CL190_DROME
ID CL190_DROME Reviewed; 1690 AA.
AC Q9VJE5; O44929; Q8INY8; Q8MSD0;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Restin homolog;
DE AltName: Full=Cytoplasmic linker protein 190;
DE AltName: Full=Microtubule-binding protein 190;
DE AltName: Full=d-CLIP-190;
GN Name=CLIP-190; ORFNames=CG5020;
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 A), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=Oregon-R; TISSUE=Embryo, and Ovary;
RX PubMed=9472041; DOI=10.1083/jcb.140.4.897;
RA Lantz V.A., Miller K.G.;
RT "A class VI unconventional myosin is associated with a homologue of a
RT microtubule-binding protein, cytoplasmic linker protein-170, in neurons and
RT at the posterior pole of Drosophila embryos.";
RL J. Cell Biol. 140:897-910(1998).
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 B).
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [MRNA] OF 1-807 (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Ovary;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11076973; DOI=10.1083/jcb.151.4.905;
RA Sisson J.C., Field C., Ventura R., Royou A., Sullivan W.;
RT "Lava lamp, a novel peripheral Golgi protein, is required for Drosophila
RT melanogaster cellularization.";
RL J. Cell Biol. 151:905-918(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-67; SER-216; SER-309;
RP SER-322; SER-325; THR-327; SER-328; THR-362; THR-1681 AND SER-1682, AND
RP 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: Together CLIP-190 and jar may coordinate the interaction
CC between the actin and microtubule cytoskeleton. May link endocytic
CC vesicles to microtubules. May play a role in formation of furrows
CC during cellularization. {ECO:0000269|PubMed:11076973,
CC ECO:0000269|PubMed:9472041}.
CC -!- SUBUNIT: Interacts with Lva. {ECO:0000269|PubMed:11076973}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:9472041}. Golgi apparatus
CC {ECO:0000269|PubMed:11076973}. Note=Microtubule-associated. Lva-CLIP-
CC 190 complexes are found at the Golgi. {ECO:0000269|PubMed:11076973,
CC ECO:0000269|PubMed:9472041}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A;
CC IsoId=Q9VJE5-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9VJE5-2; Sequence=VSP_050479;
CC Name=C;
CC IsoId=Q9VJE5-3; Sequence=VSP_050480;
CC -!- TISSUE SPECIFICITY: Specifically expressed at the tip of the furrow in
CC cellularizing blastoderms. CLIP-190 and jar are coexpressed at several
CC times in development and in a number of tissues, including embryonic
CC axonal neuron processes and posterior pole.
CC {ECO:0000269|PubMed:11076973, ECO:0000269|PubMed:9472041}.
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DR EMBL; AF041382; AAB96783.1; -; mRNA.
DR EMBL; AE014134; AAF53604.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53605.2; -; Genomic_DNA.
DR EMBL; AE014134; AAN10987.1; -; Genomic_DNA.
DR EMBL; AY118896; AAM50756.1; -; mRNA.
DR EMBL; BT011136; AAR82803.1; -; mRNA.
DR PIR; T13030; T13030.
DR RefSeq; NP_609835.2; NM_135991.4. [Q9VJE5-1]
DR RefSeq; NP_724047.2; NM_165213.5. [Q9VJE5-2]
DR RefSeq; NP_724048.1; NM_165214.2. [Q9VJE5-3]
DR AlphaFoldDB; Q9VJE5; -.
DR SMR; Q9VJE5; -.
DR BioGRID; 61038; 13.
DR DIP; DIP-21005N; -.
DR IntAct; Q9VJE5; 18.
DR STRING; 7227.FBpp0080529; -.
DR iPTMnet; Q9VJE5; -.
DR PaxDb; Q9VJE5; -.
DR PRIDE; Q9VJE5; -.
DR DNASU; 35042; -.
DR EnsemblMetazoa; FBtr0080975; FBpp0080528; FBgn0020503. [Q9VJE5-2]
DR EnsemblMetazoa; FBtr0080976; FBpp0080529; FBgn0020503. [Q9VJE5-1]
DR EnsemblMetazoa; FBtr0080977; FBpp0080530; FBgn0020503. [Q9VJE5-3]
DR GeneID; 35042; -.
DR KEGG; dme:Dmel_CG5020; -.
DR CTD; 35042; -.
DR FlyBase; FBgn0020503; CLIP-190.
DR VEuPathDB; VectorBase:FBgn0020503; -.
DR eggNOG; KOG4568; Eukaryota.
DR GeneTree; ENSGT00940000155122; -.
DR InParanoid; Q9VJE5; -.
DR PhylomeDB; Q9VJE5; -.
DR SignaLink; Q9VJE5; -.
DR BioGRID-ORCS; 35042; 0 hits in 3 CRISPR screens.
DR ChiTaRS; CLIP-190; fly.
DR GenomeRNAi; 35042; -.
DR PRO; PR:Q9VJE5; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0020503; Expressed in male reproductive gland and 29 other tissues.
DR ExpressionAtlas; Q9VJE5; baseline and differential.
DR Genevisible; Q9VJE5; DM.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0044295; C:axonal growth cone; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0045169; C:fusome; IDA:FlyBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IDA:FlyBase.
DR GO; GO:0005875; C:microtubule associated complex; IDA:UniProtKB.
DR GO; GO:0035371; C:microtubule plus-end; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; IDA:FlyBase.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:FlyBase.
DR GO; GO:0070854; F:myosin VI heavy chain binding; IPI:FlyBase.
DR GO; GO:0007349; P:cellularization; IMP:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR Gene3D; 2.30.30.190; -; 2.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR032108; CLIP1_ZNF.
DR Pfam; PF01302; CAP_GLY; 2.
DR Pfam; PF16641; CLIP1_ZNF; 2.
DR SMART; SM01052; CAP_GLY; 2.
DR SUPFAM; SSF74924; SSF74924; 2.
DR PROSITE; PS00845; CAP_GLY_1; 2.
DR PROSITE; PS50245; CAP_GLY_2; 2.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Golgi apparatus; Microtubule; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1690
FT /note="Restin homolog"
FT /id="PRO_0000083514"
FT DOMAIN 143..185
FT /note="CAP-Gly 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT DOMAIN 260..302
FT /note="CAP-Gly 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1400..1419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1635..1665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 378..468
FT /evidence="ECO:0000255"
FT COILED 484..660
FT /evidence="ECO:0000255"
FT COILED 667..916
FT /evidence="ECO:0000255"
FT COILED 926..981
FT /evidence="ECO:0000255"
FT COILED 1001..1121
FT /evidence="ECO:0000255"
FT COILED 1158..1549
FT /evidence="ECO:0000255"
FT COILED 1565..1600
FT /evidence="ECO:0000255"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 327
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 362
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1681
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1682
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..109
FT /note="MSDDTSASGGTSAPFPSPVTADPEPGATASKLPGPIRSNIPTPATSGTGIPQ
FT PSKMKAPSSFGSTGSVSKIGRPCCNHTTPKSGPPPREATSMSRESDDNLSSINSAYT
FT -> MSRESDDNLSSINSAYTDLYQETVRRFTRSSLSPTPDWDRFSPARRSLKSEAGSRA
FT SYDYYLEATGRRRSS (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_050480"
FT VAR_SEQ 348
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569, ECO:0000303|Ref.5"
FT /id="VSP_050479"
FT CONFLICT 109
FT /note="T -> I (in Ref. 5; AAR82803)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="S -> N (in Ref. 1; AAB96783)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="D -> G (in Ref. 1; AAB96783 and 5; AAR82803)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="K -> Q (in Ref. 1; AAB96783 and 5; AAR82803)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="E -> A (in Ref. 1; AAB96783)"
FT /evidence="ECO:0000305"
FT CONFLICT 614
FT /note="T -> S (in Ref. 1; AAB96783)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="S -> I (in Ref. 1; AAB96783 and 5; AAR82803)"
FT /evidence="ECO:0000305"
FT CONFLICT 692
FT /note="N -> Q (in Ref. 1; AAB96783 and 5; AAR82803)"
FT /evidence="ECO:0000305"
FT CONFLICT 717
FT /note="M -> K (in Ref. 1; AAB96783 and 5; AAR82803)"
FT /evidence="ECO:0000305"
FT CONFLICT 728
FT /note="E -> D (in Ref. 5; AAR82803)"
FT /evidence="ECO:0000305"
FT CONFLICT 745
FT /note="D -> V (in Ref. 5; AAR82803)"
FT /evidence="ECO:0000305"
FT CONFLICT 769
FT /note="F -> L (in Ref. 1; AAB96783 and 5; AAR82803)"
FT /evidence="ECO:0000305"
FT CONFLICT 787
FT /note="Q -> E (in Ref. 1; AAB96783 and 5; AAR82803)"
FT /evidence="ECO:0000305"
FT CONFLICT 805..807
FT /note="EKE -> KKK (in Ref. 5; AAR82803)"
FT /evidence="ECO:0000305"
FT CONFLICT 881
FT /note="Q -> E (in Ref. 1; AAB96783)"
FT /evidence="ECO:0000305"
FT CONFLICT 907..909
FT /note="HLL -> QLQ (in Ref. 1; AAB96783)"
FT /evidence="ECO:0000305"
FT CONFLICT 920
FT /note="G -> E (in Ref. 1; AAB96783)"
FT /evidence="ECO:0000305"
FT CONFLICT 929
FT /note="C -> Y (in Ref. 1; AAB96783)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1690 AA; 189065 MW; D6F7916A9C532F16 CRC64;
MSDDTSASGG TSAPFPSPVT ADPEPGATAS KLPGPIRSNI PTPATSGTGI PQPSKMKAPS
SFGSTGSVSK IGRPCCNHTT PKSGPPPREA TSMSRESDDN LSSINSAYTD NSSAVLTANT
EQFIIGQRVW LGGTRPGQIA FIGDTHFAAG EWAGVVLDEP NGKNDGCVSG KRYFQCEPKR
GIFSRLTRLT TYPLAGAQTP TSPLAKSSPD RSRTVSPTAS IRSSMLRSPG IGGKNGMAVG
DRVIVSSGFG SRPGILRYLG ETQFAPGNWC GVELDEPSGK NDGTVDDIRY FECKPKYGVF
VPIAKVSLSP SSKKTRLSRT GSRESLTSIG TMNSIATTAT SRMRMNAQQR KSSTPVKPIL
ATPKSQFSMQ DLLREKQQHV EKLMVERDLD REDAQNQALQ LQKNINELKA RIVELESALD
NERKKTEELQ CSIDEAQFCG DELNAQSQVY KEKIHDLESK ITKLVSATPS LQSILPPDLP
SDDGALQEEI AKLQEKMTIQ QKEVESRIAE QLEEEQRLRE NVKYLNEQIA TLQSELVSKD
EALEKFSLSE CGIENLRREL ELLKEENEKQ AQEAQAEFTR KLAEKSVEVL RLSSELQNLK
ATSDSLESER VNKTDECEIL QTEVRMRDEQ IRELNQQLDE VTTQLNVQKA DSSALDDMLR
LQKEGTEEKS TLLEKTEKEL VQSKEQAAKT LNDKEQLEKQ ISDLKQLAEQ EKLVREMTEN
AINQIQLEKE SIEQQLALKQ NELEDFQKKQ SESEVHLQEI KAQNTQKDFE LVESGESLKK
LQQQLEQKTL GHEKLQAALE ELKKEKETII KEKEQELQQL QSKSAESESA LKVVQVQLEQ
LQQQAAASGE EGSKTVAKLH DEISQLKSQA EETQSELKST QSNLEAKSKQ LEAANGSLEE
EAKKSGHLLE QITKLKSEVG ETQAALSSCH TDVESKTKQL EAANAALEKV NKEYAESRAE
ASDLQDKVKE ITDTLHAELQ AERSSSSALH TKLSKFSDEI ATGHKELTSK ADAWSQEMLQ
KEKELQELRQ QLQDSQDSQT KLKAEGERKE KSFEESIKNL QEEVTKAKTE NLELSTGTQT
TIKDLQERLE ITNAELQHKE KMASEDAQKI ADLKTLVEAI QVANANISAT NAELSTVLEV
LQAEKSETNH IFELFEMEAD MNSERLIEKV TGIKEELKET HLQLDERQKK FEELEEKLKQ
AQQSEQKLQQ ESQTSKEKLT EIQQSLQELQ DSVKQKEELV QNLEEKVRES SSIIEAQNTK
LNESNVQLEN KTSCLKETQD QLLESQKKEK QLQEEAAKLS GELQQVQEAN GDIKDSLVKV
EELVKVLEEK LQAATSQLDA QQATNKELQE LLVKSQENEG NLQGESLAVT EKLQQLEQAN
GELKEALCQK ENGLKELQGK LDESNTVLES QKKSHNEIQD KLEQAQQKER TLQEETSKLA
EQLSQLKQAN EELQKSLQQK QLLLEKGNEF DTQLAEYQKV IDEMDDAASV KSALLEQLQN
RVAELETALR QANDAQKTAY LETKELRRQL ESLELEKSRE VLSLKAQMNG ASSRSGKGDE
VESLDIETSL AKINFLNSII ADMQQKNDAL KAKVQTLETL PMDFTKPHAF DALTKRKPAP
RLFCDICDEF DQHDTEDCPI QGSEDQDYST PSSESNNNEK ERKLPAPRKY CDSCEVFGHD
TSECADDETY
