DSCL_DROME
ID DSCL_DROME Reviewed; 2074 AA.
AC Q9VS29; B7Z0C6; B7Z0C7; B7Z0C8; Q0E8H6; Q8MTB2; Q9VS28; Q9VS30;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Cell adhesion molecule Dscam2 {ECO:0000305};
DE AltName: Full=Down syndrome cell adhesion molecule-like protein Dscam2;
DE Flags: Precursor;
GN Name=Dscam2; ORFNames=CG42256;
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] {ECO:0000312|EMBL:AAF50601.3}
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 [2] {ECO:0000305, ECO:0000312|EMBL:AAF50601.3}
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAM48303.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 317-1780 (ISOFORM J).
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Testis {ECO:0000269|PubMed:12537569};
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 [4] {ECO:0000305}
RP IDENTIFICATION.
RX PubMed=14623821; DOI=10.1242/dev.00848;
RA Vogel C., Teichmann S.A., Chothia C.;
RT "The immunoglobulin superfamily in Drosophila melanogaster and
RT Caenorhabditis elegans and the evolution of complexity.";
RL Development 130:6317-6328(2003).
CC -!- FUNCTION: Cell adhesion molecule. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=J {ECO:0000269|PubMed:10731132};
CC IsoId=Q9VS29-1; Sequence=Displayed;
CC Name=E {ECO:0000269|PubMed:10731132};
CC IsoId=Q9VS29-2; Sequence=VSP_053091, VSP_053092;
CC Name=F {ECO:0000269|PubMed:10731132};
CC IsoId=Q9VS29-3; Sequence=VSP_053094, VSP_053095;
CC Name=G {ECO:0000269|PubMed:10731132};
CC IsoId=Q9VS29-4; Sequence=VSP_053097, VSP_053098;
CC Name=H {ECO:0000269|PubMed:10731132};
CC IsoId=Q9VS29-5; Sequence=VSP_053097;
CC Name=I {ECO:0000269|PubMed:10731132};
CC IsoId=Q9VS29-6; Sequence=VSP_053093, VSP_053097, VSP_053098;
CC Name=K {ECO:0000269|PubMed:10731132};
CC IsoId=Q9VS29-7; Sequence=VSP_053096, VSP_053098;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM48303.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM48303.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AE014296; AAF50600.3; -; Genomic_DNA.
DR EMBL; AE014296; AAF50601.3; -; Genomic_DNA.
DR EMBL; AE014296; AAF50602.3; -; Genomic_DNA.
DR EMBL; AE014296; ABI31239.2; -; Genomic_DNA.
DR EMBL; AE014296; ACL83251.1; -; Genomic_DNA.
DR EMBL; AE014296; ACL83252.1; -; Genomic_DNA.
DR EMBL; AE014296; ACL83253.1; -; Genomic_DNA.
DR EMBL; AY118274; AAM48303.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001036588.2; NM_001043123.3. [Q9VS29-6]
DR RefSeq; NP_001137896.1; NM_001144424.2. [Q9VS29-7]
DR RefSeq; NP_001137897.1; NM_001144425.2. [Q9VS29-2]
DR RefSeq; NP_001137898.1; NM_001144426.2. [Q9VS29-3]
DR RefSeq; NP_729223.2; NM_168194.4. [Q9VS29-5]
DR RefSeq; NP_729224.2; NM_168195.3. [Q9VS29-4]
DR RefSeq; NP_729225.2; NM_168196.4. [Q9VS29-1]
DR AlphaFoldDB; Q9VS29; -.
DR SMR; Q9VS29; -.
DR BioGRID; 64233; 2.
DR STRING; 7227.FBpp0288826; -.
DR PaxDb; Q9VS29; -.
DR EnsemblMetazoa; FBtr0299546; FBpp0288821; FBgn0265296. [Q9VS29-2]
DR EnsemblMetazoa; FBtr0299547; FBpp0288822; FBgn0265296. [Q9VS29-3]
DR EnsemblMetazoa; FBtr0299548; FBpp0288823; FBgn0265296. [Q9VS29-4]
DR EnsemblMetazoa; FBtr0299549; FBpp0288824; FBgn0265296. [Q9VS29-5]
DR EnsemblMetazoa; FBtr0299550; FBpp0288825; FBgn0265296. [Q9VS29-6]
DR EnsemblMetazoa; FBtr0299551; FBpp0288826; FBgn0265296. [Q9VS29-1]
DR EnsemblMetazoa; FBtr0299552; FBpp0288827; FBgn0265296. [Q9VS29-7]
DR GeneID; 38788; -.
DR KEGG; dme:Dmel_CG42256; -.
DR UCSC; CG42256-RE; d. melanogaster.
DR CTD; 38788; -.
DR FlyBase; FBgn0265296; Dscam2.
DR VEuPathDB; VectorBase:FBgn0265296; -.
DR eggNOG; KOG3510; Eukaryota.
DR InParanoid; Q9VS29; -.
DR PhylomeDB; Q9VS29; -.
DR Reactome; R-DME-1474228; Degradation of the extracellular matrix.
DR Reactome; R-DME-210991; Basigin interactions.
DR Reactome; R-DME-216083; Integrin cell surface interactions.
DR Reactome; R-DME-376172; DSCAM interactions.
DR Reactome; R-DME-428542; Regulation of commissural axon pathfinding by SLIT and ROBO.
DR Reactome; R-DME-433692; Proton-coupled monocarboxylate transport.
DR Reactome; R-DME-70268; Pyruvate metabolism.
DR Reactome; R-DME-9749641; Aspirin ADME.
DR BioGRID-ORCS; 38788; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Dscam2; fly.
DR GenomeRNAi; 38788; -.
DR PRO; PR:Q9VS29; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0265296; Expressed in brain and 8 other tissues.
DR ExpressionAtlas; Q9VS29; baseline and differential.
DR Genevisible; Q9VS29; DM.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:FlyBase.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:FlyBase.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:FlyBase.
DR CDD; cd00063; FN3; 6.
DR Gene3D; 2.60.40.10; -; 16.
DR InterPro; IPR043204; Basigin-like.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR PANTHER; PTHR10075; PTHR10075; 3.
DR Pfam; PF00041; fn3; 5.
DR Pfam; PF07679; I-set; 4.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00060; FN3; 6.
DR SMART; SM00409; IG; 9.
DR SMART; SM00408; IGc2; 9.
DR SUPFAM; SSF48726; SSF48726; 9.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 6.
DR PROSITE; PS50835; IG_LIKE; 9.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell adhesion; Disulfide bond; Immunoglobulin domain;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..2074
FT /note="Cell adhesion molecule Dscam2"
FT /id="PRO_0000376054"
FT TOPO_DOM 22..1619
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1620..1640
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1641..2074
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..120
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 238..326
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255"
FT DOMAIN 330..417
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255"
FT DOMAIN 422..516
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255"
FT DOMAIN 521..607
FT /note="Ig-like C2-type 5"
FT /evidence="ECO:0000255"
FT DOMAIN 612..698
FT /note="Ig-like C2-type 6"
FT /evidence="ECO:0000255"
FT DOMAIN 707..802
FT /note="Ig-like C2-type 7"
FT /evidence="ECO:0000255"
FT DOMAIN 805..902
FT /note="Ig-like C2-type 8"
FT /evidence="ECO:0000255"
FT DOMAIN 907..1003
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1008..1108
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1113..1211
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1215..1311
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1312..1400
FT /note="Ig-like C2-type 9"
FT /evidence="ECO:0000255"
FT DOMAIN 1402..1495
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1496..1595
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1739..1766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1778..1917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1936..1974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2011..2074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1828..1844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1858..1917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2039..2066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 53..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 259..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 352..400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 444..500
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 541..590
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 633..686
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 728..783
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 826..884
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1334..1382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 520..543
FT /note="LPYIRLIPKVTAVSGETLNLKCPV -> TLYSHTHGMHSKHTDAHMRKMLMA
FT (in isoform E)"
FT /evidence="ECO:0000303|PubMed:10731132"
FT /id="VSP_053091"
FT VAR_SEQ 544..2074
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000303|PubMed:10731132"
FT /id="VSP_053092"
FT VAR_SEQ 613..704
FT /note="SIEPFAFQEGLAEGMRTRTVCGVSRGDPPLKLIWLKDGDPLPDLLGANVTML
FT DQYSSLLSIPSLSATHSGEYTCVAKNPAAEIKYTALLQVK -> KLSPFQTNILQLNMG
FT DRASLTCSVVKGDLPLTINWRKDGRPIDPTQHMSVKQVDQYNSILVIENLGSDHTGNYS
FT CVVRNSAAEVENSQALLVN (in isoform I)"
FT /evidence="ECO:0000303|PubMed:10731132"
FT /id="VSP_053093"
FT VAR_SEQ 705..752
FT /note="VPPRWIVEPVDANVERNRHIMLHCQAQGVPTPSIVWKKATGSKSGEYE ->
FT GSVLAYPSQKLNTEHKKRKPHKYRSHLLSKLKLSQCSLTLAASLKPFI (in
FT isoform F)"
FT /evidence="ECO:0000303|PubMed:10731132"
FT /id="VSP_053094"
FT VAR_SEQ 753..2074
FT /note="Missing (in isoform F)"
FT /evidence="ECO:0000303|PubMed:10731132"
FT /id="VSP_053095"
FT VAR_SEQ 1645..1654
FT /note="MLKNAPPLAE -> K (in isoform K)"
FT /evidence="ECO:0000303|PubMed:10731132"
FT /id="VSP_053096"
FT VAR_SEQ 1749..1782
FT /note="Missing (in isoform G, isoform H and isoform I)"
FT /evidence="ECO:0000303|PubMed:10731132"
FT /id="VSP_053097"
FT VAR_SEQ 1825..2074
FT /note="SIIYHGAQSSTSSDLSPMSEQKSLPRRGRSRYHHQQYQFSTNTTPRHHNSNK
FT MNNNTTSNTNTTATNTTATPSTSSNSNKILSPRGGNLKSISSTFKSQDSIQCHIPTLVK
FT SPSISTQQQKQFHKQQLQNSSTNNSQHSSSNPNSSSLKQQQPLLITPKLHQLEANGQEL
FT LGLDGIGNSPLVACMPPSSQFRPIPHKSIMPAHEPPHHHNHSQQSHPHQQQQQQQHPGT
FT LLNPSTAMLSSKFFTAPTLPK -> NSRLIQHFPNHNISITYL (in isoform G,
FT isoform I and isoform K)"
FT /evidence="ECO:0000303|PubMed:10731132"
FT /id="VSP_053098"
FT CONFLICT 1640
FT /note="V -> I (in Ref. 3; AAM48303)"
FT /evidence="ECO:0000305"
FT CONFLICT 1755
FT /note="T -> A (in Ref. 3; AAM48303)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2074 AA; 227598 MW; 74D0AB835A093A0A CRC64;
MWISSRFFVI LLLLNLDNTC SEPFEAHLRG PGFVMEPPGR VEFSNSSGGW LDCSASGSPQ
PTVDWVHADG SAVTEIHGVR RVLRNGTLVL MPFAAAAYHQ DVHNTIYRCI ASNSVGRIVS
RDVQVRAVVA QAYKVDVEVL SAARGCTAIL RCVVPTFVKE LVRVVSWVHE PAIYIYPSLQ
GDGKFHLLPT GELLIHNLQE SDESQSFRCR SMHRLTRQVV VSSPTRLRIN SHRGIISPSV
VEHTAHVQVS QDEGAVLLCV AQGCPSPEYS WFTHNGAGPL PVLSGPRVRL LGPILAIEAV
TGEDSGVYKC TAGNVGGEAS AELRLTVATP IQVEISPNVL SVHMGGTAEF RCLVTSNGSP
VGMQNILWYK DGRQLPSSGR VEDTLVVPRV SRENRGMYQC VVRRPEGDTF QATAELQLGD
APPVLLYSFI EQTLQPGPAV SLKCSAAGNP TPQISWTLDG FPLPSNGRFM IGQYITVHGD
VISHVNISHV MVEDGGEYAC IAENRAGRVQ HAARLNIYGL PYIRLIPKVT AVSGETLNLK
CPVAGYPIEE IHWERGGREL PDDIRQRVQP DGSLTISPVQ KNSDSGVYTC WARNKQGHSA
RRSGEVTVIV PPSIEPFAFQ EGLAEGMRTR TVCGVSRGDP PLKLIWLKDG DPLPDLLGAN
VTMLDQYSSL LSIPSLSATH SGEYTCVAKN PAAEIKYTAL LQVKVPPRWI VEPVDANVER
NRHIMLHCQA QGVPTPSIVW KKATGSKSGE YEEVRERPFT KLLGNGSLLL QHVKEDREGF
YLCQANNGIG TGIGKVIQLK VNSSPYFSST SRSVMVKKGD TALLQCAVSG DKPINIVWMR
SGKNTLNPST NYKISVKQEA TPDGVSAELQ IRTVDATDSG PYFCRASNLY GNDQQLVQLQ
VQEPPLPPSV LEAAMISSRS VNIKWQPKTL GTGDVTKYIV EFREADPLFV DQWQQIEVKD
PPHFNAMIEN LKPATRYAFR VIAEGSAGRS APSQELIVRT EPQRPAGPPL SLSARPLSST
ELLISWVAPL PELRHGDIQG YNVGYKLSSS GNTAYNFTSV SGDGDGGNGE LLLSGLAKFA
RYTVVVQAFN QVGPGPLSEP TAAQTMEDVP SRPPEDVRCA ALSSQSLQVS WQPPPIYHTN
GLLQGYKLIF EPIIDDIQPS KDEVESRKTT ALTMVLTGLR KYTNYSIQVL AHTRMGDGVV
SKPLFCHSEE DVPEAPADIK VVSSSSQSLY ISWLPPNEPN GVITKYSLYT RVVNGREELN
NEKRSLPSQQ AYYEAKGLHP HMEYQFWVTA STRVGEGKSS RVSSQITTNR IPARIISFGG
PVVRPWRSTV TLPCTAVGKP KREWFKSDVA LRQGGLHNSQ LLDSGDLIIS SLQLADGGNY
SCQVDNGIGT DRLTHTLIVQ VPPTAPVLYV TSATSSSILM HWKCGFTGNA PITGYTLFYR
RANGNTDEMQ LSRHASSHEL KGLMCGSTYQ IHLSAQNKVG TSPTSTILHV RTQGQSPGHP
ASTALLAPNS TSLLVRLHSW PDNGCPLLYF VLQYRAVTDD PDAEWVLVSN ALKPQRRIVI
NNLQPSTLYQ LRMEAHNVAG ISQAEFNFVT LTKDGDPPPP EIMHRGRSGQ TTVIFANINL
LIPTIAAVSG MFCTIIMIIV CYRHMLKNAP PLAEQSQIQK ESLENRANSE AAQRERYYAT
IHKVSMQNND KIPETSEDIS PYATFQLSEA GGNMSQPHHG GPANTLLHSF MYHERALAEG
CSSPPPAAVL NPPTTTTHHH HHHQRPLKTI HNYYQTSPFH NISKNRRRHS RKTEPESEES
ESDQDQLTSS RTESSNQHEG KIKHSIIYHG AQSSTSSDLS PMSEQKSLPR RGRSRYHHQQ
YQFSTNTTPR HHNSNKMNNN TTSNTNTTAT NTTATPSTSS NSNKILSPRG GNLKSISSTF
KSQDSIQCHI PTLVKSPSIS TQQQKQFHKQ QLQNSSTNNS QHSSSNPNSS SLKQQQPLLI
TPKLHQLEAN GQELLGLDGI GNSPLVACMP PSSQFRPIPH KSIMPAHEPP HHHNHSQQSH
PHQQQQQQQH PGTLLNPSTA MLSSKFFTAP TLPK
