SUR_DROME
ID SUR_DROME Reviewed; 2171 AA.
AC Q9VL32; Q9U6Z2;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 4.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=ATP-binding cassette sub-family C member Sur;
DE AltName: Full=Sulfonylurea receptor;
DE Short=Dsur;
GN Name=Sur; ORFNames=CG5772;
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], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=10506204; DOI=10.1074/jbc.274.41.29420;
RA Nasonkin I., Alikasifoglu A., Ambrose C., Cahill P., Cheng M., Sarniak A.,
RA Egan M., Thomas P.M.;
RT "A novel sulfonylurea receptor family member expressed in the embryonic
RT Drosophila dorsal vessel and tracheal system.";
RL J. Biol. Chem. 274:29420-29425(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 FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=16882722; DOI=10.1073/pnas.0603098103;
RA Akasaka T., Klinedinst S., Ocorr K., Bustamante E.L., Kim S.K., Bodmer R.;
RT "The ATP-sensitive potassium (KATP) channel-encoded dSUR gene is required
RT for Drosophila heart function and is regulated by tinman.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11999-12004(2006).
RN [5]
RP POSSIBLE FUNCTION IN REGULATION OF SLEEP PATTERN.
RX PubMed=22105623; DOI=10.1038/mp.2011.142;
RA Allebrandt K.V., Amin N., Muller-Myhsok B., Esko T., Teder-Laving M.,
RA Azevedo R.V., Hayward C., van Mill J., Vogelzangs N., Green E.W.,
RA Melville S.A., Lichtner P., Wichmann H.E., Oostra B.A., Janssens A.C.,
RA Campbell H., Wilson J.F., Hicks A.A., Pramstaller P.P., Dogas Z., Rudan I.,
RA Merrow M., Penninx B., Kyriacou C.P., Metspalu A., van Duijn C.M.,
RA Meitinger T., Roenneberg T.;
RT "A K(ATP) channel gene effect on sleep duration: from genome-wide
RT association studies to function in Drosophila.";
RL Mol. Psychiatry 18:122-132(2013).
CC -!- FUNCTION: May function as regulatory subunit of ATP-sensitive potassium
CC channels (KATP) and form KATP channels with a member of the ATP-
CC sensitive inward rectifier potassium channel family (By similarity).
CC May also have channel activity by itself (in vitro). May protect the
CC heart during hypoxia. May protect against heart failure under
CC conditions of tachycardic stress. {ECO:0000250,
CC ECO:0000269|PubMed:10506204, ECO:0000269|PubMed:16882722}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in adult heart. Detected at lower
CC levels in head and abdomen. {ECO:0000269|PubMed:16882722}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryonic myocardial cells and in the
CC developing heart tube. Detected in embryonic dorsal vessels and
CC tracheal system. {ECO:0000269|PubMed:10506204,
CC ECO:0000269|PubMed:16882722}.
CC -!- MISCELLANEOUS: Drosophila is predominantly active around dawn and dusk,
CC and has large sleep periods during the day and during night. Knockdown
CC of Sur reduces sleep duration during the first half of the night, but
CC has little effect on sleep during the day (PubMed:22105623).
CC {ECO:0000305|PubMed:22105623}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF06736.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=On The Other Side - Issue
CC 139 of June 2012;
CC URL="https://web.expasy.org/spotlight/back_issues/139";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF167431; AAF06736.1; ALT_INIT; mRNA.
DR EMBL; AE014134; AAF52866.4; -; Genomic_DNA.
DR AlphaFoldDB; Q9VL32; -.
DR BioGRID; 60441; 1.
DR IntAct; Q9VL32; 3.
DR STRING; 7227.FBpp0288707; -.
DR PaxDb; Q9VL32; -.
DR FlyBase; FBgn0028675; Sur.
DR VEuPathDB; VectorBase:FBgn0028675; -.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_8_1; -.
DR InParanoid; Q9VL32; -.
DR OMA; THVEKEM; -.
DR PhylomeDB; Q9VL32; -.
DR Reactome; R-DME-189483; Heme degradation.
DR Reactome; R-DME-382556; ABC-family proteins mediated transport.
DR Reactome; R-DME-9749641; Aspirin ADME.
DR Reactome; R-DME-9753281; Paracetamol ADME.
DR Reactome; R-DME-9754706; Atorvastatin ADME.
DR SignaLink; Q9VL32; -.
DR ChiTaRS; Sur; fly.
DR PRO; PR:Q9VL32; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR ExpressionAtlas; Q9VL32; baseline and differential.
DR Genevisible; Q9VL32; DM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0001666; P:response to hypoxia; IMP:FlyBase.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Hydrolase; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..2171
FT /note="ATP-binding cassette sub-family C member Sur"
FT /id="PRO_0000415415"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 58..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 93..112
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 134..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 167..182
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 204..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 246..299
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 321..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 469..474
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 496..562
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 563..583
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 584..600
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 601..621
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 622..1409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1410..1430
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1431..1468
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1469..1489
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1490..1558
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1559..1579
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1580..1655
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1656..1676
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1677..1718
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1719..1739
FT /note="Helical; Name=16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1740..2171
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 344..622
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 785..1014
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1421..1715
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1930..2165
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 388..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1193..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1766..1844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1866..1902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1779..1800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1878..1892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 822..829
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1964..1971
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 34..35
FT /note="VR -> CA (in Ref. 1; AAF06736)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="C -> Y (in Ref. 1; AAF06736)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="L -> I (in Ref. 1; AAF06736)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="D -> E (in Ref. 1; AAF06736)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="M -> V (in Ref. 1; AAF06736)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="S -> G (in Ref. 1; AAF06736)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="N -> S (in Ref. 1; AAF06736)"
FT /evidence="ECO:0000305"
FT CONFLICT 731
FT /note="R -> G (in Ref. 1; AAF06736)"
FT /evidence="ECO:0000305"
FT CONFLICT 1022
FT /note="K -> E (in Ref. 1; AAF06736)"
FT /evidence="ECO:0000305"
FT CONFLICT 1603
FT /note="A -> T (in Ref. 1; AAF06736)"
FT /evidence="ECO:0000305"
FT CONFLICT 1757
FT /note="H -> Q (in Ref. 1; AAF06736)"
FT /evidence="ECO:0000305"
FT CONFLICT 1763..1766
FT /note="Missing (in Ref. 1; AAF06736)"
FT /evidence="ECO:0000305"
FT CONFLICT 1772
FT /note="A -> T (in Ref. 1; AAF06736)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2171 AA; 242375 MW; 5BA7802AD742B6D2 CRC64;
MKQLFNIIHC DHLNGHVRSI YDNLNTDICG IDRVRRVFTF FSIFLLLFGL MFVCSRYKKC
HKTLLTFHNG RAAISLLLLA LNSFDLARIF LPHQNVRNLN RLFQSSPRDL NYLVVIGSGE
LWNALFSTLL TLMLMLYHRM VERKKATVFL YASTAVEALT FALLSNELFE LVRYEDFLEL
QTCLVAMSAM CMVSLAMLDG LTVYKECYHD DYLDDYGKIG YKHSMATFYS KSCFWWLTPL
LWLGYKEPLE LEDLGQMKLE DSARSHYDHF LYIYTEKKKK SNSSPSLWYC YIKNSWQMFA
LGGILKLAGD LFALIGPLAI QKIVEYIEQL YAQASEPPAK SPGNEVANVL LSTSRILGTE
FDEVFGTNID KGLIYRKSLL LNADGGCDSS DSAGQVQSTS STSDEKQKND DSMATPEHVD
NPSEPNISHD IGSITNHMTE DTRNIMEFFL IIHYAWAIPF KIAVVIYLLY MNLGISAVIG
SIACIVIMTP LQFFIGNAMS KNAEVIAGYT DERLKRIHDT LVGIKVIKLN AWDEVFLKKI
QEARRKELKY LNKDATFWTL MAVLTHIATV LITFVTLGVY VWLHRDQEFD LNASRLFSSL
ALFQQLTVPL LIFPITVPII IAARVSTRRL ERFLKSSEIQ KQFEGIRNMA RILSKSDASL
DMYETQEKSN MTMRTAQAEN RLNEKRLAQK SQTPELATNS TPLLQNAEES AEDISPSTVQ
ELGHNKLVQQ RRELLRNTPY VAIRPPKMRG SVMERPVEFS VIRARNTDSW RRDSLLLKMP
DDIAVSINDG LFTWQPQSQM PVVQLHVPGI IVPKGKLTIV VGKNGSGKTS LLSALLMEMP
LLAGNMFWHK TCTISYVSQQ PWLLNDTIRE NILFGESFRP KRYDFVLEAC ALKPDIELMP
RGDLSIIGER GINISGGQRQ RIAIARAIYS SANVVIMDDP LASLDNEVGE HIFQHCIREM
LQKSNRTFIL VTQQLHRIKE AEYLIAIKDG RVEACGSYAD IELMQPRITA EWNAIIAMAK
AKNDNPSQNP GEKTAGERWK LLKNVSKLGL QRSISVTMDA NVACHADAID GSGCISVANM
QSNVVEEDDQ VSVSYPIGNA SCGGFNLQRK RSSIYGSRHL MYDVPLPIDE CQGDDVIMRP
RRRHTLGRRG SRNTNSSHRL SGLSTLTATS ESSSISGDVL SRSVLATSCS SYAESSVDGG
DLATAAPEPR VQSWQPPQHV THHQPLSRNA SSPPAMEVAN PDVKKSEEAR RSNTSSESPL
DDHVRGSFQQ FLRRMSMRRS NKPKNHHHPL SATNSILSIS EESPPVVHFP ASILATDGNK
NETQSEEKPK KCVNIDSKET TINCDDNCYS ASDKELRANV TSSPADQEQH NERHVLAEVA
GESGRESMPL ARLAIDTERK YGKISDDIYL MYIRAAGLPI ITIFFITALI WQCLRVYTDI
WLQQWSNVHG RVASKGHVVL HPSEQDHEVT YYFRMYAAIS CVCIIMALVS TPAGQYAGCN
ARRNLHDKLL QTILHKTLHF FQVTPLGRIV NRFSNDMAVI DKKIAATGQR LLQFTLLCLS
AILINVTITP WILVLTLPIC GAYYLIQKFY RCSARELQRI ENATNSPVIS HLSETIQGVT
TIRAFNQQTR FTEILFKRLE ANTIAYALLN TSHRWLGVSL DYLGGCIVFV ATVTALTAAS
VSCRRHYEAT TSPSASASPS PFETYAVTKS PSELRPSPSL VGLAINYTLL VPIYLNWVVK
LLADMEMYAG SVERIAHYAQ GQDADADADA DADADVDADL DHEPSSNEDV SAEVDRSSQS
DAGDKVYPGA TTAAGDVDED GDQQRIGGAR GGGGDCGYRQ GHENGAEANA DKLNAGNVTG
DGNHLNFHHP PATAGDKVEQ ATTKTSVIKD KQLPPQQDDK DKKVVLPNEP ARKLERYQSV
PISWPQRGDI HFDNVSLRYE GQKQNVISNL TLKIPAGQRI GICGRTGSGK SSLGLSLFGV
LQTTRGHIYI DDVDIQRIRP DELRTRLSII PQDVHLFNAT IRENLDPHGY FQDLQLWNCL
ELAQLKEFVN GHLPLGLDTV ICDGGLNLSA GHRQLLCLAR AILRGSVCLV LDEATSVLDS
STESALLKAA DLAFRGRTII TIAHRLTTIL DYDRLIVLDQ GRIVEDGNPR ELQQLEGSVF
RGLLEKGASK W
