MESH_DROME
ID MESH_DROME Reviewed; 1454 AA.
AC Q0KHY3; B3DNA3; E1JJ26; E1JJ27; E2QD49; Q6NND0; Q8MR59;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Protein mesh;
DE Flags: Precursor;
GN Name=mesh; ORFNames=CG31004;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Booth B., Chavez C., Frise E., George R.A.,
RA Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 217-1431 (ISOFORM 1).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-888, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1249; THR-1251; SER-1254;
RP THR-1295 AND SER-1297, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [7]
RP FUNCTION, INTERACTION WITH SSK, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=22854041; DOI=10.1242/jcs.112243;
RA Izumi Y., Yanagihashi Y., Furuse M.;
RT "A novel protein complex, Mesh-Ssk, is required for septate junction
RT formation in the Drosophila midgut.";
RL J. Cell Sci. 125:4923-4933(2012).
RN [8]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH SSK AND TSP2A, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=26848177; DOI=10.1242/jcs.180448;
RA Izumi Y., Motoishi M., Furuse K., Furuse M.;
RT "A tetraspanin regulates septate junction formation in Drosophila midgut.";
RL J. Cell Sci. 129:1155-1164(2016).
CC -!- FUNCTION: Required, together with Ssk and Tsp2A, for the proper
CC organization of smooth septate junctions (sSJs), probably by mediating
CC cell adhesion via its homophilic interaction (PubMed:22854041,
CC PubMed:26848177). Also required for the correct subcellular
CC localization of several sSJ components, such as Ssk, cora and l(2)gl,
CC and for the barrier function of the midgut epithelium
CC (PubMed:22854041). Required for maintaining the three-layered structure
CC of the proventriculus (PubMed:22854041). {ECO:0000269|PubMed:22854041}.
CC -!- SUBUNIT: Forms a complex with Ssk and Tsp2A (PubMed:26848177).
CC Interacts with Ssk; the interaction may be necessary for the
CC localization of both proteins to the cell apicolateral region
CC (PubMed:22854041). {ECO:0000269|PubMed:22854041,
CC ECO:0000269|PubMed:26848177}.
CC -!- SUBCELLULAR LOCATION: Cell junction, septate junction
CC {ECO:0000269|PubMed:22854041, ECO:0000269|PubMed:26848177}.
CC Apicolateral cell membrane {ECO:0000269|PubMed:22854041,
CC ECO:0000269|PubMed:26848177}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:22854041}. Note=Colocalizes with Ssk, cora, dlg1,
CC l(2)gl and Fas3 at the apicolateral region of epithelial cells in the
CC midgut. Also localizes to the apicolateral region of epithelial cells
CC in the outer epithelial layer of the proventriculus and Malpighian
CC tubules.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3; Synonyms=D;
CC IsoId=Q0KHY3-3; Sequence=Displayed;
CC Name=1; Synonyms=B;
CC IsoId=Q0KHY3-1; Sequence=VSP_053282;
CC Name=2; Synonyms=C;
CC IsoId=Q0KHY3-2; Sequence=VSP_035956;
CC -!- TISSUE SPECIFICITY: At embryonic stage 12, expressed in endoderm-
CC derived tissues (at protein level) (PubMed:22854041). In late-stage
CC embryos, third-instar larvae and adult flies, expressed in the midgut,
CC outer epithelial layer of the proventriculus and Malpighian tubules,
CC but not expressed in the foregut and hindgut (at protein level)
CC (PubMed:22854041, PubMed:26848177). {ECO:0000269|PubMed:22854041,
CC ECO:0000269|PubMed:26848177}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic, larval and adult
CC stages (at protein level). {ECO:0000269|PubMed:22854041}.
CC -!- DISRUPTION PHENOTYPE: Homozygous larval lethal. Mutant embryos hatch
CC into the first instar larvae, but die within 1 day. In mutant larvae
CC midgut, a few septa are present at the cell contacts but large gaps
CC between the lateral membranes of adjacent epithelial cells are
CC frequently observed. Mutant larvae lack the three-layered structure of
CC the proventriculus. {ECO:0000269|PubMed:22854041}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM52621.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAR96152.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE014297; AAF57124.2; -; Genomic_DNA.
DR EMBL; AE014297; ACZ95074.1; -; Genomic_DNA.
DR EMBL; AE014297; ACZ95075.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF57123.2; -; Genomic_DNA.
DR EMBL; BT032891; ACD99455.1; -; mRNA.
DR EMBL; BT133164; AEZ02857.1; -; mRNA.
DR EMBL; BT011360; AAR96152.1; ALT_FRAME; mRNA.
DR EMBL; AY122109; AAM52621.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001163781.1; NM_001170310.1. [Q0KHY3-2]
DR RefSeq; NP_001163782.1; NM_001170311.1. [Q0KHY3-3]
DR RefSeq; NP_001287618.1; NM_001300689.1. [Q0KHY3-2]
DR RefSeq; NP_733418.1; NM_170539.1. [Q0KHY3-1]
DR RefSeq; NP_733419.1; NM_170540.1. [Q0KHY3-1]
DR AlphaFoldDB; Q0KHY3; -.
DR BioGRID; 68533; 3.
DR IntAct; Q0KHY3; 5.
DR STRING; 7227.FBpp0290183; -.
DR GlyGen; Q0KHY3; 13 sites.
DR iPTMnet; Q0KHY3; -.
DR PaxDb; Q0KHY3; -.
DR PRIDE; Q0KHY3; -.
DR DNASU; 43688; -.
DR EnsemblMetazoa; FBtr0085779; FBpp0085140; FBgn0051004. [Q0KHY3-1]
DR EnsemblMetazoa; FBtr0085780; FBpp0085141; FBgn0051004. [Q0KHY3-1]
DR EnsemblMetazoa; FBtr0300960; FBpp0290182; FBgn0051004. [Q0KHY3-2]
DR EnsemblMetazoa; FBtr0300961; FBpp0290183; FBgn0051004. [Q0KHY3-3]
DR EnsemblMetazoa; FBtr0344066; FBpp0310483; FBgn0051004. [Q0KHY3-2]
DR GeneID; 43688; -.
DR KEGG; dme:Dmel_CG31004; -.
DR UCSC; CG31004-RA; d. melanogaster. [Q0KHY3-3]
DR UCSC; CG31004-RB; d. melanogaster.
DR CTD; 43688; -.
DR FlyBase; FBgn0051004; mesh.
DR VEuPathDB; VectorBase:FBgn0051004; -.
DR eggNOG; KOG4291; Eukaryota.
DR GeneTree; ENSGT00730000110943; -.
DR InParanoid; Q0KHY3; -.
DR OMA; YFRMERD; -.
DR PhylomeDB; Q0KHY3; -.
DR Reactome; R-DME-913709; O-linked glycosylation of mucins.
DR Reactome; R-DME-977068; Termination of O-glycan biosynthesis.
DR SignaLink; Q0KHY3; -.
DR BioGRID-ORCS; 43688; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 43688; -.
DR PRO; PR:Q0KHY3; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0051004; Expressed in adult midgut (Drosophila) and 22 other tissues.
DR ExpressionAtlas; Q0KHY3; baseline and differential.
DR Genevisible; Q0KHY3; DM.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:FlyBase.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005920; C:smooth septate junction; IDA:FlyBase.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR GO; GO:0090528; P:smooth septate junction assembly; IMP:FlyBase.
DR CDD; cd00033; CCP; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR005533; AMOP_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR003886; NIDO_dom.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR001846; VWF_type-D.
DR Pfam; PF03782; AMOP; 1.
DR Pfam; PF06119; NIDO; 1.
DR Pfam; PF00084; Sushi; 1.
DR Pfam; PF00094; VWD; 1.
DR SMART; SM00723; AMOP; 1.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00539; NIDO; 1.
DR SMART; SM00216; VWD; 1.
DR SUPFAM; SSF57535; SSF57535; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50856; AMOP; 1.
DR PROSITE; PS51220; NIDO; 1.
DR PROSITE; PS50923; SUSHI; 1.
DR PROSITE; PS51233; VWFD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
KW Developmental protein; Disulfide bond; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Signal; Sushi; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1454
FT /note="Protein mesh"
FT /id="PRO_0000355637"
FT TOPO_DOM 22..1186
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1187..1207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1208..1454
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 259..425
FT /note="NIDO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00570"
FT DOMAIN 656..807
FT /note="AMOP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00347"
FT DOMAIN 820..1028
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1119..1179
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 1229..1454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1281..1307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1249
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1251
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1254
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1295
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1297
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 888
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 942
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 977
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 985
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1048
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1066
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1121..1161
FT /evidence="ECO:0000250"
FT DISULFID 1147..1177
FT /evidence="ECO:0000250"
FT VAR_SEQ 1180..1454
FT /note="EVYYTRRVAFIAIGIIFLVICPLMLCIVCGVYRYRQKQLKEDPQWQMPMLPR
FT SRASSARNLRTLNYDDDSDTDASTLKKSRSYDKVYRTNEPLPGKPQIDFPAKKWDLDEN
FT DEDVTSSEGEKPKQLGRRSLHSASGTELDQHGSPVDGDHPDEDDDFDEADVHTGTTHPV
FT GYHQPLSPEEADQLHRQQYSPTFSGLDSRTSGASSINYTPQAATQNRFGGVPVLPSNTQ
FT YYSRPPSSVNTVPLRTAPTPLTQDTGLPSPPLATSPTPSVQKSTEV -> HEERSARVA
FT SISLGMVLLILIPCLLLLVCGASYWIRERIAREEEEAAQALLPKSKWQQSKQHVI (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_035956"
FT VAR_SEQ 1259..1282
FT /note="SRSYDKVYRTNEPLPGKPQIDFPA -> T (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:12537569, ECO:0000303|Ref.3"
FT /id="VSP_053282"
FT CONFLICT 686
FT /note="C -> Y (in Ref. 4; AAM52621)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1454 AA; 165038 MW; 2C8C1239C69EA6F8 CRC64;
MRFKLFVVCA LACGFMAFVL ANENISTEEF EDQIINAVPE PVKVTKPKAQ AEFVEVPKAT
PAPKKAEADN PKTKPLALQK PTLIPVVHVS SRGTDDILTV AGLKPEKMFG ALIMPNDYLG
ELYDVDNSGY NWDPNNNVAP PTTYSTAAGG YTITAARLAE LRSNFMYWYF DKDMYGGRGD
YQFDIHASMT QLHKNLNFQL PFYGFRFNYT RLSLNGYLEF SDPPEYLTYP LVFPIKDWPA
KRDPSFMGIF FSKCRVGRIY PSDIDQRTPG VYFRVERDLM GRTDRFGVEV RERTMWDIRQ
GVVGADTFIP KHVVIATWKN VSFAGGIDNS LYTTNTFQMV LATDEVYTYI IFNYAVLNWL
SHTEAGGDTT KGEGGVPAYV GFNAGNGTQA YEYNPYSQNM VIRDLANRGW ANGFPGRHIF
RVDEQILIGS CNKDIDAALL PLTFAPESGN MLGGQVVNIT GPCFDPAIRV TCHFDTESVL
GTYVDRNRVI CVQPYLKAEG YIRFQISVGT QRFKWRGKYF VETPAAATEK IFFTTDDVHK
KNPAEIRITW NQYNLTSNAN ANVMISLWGY RETKIEPQLE YIDVIEASYS NSGSYVITPS
NYINRNNINR DMQFGFLQIN LTQPDQYSGL AISPVLWSRP IPLAWYMAPQ WERQHGKRWA
RALCDNWIRA DRFLRNFAAD LPLCPCTLDQ AVLDKGRFRP DRECDKDSNP SCLRHRGAIH
CVVSGTPVAQ GAEQQCCYDR YGFLMLTYDQ MWGSRPRRVH NLGKMPWNEA SKVPSLSMWF
HDMRPFYSCC YWQEEQAVGC ETYRFERRPS QDCVAYQAPG IAGVFGDPHF VTFDGTAYTF
NGLGEFVLAR SVDESNKFEV QGRFEQLPVN YYGEVKATQL TAVAMRGNTT TTIEVRLRPL
HARWRYRLDV LADGRRVYFD RESLKFQHFD GVTVYTPTYL LNQSQVVVQF DAGIGVEVVE
NEGYMTGRVF LPWKFINKTA GLFGNWSFNK LDDFMLPNGQ VAQLNLNDLR SIHTNFGIKW
MLTDREVPGV GAALFKREFG RMSGYYANAT FQPNYVLDPA DFLPANRSYD LERAEELCGE
CMQCQYDYAM TLNRDLAHFT KNYYDTIVNM QAENAVRVVS CGVLQTPRFG RKLSFDFMPG
AKVSFECNEG FILIGDQRRE CLSNGLWNIP EYGYTECLRE VYYTRRVAFI AIGIIFLVIC
PLMLCIVCGV YRYRQKQLKE DPQWQMPMLP RSRASSARNL RTLNYDDDSD TDASTLKKSR
SYDKVYRTNE PLPGKPQIDF PAKKWDLDEN DEDVTSSEGE KPKQLGRRSL HSASGTELDQ
HGSPVDGDHP DEDDDFDEAD VHTGTTHPVG YHQPLSPEEA DQLHRQQYSP TFSGLDSRTS
GASSINYTPQ AATQNRFGGV PVLPSNTQYY SRPPSSVNTV PLRTAPTPLT QDTGLPSPPL
ATSPTPSVQK STEV
