KLAR_DROME
ID KLAR_DROME Reviewed; 2262 AA.
AC Q9Y0E4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Klarsicht protein {ECO:0000303|PubMed:10556085};
GN Name=klar {ECO:0000312|FlyBase:FBgn0001316};
GN ORFNames=CG17046 {ECO:0000312|FlyBase:FBgn0001316};
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], DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=10556085; DOI=10.1016/s0960-9822(99)80501-6;
RA Mosley-Bishop K.L., Li Q., Patterson L., Fischer J.A.;
RT "Molecular analysis of the klarsicht gene and its role in nuclear migration
RT within differentiating cells of the Drosophila eye.";
RL Curr. Biol. 9:1211-1220(1999).
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.
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 SUBCELLULAR LOCATION, DOMAIN, FUNCTION, AND REGION.
RX PubMed=15579692; DOI=10.1534/genetics.104.028662;
RA Fischer J.A., Acosta S., Kenny A., Cater C., Robinson C., Hook J.;
RT "Drosophila klarsicht has distinct subcellular localization domains for
RT nuclear envelope and microtubule localization in the eye.";
RL Genetics 168:1385-1393(2004).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=14617811; DOI=10.1091/mbc.e03-06-0374;
RA Patterson K., Molofsky A.B., Robinson C., Acosta S., Cater C.,
RA Fischer J.A.;
RT "The functions of Klarsicht and nuclear lamin in developmentally regulated
RT nuclear migrations of photoreceptor cells in the Drosophila eye.";
RL Mol. Biol. Cell 15:600-610(2004).
RN [6]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18820457; DOI=10.4161/fly.4254;
RA Kracklauer M.P., Banks S.M., Xie X., Wu Y., Fischer J.A.;
RT "Drosophila klaroid encodes a SUN domain protein required for Klarsicht
RT localization to the nuclear envelope and nuclear migration in the eye.";
RL Fly 1:75-85(2007).
RN [7]
RP SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH MSP300, AND DOMAIN.
RX PubMed=22927463; DOI=10.1083/jcb.201204102;
RA Elhanany-Tamir H., Yu Y.V., Shnayder M., Jain A., Welte M., Volk T.;
RT "Organelle positioning in muscles requires cooperation between two KASH
RT proteins and microtubules.";
RL J. Cell Biol. 198:833-846(2012).
RN [8]
RP INTERACTION WITH KUD.
RX PubMed=28716842; DOI=10.1083/jcb.201606043;
RA Ding Z.Y., Wang Y.H., Huang Y.C., Lee M.C., Tseng M.J., Chi Y.H.,
RA Huang M.L.;
RT "Outer nuclear membrane protein Kuduk modulates the LINC complex and
RT nuclear envelope architecture.";
RL J. Cell Biol. 216:2827-2841(2017).
CC -!- FUNCTION: Component of the LINC (LInker of Nucleoskeleton and
CC Cytoskeleton) complex involved in the connection between the nuclear
CC lamina and the cytoskeleton (By similarity). Plays a role in the
CC nuclear positioning and links the nucleus to the microtubule organizing
CC center (MTOC) (PubMed:10556085, PubMed:22927463, PubMed:15579692).
CC Collaborates with Klar to promote even spacing of the myonuclei at the
CC periphery of striated muscle fibers by mediating a tight association
CC between a nuclear ring structure of Msp300 and the plus ends of a
CC unique astral microtubule (MT) network (PubMed:22927463).
CC {ECO:0000250|UniProtKB:Q8WXH0, ECO:0000269|PubMed:10556085,
CC ECO:0000269|PubMed:15579692, ECO:0000269|PubMed:22927463}.
CC -!- SUBUNIT: Core component of LINC complexes which are composed of inner
CC nuclear membrane SUN domain-containing proteins coupled to outer
CC nuclear membrane KASH domain-containing nesprins (By similarity).
CC Interacts with kud (PubMed:28716842). Interacts with Msp300; this
CC interaction allows the anchoring of Msp300 nuclear ring structure to
CC the nuclear envelope (PubMed:22927463). {ECO:0000250|UniProtKB:Q8WXH0,
CC ECO:0000269|PubMed:22927463, ECO:0000269|PubMed:28716842}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:10556085, ECO:0000269|PubMed:15579692,
CC ECO:0000269|PubMed:18820457, ECO:0000269|PubMed:22927463}. Nucleus
CC membrane {ECO:0000269|PubMed:14617811, ECO:0000269|PubMed:15579692,
CC ECO:0000269|PubMed:18820457}. Nucleus envelope
CC {ECO:0000269|PubMed:14617811}. Note=Associated with microtubules, both
CC apical to the nucleus and also at the basal-most area of the eye disk
CC (PubMed:15579692, PubMed:18820457, PubMed:14617811). Koi is required
CC for perinuclear localization of Klar (PubMed:18820457). Nuclear
CC envelope localization requires nuclear lam (PubMed:14617811).
CC {ECO:0000269|PubMed:14617811, ECO:0000269|PubMed:15579692,
CC ECO:0000269|PubMed:18820457}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously in the eye disk, but at much
CC higher levels posterior to the morphogenetic furrow (PubMed:18820457).
CC Expressed in R-cells and also in non-neural cone cells
CC (PubMed:18820457). {ECO:0000269|PubMed:18820457}.
CC -!- DOMAIN: The KASH domain mediates localization to the nuclear membrane
CC (PubMed:15579692). Msp300 and Klar KASH domains cooperate to mediate
CC the connection between a nuclear ring structure of Msp300 and the plus
CC ends of a unique astral microtubule (MT) network (PubMed:22927463).
CC {ECO:0000269|PubMed:15579692, ECO:0000269|PubMed:22927463}.
CC -!- DISRUPTION PHENOTYPE: Homozygous mutant flies are viable and fertile
CC but have eye defects; photoreceptor nuclei fail to migrate apically as
CC they are specified, resulting in aberrantly shaped photoreceptors in
CC adult eyes (PubMed:28716842). In larval mutants eye disks, both the R-
CC cell and cone cell nuclei are positioned randomly within the
CC apical/basal axis (PubMed:18820457). {ECO:0000269|PubMed:18820457,
CC ECO:0000269|PubMed:28716842}.
CC -!- SIMILARITY: Belongs to the nesprin family. {ECO:0000305}.
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DR EMBL; AF157066; AAD43129.1; -; mRNA.
DR EMBL; AE014296; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR IntAct; Q9Y0E4; 2.
DR PRIDE; Q9Y0E4; -.
DR FlyBase; FBgn0001316; klar.
DR VEuPathDB; VectorBase:FBgn0001316; -.
DR ChiTaRS; klar; fly.
DR Proteomes; UP000000803; Chromosome 3L.
DR ExpressionAtlas; Q9Y0E4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:FlyBase.
DR GO; GO:0005640; C:nuclear outer membrane; IDA:FlyBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0019894; F:kinesin binding; IDA:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0042051; P:compound eye photoreceptor development; IMP:FlyBase.
DR GO; GO:0060361; P:flight; IMP:FlyBase.
DR GO; GO:0007523; P:larval visceral muscle development; IMP:FlyBase.
DR GO; GO:0031887; P:lipid droplet transport along microtubule; IMP:FlyBase.
DR GO; GO:0006869; P:lipid transport; IMP:FlyBase.
DR GO; GO:0040011; P:locomotion; IMP:FlyBase.
DR GO; GO:0035149; P:lumen formation, open tracheal system; IMP:FlyBase.
DR GO; GO:0061024; P:membrane organization; IMP:FlyBase.
DR GO; GO:0034453; P:microtubule anchoring; IGI:FlyBase.
DR GO; GO:0045855; P:negative regulation of pole plasm oskar mRNA localization; IMP:FlyBase.
DR GO; GO:0007097; P:nuclear migration; IMP:FlyBase.
DR GO; GO:0051647; P:nucleus localization; IGI:FlyBase.
DR GO; GO:0006997; P:nucleus organization; IGI:FlyBase.
DR GO; GO:0032386; P:regulation of intracellular transport; IMP:FlyBase.
DR GO; GO:0035239; P:tube morphogenesis; IMP:FlyBase.
DR InterPro; IPR039906; Anc-1-like.
DR InterPro; IPR012315; KASH.
DR PANTHER; PTHR21524; PTHR21524; 2.
DR Pfam; PF10541; KASH; 1.
DR SMART; SM01249; KASH; 1.
DR PROSITE; PS51049; KASH; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Membrane; Nucleus; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..2262
FT /note="Klarsicht protein"
FT /id="PRO_0000454908"
FT TOPO_DOM 1..2215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT TRANSMEM 2216..2236
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT TOPO_DOM 2237..2262
FT /note="Perinuclear space"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT DOMAIN 2207..2262
FT /note="KASH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT REGION 1..1774
FT /note="Required for apical microtubules localization"
FT /evidence="ECO:0000269|PubMed:15579692"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1533..1670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2092..2205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1809..1842
FT /evidence="ECO:0000255"
FT COMPBIAS 83..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..475
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..561
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1301
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1543..1586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1613..1637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1656..1670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2092..2111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2152..2167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2262 AA; 245117 MW; 4AF852E57BFC9C7D CRC64;
MEMQQENETG REGVIPNSEK EVALISNQET EKAAMISGGK EGSVRDLESP NETATTQKIE
HTTKPLKLDG IFAMPATPPN KAGLATKSAS SSRSSSLKKQ RRGSRGSANL NVAGMGDGAP
KRSAPGGGQL NYGTNSVGND LMKQSQSMTS LKASNEEQQE SRDVIQAKLH LERPYNSLKK
NSHSNKMHRY SWGSGNSQCS STSLHSSATL GLGSSGKDDL WAAIQTNYNY IMDTNLLDTC
KEARCEIEGA ATVLEKSSEC SFKMLDETQR PEGLCEDPKE LRRSWREMEN KLESSPTITE
LTLFGNAELQ RHLAVHSVLY HEIASHARVV SSCIRAAEKE QQLQQQQQLS SQQPASLTSN
CSSESTSESA TKSSSLSSGF ASDPVTTPIG TAAAAPPSSS THPSKKGEGN LERLRDRYHL
LYLKAFELQL CLDNLLRKRS SAANGLDDDE DEEEDTEDDS FGYEGEATED DLNEVNSDLD
LENSESKSAT PAELILQRCQ IAATQIVCGL DETQSQSRSQ QVPSQAKSPS ADQPRDCLAP
QKPGDEADEE LEEEDEDPDI GTDVVDFLIA KRSWRQVNHP NPSGTATLTD FEADSESSDF
EQVQQLSRRG LPPTVGSTRR VLNLIEMPQS SNTNISSSNS LLQQRNHNIG NKMLPNKAHG
KNIAVAVITP NSHGNTSHGH GLGHGLGHEL NKSPLGLRKT RHHHNDTSKF NRSNRKSKNC
AIFYFKHLDT DNEQGNAAGS DLQSEDDPSL IHRRRAGGDI LKSADASTDD DDEGCLYTAT
AAATLEVATA ATAAPTAAAA TSSVDGLQST AVSSTTATGG PLPPSDDSDK ENKVALVSAS
TITAARTATA TSIATLHSSN YDSSSACSSS NSNSNSNSNS NGRLTETSAT SRVTQLQMQI
HSQSQSQSQM ELQINGNAID GRHIISNNNC YSSMQHQPQN NNEGEAAEDL AKIKMGDDEA
AADMANGNAT KSQQMSNGVY SRADSCNFTV WAAETVASCH LPPRSPAKSA KSTKSQASNA
TVSGSTLVSP VKGKVSHDSI KQLVLKAEHL VRDAQETALK TPTKQKHSII KISSTVKKRE
VTMPHPIKQR VEEWLEHQPS TPQLLTRSHT NELLPSCKPD DCEASGEASE TDSVPQAGAG
VNGGAPNGAG SDTSEGFTDS IATCMQTSTN SYGNSTERIG GSAEPIGQPV TPLGFGSSNQ
SLNVKIVKRS QTRRKSERPW SVSCLSQLTT DAAQLTTARI VENSPSGLAS HSISESALDS
LSPGPRPRAA SSSGTGSNAA KKADSKGSLR RRKARKKRIS AASAGRKSDS GSELGGDLTQ
TLMKSCESMS SQQLQEFTNA LLSIQKGAVV APLSPKGEVS GVPSLHDGEG GETQLMLPKF
RVGSFTTAGL LATDTRLGAL AALSNYMNED EQQAELSTED HHSSISETAW DNYQEKYNSE
NYSEGFDSDA ARRLLEFGDD YRNFIDSQSD CCSSLSAANN LDSFSPPRMD SLQKHELKSL
HINQDTITSS VDHARRQRAL ELQYERRRKT LEVRRKSCQD MDESLMASPQ SDQQQQQLQV
TPSLSASATA LMTTPKNQST SHQISHRAES VGRKLDFGGM SHSAQSLLRR TSESDTSTRR
RRTVTADERR RSSRNLEKCI KLIPATTSSS SGSDSEDGEQ EMRSLLQQSR DRLDDTRALK
IRCHLLRPED YNEIINTCRD NIRCLEAVLR GPPGTVLSNH CAGQTKDLLG AWEDLLSWSE
NASAARKLQQ EMSVLKSSLQ RLGDKPTPEL LDTEPAIQIA VEALKLEQTQ LTSYRTNMLR
LNASVHSWLT KQERRLQSAL EEQEQQQESE QLKQQKLVEE EKGADVQKEL ASTGAVAITV
TDSNGNQVEA LATGEASTST PAWDVHSLMS SEQEFHKHLK NEVSDMYSAW DEADARINTQ
LEMLTNSLIA WRQLESGLSE FQLALGQDRG TLKGLEGALD KGQATPVELA QNVKLVAKLL
SEKVHVSQEQ LLAVQQHLDP NHIYHITKFT ASNGSLSDSG ISDGGATSDG GLSERERRLG
VLRRLAKQLE LALAPGSEAM RSIAARMESA EADLKHLQNT CRDLIVRTAA SHQQKQQIQQ
NQTQQVSPKA NGHIKKQAAK GKAEPQSPGR RGKGARKARQ AKKAGEDQQV EEPSLSPEQQ
KMVLKQLKTL TSGDGGDDPS DDPSLLFNLE SSEEDGEGAD PAQTSKRGWA WRIARAAVPM
QVALFTIFCA ACLMQPNCCD NLNNLSMSFT PQLRYIRGPP PI
