EPB41_DROME
ID EPB41_DROME Reviewed; 1698 AA.
AC Q9V8R9; A1ZBI0; Q1WWD0; Q24440; Q24441; Q24442; Q9V8R8; Q9V8S0;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Protein 4.1 homolog;
DE AltName: Full=Protein coracle;
GN Name=cora; ORFNames=CG11949;
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 [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 278-1698 (ISOFORMS 2 AND 3), AND FUNCTION.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=8162854; DOI=10.1242/dev.120.3.545;
RA Fehon R.G., Dawson I.A., Artavanis-Tsakonas S.;
RT "A Drosophila homologue of membrane-skeleton protein 4.1 is associated with
RT septate junctions and is encoded by the coracle gene.";
RL Development 120:545-557(1994).
RN [2]
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 [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC STRAIN=Berkeley;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-659 AND SER-1590, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471; SER-474; SER-478;
RP SER-566; SER-687; THR-689; SER-697; SER-1398; SER-1401; SER-1402 AND
RP THR-1407, 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).
CC -!- FUNCTION: An integral component of the septate junction. May play a
CC role in cell-cell interactions that are necessary for proper
CC development. Vital for embryonic development.
CC {ECO:0000269|PubMed:8162854}.
CC -!- SUBCELLULAR LOCATION: Cell junction, septate junction. Note=Septate
CC junction in the apical-lateral domain of epithelial cells during
CC embryonic and imaginal disk development.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=A;
CC IsoId=Q9V8R9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9V8R9-2; Sequence=VSP_000476, VSP_000477, VSP_000479,
CC VSP_000480, VSP_000481;
CC Name=3; Synonyms=C;
CC IsoId=Q9V8R9-3; Sequence=VSP_000475, VSP_000478, VSP_000479;
CC Name=4; Synonyms=B;
CC IsoId=Q9V8R9-4; Sequence=VSP_000476, VSP_000477, VSP_000479;
CC Name=5;
CC IsoId=Q9V8R9-5; Sequence=VSP_000474, VSP_000478;
CC Name=6; Synonyms=D;
CC IsoId=Q9V8R9-6; Sequence=VSP_000478;
CC -!- TISSUE SPECIFICITY: At onset of germ band retraction, expression is
CC seen in epidermis, hindgut and foregut. During retraction, expression
CC extends to tracheal branches and salivary glands.
CC -!- DEVELOPMENTAL STAGE: Expressed weakly in 4-8 hours embryos, more
CC abundant expression in 8-12 hours and remains throughout later
CC embryonic and larval stages.
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DR EMBL; L27467; AAB59187.1; -; mRNA.
DR EMBL; L27468; AAA28742.1; -; mRNA.
DR EMBL; L27469; AAA28743.1; -; mRNA.
DR EMBL; AE013599; AAF57591.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF57592.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF57593.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM70846.1; -; Genomic_DNA.
DR EMBL; AY070992; AAL48614.1; -; mRNA.
DR EMBL; BT024976; ABE01206.1; -; mRNA.
DR PIR; T13800; T13800.
DR RefSeq; NP_523791.2; NM_079067.4. [Q9V8R9-1]
DR RefSeq; NP_725864.1; NM_166336.2. [Q9V8R9-3]
DR RefSeq; NP_725865.1; NM_166337.2. [Q9V8R9-4]
DR RefSeq; NP_725866.1; NM_166338.3. [Q9V8R9-6]
DR AlphaFoldDB; Q9V8R9; -.
DR SMR; Q9V8R9; -.
DR BioGRID; 62870; 26.
DR DIP; DIP-20283N; -.
DR IntAct; Q9V8R9; 6.
DR STRING; 7227.FBpp0085697; -.
DR iPTMnet; Q9V8R9; -.
DR PaxDb; Q9V8R9; -.
DR PeptideAtlas; Q9V8R9; -.
DR PRIDE; Q9V8R9; -.
DR DNASU; 37205; -.
DR EnsemblMetazoa; FBtr0086506; FBpp0085694; FBgn0010434. [Q9V8R9-3]
DR EnsemblMetazoa; FBtr0086508; FBpp0085696; FBgn0010434. [Q9V8R9-4]
DR EnsemblMetazoa; FBtr0086509; FBpp0085697; FBgn0010434. [Q9V8R9-1]
DR EnsemblMetazoa; FBtr0301279; FBpp0290494; FBgn0010434. [Q9V8R9-6]
DR GeneID; 37205; -.
DR KEGG; dme:Dmel_CG11949; -.
DR UCSC; CG11949-RA; d. melanogaster.
DR CTD; 37205; -.
DR FlyBase; FBgn0010434; cora.
DR VEuPathDB; VectorBase:FBgn0010434; -.
DR eggNOG; KOG3527; Eukaryota.
DR GeneTree; ENSGT00940000167098; -.
DR HOGENOM; CLU_002715_0_0_1; -.
DR InParanoid; Q9V8R9; -.
DR OMA; DMEHIDQ; -.
DR PhylomeDB; Q9V8R9; -.
DR Reactome; R-DME-6794361; Neurexins and neuroligins.
DR SignaLink; Q9V8R9; -.
DR BioGRID-ORCS; 37205; 0 hits in 3 CRISPR screens.
DR ChiTaRS; cora; fly.
DR GenomeRNAi; 37205; -.
DR PRO; PR:Q9V8R9; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0010434; Expressed in oviduct (Drosophila) and 40 other tissues.
DR ExpressionAtlas; Q9V8R9; baseline and differential.
DR Genevisible; Q9V8R9; DM.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0005918; C:septate junction; IDA:UniProtKB.
DR GO; GO:0005920; C:smooth septate junction; IDA:FlyBase.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR GO; GO:0007527; P:adult somatic muscle development; IMP:FlyBase.
DR GO; GO:0061343; P:cell adhesion involved in heart morphogenesis; IMP:FlyBase.
DR GO; GO:0045216; P:cell-cell junction organization; TAS:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:0060857; P:establishment of glial blood-brain barrier; IMP:FlyBase.
DR GO; GO:0003015; P:heart process; IMP:FlyBase.
DR GO; GO:0035321; P:maintenance of imaginal disc-derived wing hair orientation; IMP:FlyBase.
DR GO; GO:0006612; P:protein targeting to membrane; TAS:FlyBase.
DR GO; GO:0035151; P:regulation of tube size, open tracheal system; IMP:FlyBase.
DR CDD; cd14473; FERM_B-lobe; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR008379; Band_4.1_C.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014847; FERM-adjacent.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF05902; 4_1_CTD; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR PRINTS; PR00935; BAND41.
DR SMART; SM00295; B41; 1.
DR SMART; SM01195; FA; 1.
DR SMART; SM01196; FERM_C; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Developmental protein; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1698
FT /note="Protein 4.1 homolog"
FT /id="PRO_0000219394"
FT DOMAIN 32..314
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..434
FT /note="Hydrophilic"
FT REGION 335..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1286..1698
FT /note="C-terminal (CTD)"
FT REGION 1509..1599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1509..1527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1528..1571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1583..1599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 689
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1398
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1401
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1402
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1407
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1590
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT VAR_SEQ 1..312
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_000474"
FT VAR_SEQ 409
FT /note="K -> KSSTGTASASSQSSLEGDYETNLEIEAIEAEPPVQ (in isoform
FT 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:8162854"
FT /id="VSP_000476"
FT VAR_SEQ 409
FT /note="K -> KLMRQSSTGTASASSQSSLEGDYETNLEIEAIEAEPPVQ (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:8162854, ECO:0000303|Ref.5"
FT /id="VSP_000475"
FT VAR_SEQ 482..1480
FT /note="Missing (in isoform 3, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:8162854, ECO:0000303|Ref.5"
FT /id="VSP_000478"
FT VAR_SEQ 482..1290
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:8162854"
FT /id="VSP_000477"
FT VAR_SEQ 1554..1587
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:8162854, ECO:0000303|Ref.5"
FT /id="VSP_000479"
FT VAR_SEQ 1629..1635
FT /note="VSSKTRT -> GGGGGGI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8162854"
FT /id="VSP_000480"
FT VAR_SEQ 1636..1698
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8162854"
FT /id="VSP_000481"
FT CONFLICT 970
FT /note="I -> V (in Ref. 1; AAB59187)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1698 AA; 184168 MW; 93940FC4F1ACEB83 CRC64;
MPAEIKPSAP AEPETPTKSK PKSSSSSHGK PALARVTLLD GSLLDVSIDR KAIGRDVINS
ICAGLNLIEK DYFGLTYETP TDPRTWLDLE KPVSKFFRTD TWPLTFAVKF YPPEPSQLKE
DITRYHLCLQ VRNDILEGRL PCTFVTHALL GSYLVQSEMG DYDAEEMPTR AYLKDFKIAP
NQTAELEDKV MDLHKTHKGQ SPAEAELHYL ENAKKLAMYG VDLHPAKDSE GVDIMLGVCA
SGLLVYRDKL RINRFAWPKI LKISYKRHHF YIKIRPGEFE QYESTIGFKL ANHRAAKKLW
KSCVEHHTFF RLMTPEPVSK SKMFPVFGST YRYKGRTQAE STNTPVDRTP PKFNRTLSGA
RLTSRSMDAL ALAEKEKVAR KSSTLDHRGD RNADGDAHSR SPIKNKKEKD ADKEAKLREK
KQKEKEEKER KEREKRELEE KKKAEKAAKA ALAAGAAAGA AVNGNDELND SNKSDKSSGR
RGVGIFSSGR KSKSGSPSKD GKDKSGKDKD KEVGRLGLVV TSGLGDNQQD QNLDEAARNA
AKNRGSTTPG VTRQYEYAVD NDGNTSPTRK SYTPGGFRYD QDPNSRKSGA DGQEQLSPTS
QQKKIGLAFN YAPGNENALK ETAEKLKAGQ LSPRTQDKLN RGQLSPKSRA KLLQDPLLSP
TTRAKLQGSA VDAAAVPLSD SQKRSYSPTK GPQGYSSGAP GSYKPISDPT ADFLESQRYN
KEPGYVGPSK ADVAAGLAGA AGSKKPGSPT KTGKGAPGAA AAAAAGAAGA AAAAAKPKKR
RVKIMVITSK FDPSTKRIDA ENGSIEHSTG ILDPATGLID TKYGVIDPKK GTLEALNTKT
GKKEVFQGDV DGKTGNLHLV SGVADPKTGR LDDTLGQIVC ITPQDNPVVE LTVITSRIDP
ATGKIDTVNG DVERSLGVLN LDTGLLDTKY GEINTRTGEL KAIDPKSGKI VVSKNVKVDP
GTGQITILGI VDPKTNKIDP NQGRLIEVGQ QIDPIVEVTS LAGKFDSKRN IIDPKTAQVE
TSGGQFDPKA GKIDTKYGQI DLVKHTITFN DPKSGKTVTR DIKIEPTTGQ IVLKNQVNPK
NNKPDKDYAR IISLRIVQQR VDPATKAPIT EVSASKDKDI VVDPKSNQIW VPTGATDPAT
KEQQYISSSV DPKTGYVITI YGYLDPKTNE IKKQTKLDPN TIKIEPTSGK IYTATGEVDQ
ATGEPLYAAT QVDPESGEVY TKLARVDPKT GKIVIVRILL ISKTDERGRP EEIDPSTCEI
DPVSGRVLKF FNKTVYVYNM IDPVTGEIVQ VDPNDPRFAG ARTTVTHTMT LTGEIDPVTG
RIKSEYGDID PNTGDIDPAT AVTDPVTGKL ILNYAQIDPS HFGKQAQVQT TTETVPITRQ
QFFDGVKHIS KGALRRDSEG SSDDDMTAQY GADQVNEILI GSPAGQAGGK LGKPVSTPTV
VKTTTKQVLT KNIDGVTHNV EEEVRNLGTG EVTYSTQEHK ADATPTDLSG AYVTATAVTT
RTATTHEDLG KNAKTEQLEE KTVATTRTHD PNKQQQRVVT QEVKTTATVT SGDQYQRRDS
VSSTSSGDSG TPIDGPYDGA SVVRTDNQKS PLFTTSATTG PHVESTRVVL GEDTPGFSGH
GEIISTQTVS SKTRTVETIT YKTERDGIVE TRVEQKITIQ SDGDPIDHDK ALAEAIQEAT
AMNPDMTVEK IEIQQQTQ
