ID A0A0Q9WSU5_DROVI Unreviewed; 3255 AA.
AC A0A0Q9WSU5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Uncharacterized protein, isoform E {ECO:0000313|EMBL:KRF83659.1};
GN Name=Dvir\GJ22727 {ECO:0000313|EMBL:KRF83659.1};
GN ORFNames=Dvir_GJ22727 {ECO:0000313|EMBL:KRF83659.1};
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244 {ECO:0000313|EMBL:KRF83659.1, ECO:0000313|Proteomes:UP000008792};
RN [1] {ECO:0000313|EMBL:KRF83659.1, ECO:0000313|Proteomes:UP000008792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87 {ECO:0000313|Proteomes:UP000008792};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000256|ARBA:ARBA00004278}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004278}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004278}. Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR EMBL; CH940650; KRF83659.1; -; Genomic_DNA.
DR RefSeq; XP_015026891.1; XM_015171405.1.
DR SMR; A0A0Q9WSU5; -.
DR EnsemblMetazoa; FBtr0435237; FBpp0392227; FBgn0209831.
DR GeneID; 6629515; -.
DR OrthoDB; 2880153at2759; -.
DR Proteomes; UP000008792; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IEA:UniProt.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007154; P:cell communication; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:UniProt.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:UniProt.
DR GO; GO:0023052; P:signaling; IEA:UniProt.
DR CDD; cd21186; CH_DMD-like_rpt1; 1.
DR CDD; cd16242; EFh_DMD_like; 1.
DR CDD; cd00176; SPEC; 4.
DR CDD; cd00201; WW; 1.
DR CDD; cd02334; ZZ_dystrophin; 1.
DR Gene3D; 1.20.58.60; -; 9.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR035436; Dystrophin/utrophin.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR015153; EF-hand_dom_typ1.
DR InterPro; IPR015154; EF-hand_dom_typ2.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR12268:SF14; DYSTROPHIN-1; 1.
DR PANTHER; PTHR12268; E3 UBIQUITIN-PROTEIN LIGASE KCMF1; 1.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF09068; EF-hand_2; 1.
DR Pfam; PF09069; EF-hand_3; 1.
DR Pfam; PF00435; Spectrin; 2.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF002341; Dystrophin/utrophin; 2.
DR SMART; SM00033; CH; 2.
DR SMART; SM00150; SPEC; 10.
DR SMART; SM00456; WW; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 9.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008792};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 44..148
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 159..262
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2548..2581
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 2806..2862
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT REGION 675..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1674..1693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1891..1914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2334..2357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2522..2551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3009..3042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3085..3118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3198..3227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 439..490
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 727..816
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 853..890
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1054..1109
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1220..1256
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1952..1979
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2416..2476
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 683..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2341..2357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3009..3040
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3089..3118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3255 AA; 371708 MW; 7F9073B1D0CF30F8 CRC64;
MHDPSDYDSV YSEEDFLDIV QGATTPPLMN YDEFLVKTMD ERQHIQKKTF TKWINSHLSN
TQCTPVNDLF LDLRDGHRLL ALLSTLTHTQ LKPEKGRMRV HHINNLNKVL QVIQQHGVKL
VNISSDDIVG GNPKLTLGLI WLIALEFNGQ HLVKSHSSNG VEKSLLAWAR QYTEPHGLGL
NDFASSWADG RAFLMILAAH LDELDLETAL SQHALQRLYL AFDLAHRHFK IEKLLDAEDV
HTHKPDNKSI QMYVMCLYHA MESMRATERD RVPCTSITDL DEVPLDGERE LYTSDSTASI
ELKSAVESSS QRPLSTSTNA SCGIGSYQTA LEAVLTLLLE DEELLSQELP DPENFQAAKM
QFHENESFML KLTEHQEFVG EALEAGSNLI NESQQKDGSS LSQVDQNEVR QQMVLLNERW
ETLRLRALDM QAKILMRLAE FQKQKLEQLR QFLTNVEDRI SHMSDLGPTI AEAEQQLAEA
RQLKADLCEQ QELVDSISSM VVIVNDTSGN FNDLEDRLSA LGERWSHVVK WIDLRTEKLQ
QYKCISRWLD AREQDLKRME SRDVTDVGGI TQRINELNYC AKDLLELHRY LIDLRQMVAA
TLQDGDDKGE RVLMQLESYE DRLDALKQIL EVQTLRIESK GFNFGRDRAS YDDSRVVRPE
GWVDYQMIIR FGEDEEDEYE PEPTQQQQQQ QQQQQEQQAG LHEPDELASK KRKLRNADNF
FALENQIQHH FSHVQDVEQQ LQQLQRQSLR NQCELLKELQ AESQQRANSL PELKKLYEVC
EQEQPGRKLL LEAAQIKQLE QRYAALAQRL ASQHSESSTL LAKERYYNSL TGFKLVLADS
RDWYKQHAGT ASCQELEQRL SHMESLATEI AEARETTEAL DDQLLEWKQD FGLFYDSWHD
MKQALQALIQ QRGGENIAQQ VQQLENFVSK VAAQKVRVSN LEAMQQQQQL LNQLVDELES
LKPCYERVPA HMLSEELQAA WQRLPEQLSE RVIKQTTAIE NLNHFVAEYN SIIAVLRSAP
EVLQTQDLRK LEIDVISARN FSEILIKEAE PPQREALQSQ IRALNALYEQ VEQLHQAQRQ
QQSAMQSQTD AIQKRLQQTE RWLNELEANT PKSGVAEIRN SNELFQSKSK FQTLKETCER
EATQFRELNE LGGELLLQMD ELQDKEKDAK YGTLAKQFTR LNARWTEVTE RVYAKTALLE
HISTQLGEFK KFMVSETGYL DRLENKIRNT TNAADAEEII EELDDLENVL RAHSDEWLDK
IQEIGNELID NEFMGDVMRQ DIDGIVERWT KLQQLAKKRT ELLEEKVSEA EQSEKAVVHL
EAWLTRMDEI LSEHLENDVT IEDLPDDFQI LAREFAINEQ NFKDISELIA EHTAKGKTGA
ANRLQEQLNL MELRFKACQA KLNKCTAPQP AYESRLNRAY GDLRNVEHST LVLDVASAGP
STVQAQYQKC LQIYRTLSEI KAQIESTIKT GRRVCEDKFT KSPKQLSQRI DALKHLYNTL
GESVTQSKAF LEGLIKLARQ LEQCFDSADD LIRRFESPQE LHDRNSILLE FEDVLQRCEE
HYNEYSKSCD KSCMQETRQR IDGLKATYHK LTSADIIKRL TEMKTTLQNL DNISLDTLKT
MEHDLKEINV PSNPEIEKLQ QQVIAIVVSR IETPSTKKPN SFLSKVLNSM PSPLDDSNVT
LKSPPSEQPS TSPINLEQRV QEFNKLAKQM IYKLELTKVK IEQGHESEAE DLRMLIAPDA
ATLISQGDSL VLETHGKQGS ISRLVMRTQI ILREKFREVQ QAKSKVTGSS AARPTPDSVN
IEELVTKGLR RINVLIEKPV NVKSSTELEK RMEDINERRD DLQVIVGAIG KNPQMPKVTP
VMMNEIEKTK NNLIAHADCV ELSLTELKNG NQIGNGNGNG NGSTNSRQDY NNEASGTGAL
ASSFDKSVLH ISDWLTWEQN MIKIQSVLVD DVDAVRLAIE KQEKVLRELK MKKPQLNELV
HTAEVLKGDI KRQQLQEKEL KQFSIAPHCS ADLDYIRCFL KVTRLREHWD ETSQCVLQRA
AQLKNMLSDS QRFEAKRLEL EKWLGRMEQR AERMGTVATT ADILEAQQKE QKSFHAELHQ
NKQHFELFSD LTQKLIAVYP NDDTTRIKKM TEALNQRYSN LNNGVINRGK QLHAAVHSLQ
SFDRAMDQFL AFLSEMETLC ENAESDVERN PMMFKDLQSE IETHRVVYDR LDGTGRKLLG
SLTSQEDAVM LQHRLDEMNQ RWNNLKSKSI AIRNRLESNS EHWHALLLSL RELTEWVIRK
DTELSSLGLG PVRGDAASLQ KQLDDHKAFR RQLEDKRPIV ESNLTSGRQY IASEAPVSDT
SDTEAAHDSD SRYMSAEEQS RELARSIRRE VGKLSEQWNN LIDRSDNWKH RLDEYMTTSS
VSVVAQILIT NTLKKMRQFQ KVLEDLSSRV ALAEQTKNAW QTPTSVGEAN EQMQQLQRLR
DKMTTASALL DDCNEQQSFF TANQVLVPTP CLSKLEDLNT RMKLLQIAMD ERQKVLCQAG
ANHTHENGDD GRNTSNSGTI GPLPNLGQSV KPPWERATTA ANVPYYIDHE RETTHWDHPE
MIELMKGLAD LNEIRFSAYR TAMKLRAVQK RLALDRISMA TACESFDRHG LRAQNDKLID
IPDMTTVLHS LYVTIDKIDL TLMLDLAINW ILNVYDSQRT GQIRVLSFKV GLVLLCRGHL
EEKYRYLFRL VADTERRADQ RRLGLLLHDC IQVPRQLGEV AAFGGSNIEP SVRSCLEQAG
ISQEAIDGNQ EISIELQHFL GWLQHEPQSL VWLPVLHRLA AAEAARHQAK CNICKEYPIV
GFRYRCLKCF NFDMCQKCFF FGRNAKNHKL THPMHEYCTT TTSTEDVRDF TRALKNKFKS
RKYFKKHPRV GYLPVQSVLE GDALESPAPS PQHTTHQLQS DMHSRLEMYA SRLAQVEYGG
TGSNSTPDSD DEHQLIAQYC QALPTNNGSA PKSPVQVMAA MDAEQREELE AIIRDLEEEN
ANLQAEYQQL CSKQQSGTPD ESNGMQHSSS SMTGLSSQGE HGQDMMAEAK LLRQHKGRLE
SRMQILEDHN RQLEAQLQRL RQLLDEPNGG GCSSANSSGL PSAPGSALNS KPNTLQTRSV
TASQLNTDSP AKMNQQNGHY EHNSKGIMLP GLSNELQQHS QLASLAAKHH QHQLSGALNA
LHQQQQQLQH SQRGVLTGNG GIDMPNSGMQ TSSYLGDDGR PPPPPHSSLL QQQMNGAKFV
GMNQFFVFFF FCFCC
//
