDPRIVFIKK SQLDLGVHLC GGNLHGVFVA EVEDDSPAKG PDGLVPGDLI LEYGSLDMRS
RTVEDVYVEM LKPKDSLRLK VQYRHEEFTR VKGLPGDSFY IRALYDRLAE VEPELSFKKD
DILYVDDTLP QGVFGSWMAW QLDENAQKIQ RGQIPSKYVM DQEFSRRLSM SEVKDDNTAK
TLSAAARRSF FRRKHKHKRS GSKDGKDLLA LDTFSNDSIP LFEDSVSLAY QRVQKVDCTS
LRPVLLLGPL LDVVKEMLVN EAPGKFCRCP LEVMKASQQA IERGVKDCLF VDYKRRSGHF
DVTTVASIKE ITEKNRHCLL DIAPHAIERL HHMHIYPIVI FIRYKSAKHI KEQRDPVYLR
DKVTQRHSKE QFETAQKIDQ EYSRYFTGVV QGGALSSICT QILAMVSQEQ SKVLWIPACP
P
