TENA_DROME
ID TENA_DROME Reviewed; 3004 AA.
AC Q9VYN8; Q24550;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Teneurin-a;
DE Short=Tena;
DE AltName: Full=Tenascin-like protein;
GN Name=Ten-a {ECO:0000312|FlyBase:FBgn0267001};
GN ORFNames=CG42338 {ECO:0000312|FlyBase:FBgn0267001};
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].
RC STRAIN=Canton-S;
RX PubMed=7684246; DOI=10.1016/0925-4773(93)90074-8;
RA Baumgartner S., Chiquet-Ehrismann R.;
RT "Tena, a Drosophila gene related to tenascin, shows selective transcript
RT localization.";
RL Mech. Dev. 40:165-176(1993).
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 HOMODIMERIZATION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=12175511; DOI=10.1016/s0925-4773(02)00055-2;
RA Fascetti N., Baumgartner S.;
RT "Expression of Drosophila Ten-a, a dimeric receptor during embryonic
RT development.";
RL Mech. Dev. 114:197-200(2002).
RN [5]
RP FUNCTION IN SYNAPSE FORMATION, HOMODIMERIZATION, HETERODIMERIZATION,
RP INTERACTION WITH TEN-M, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=22425994; DOI=10.1038/nature10926;
RA Hong W., Mosca T.J., Luo L.;
RT "Teneurins instruct synaptic partner matching in an olfactory map.";
RL Nature 484:201-207(2012).
RN [6]
RP FUNCTION IN NEUROMUSCULAR SYNAPSE FORMATION, INTERACTION WITH TEN-M, AND
RP SUBCELLULAR LOCATION.
RX PubMed=22426000; DOI=10.1038/nature10923;
RA Mosca T.J., Hong W., Dani V.S., Favaloro V., Luo L.;
RT "Trans-synaptic Teneurin signalling in neuromuscular synapse organization
RT and target choice.";
RL Nature 484:237-241(2012).
CC -!- FUNCTION: Involved in neural development, regulating the establishment
CC of proper connectivity within the nervous system. Acts as a homophilic
CC and heterophilic synaptic cell adhesion molecule that drives synapse
CC assembly. Promotes bi-directional trans-synaptic signaling with ten-m
CC to organize neuromuscular synapses. {ECO:0000269|PubMed:22425994,
CC ECO:0000269|PubMed:22426000}.
CC -!- SUBUNIT: Homodimer. Heterodimer with Ten-m; the interaction occurs at
CC the neuromuscular junction.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon. Presynaptic cell membrane.
CC Synapse, synaptosome. Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Note=Localizes in the cell body and axon of
CC neuronal cells. Localizes at neuromuscular junction.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000305}; Synonyms=D {ECO:0000312|FlyBase:FBgn0267001}, F
CC {ECO:0000312|FlyBase:FBgn0267001}, I {ECO:0000312|FlyBase:FBgn0267001},
CC K {ECO:0000312|FlyBase:FBgn0267001}, N
CC {ECO:0000312|FlyBase:FBgn0267001};
CC IsoId=Q9VYN8-1; Sequence=Displayed;
CC Name=2; Synonyms=O {ECO:0000312|FlyBase:FBgn0267001};
CC IsoId=Q9VYN8-2; Sequence=VSP_058144, VSP_058145;
CC -!- DEVELOPMENTAL STAGE: Expressed in the developing antennal lobe.
CC Expressed in subset of matching olfactory receptor neurons (ORN) and
CC projection neurons (PN) in select glomeruli between 12 to 48 hours
CC after puparium formation (apf) (at protein level).
CC {ECO:0000269|PubMed:12175511, ECO:0000269|PubMed:22425994}.
CC -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC {ECO:0000305}.
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DR EMBL; X68794; CAA48691.2; -; mRNA.
DR EMBL; AE014298; AAF48154.2; -; Genomic_DNA.
DR EMBL; AE014298; ACL82922.1; -; Genomic_DNA.
DR EMBL; AE014298; ACZ95266.1; -; Genomic_DNA.
DR EMBL; AE014298; ACZ95267.2; -; Genomic_DNA.
DR RefSeq; NP_001138190.1; NM_001144718.3. [Q9VYN8-1]
DR RefSeq; NP_001162731.1; NM_001169260.3. [Q9VYN8-1]
DR RefSeq; NP_001162732.2; NM_001169261.3. [Q9VYN8-2]
DR RefSeq; NP_001245640.1; NM_001258711.2. [Q9VYN8-1]
DR RefSeq; NP_001259483.1; NM_001272554.2. [Q9VYN8-1]
DR RefSeq; NP_511137.3; NM_078582.4. [Q9VYN8-1]
DR SMR; Q9VYN8; -.
DR BioGRID; 58586; 4.
DR IntAct; Q9VYN8; 5.
DR STRING; 7227.FBpp0289137; -.
DR PaxDb; Q9VYN8; -.
DR EnsemblMetazoa; FBtr0299858; FBpp0289136; FBgn0267001. [Q9VYN8-1]
DR EnsemblMetazoa; FBtr0299860; FBpp0289138; FBgn0267001. [Q9VYN8-1]
DR EnsemblMetazoa; FBtr0300203; FBpp0289440; FBgn0267001. [Q9VYN8-1]
DR EnsemblMetazoa; FBtr0308221; FBpp0300541; FBgn0267001. [Q9VYN8-1]
DR EnsemblMetazoa; FBtr0310078; FBpp0301779; FBgn0267001. [Q9VYN8-1]
DR EnsemblMetazoa; FBtr0346129; FBpp0311958; FBgn0267001. [Q9VYN8-2]
DR GeneID; 32183; -.
DR KEGG; dme:Dmel_CG42338; -.
DR CTD; 32183; -.
DR FlyBase; FBgn0267001; Ten-a.
DR VEuPathDB; VectorBase:FBgn0267001; -.
DR eggNOG; KOG1225; Eukaryota.
DR eggNOG; KOG4659; Eukaryota.
DR GeneTree; ENSGT01030000234566; -.
DR InParanoid; Q9VYN8; -.
DR PhylomeDB; Q9VYN8; -.
DR SignaLink; Q9VYN8; -.
DR BioGRID-ORCS; 32183; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Ten-a; fly.
DR GenomeRNAi; 32183; -.
DR PRO; PR:Q9VYN8; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0267001; Expressed in wing disc and 13 other tissues.
DR ExpressionAtlas; Q9VYN8; baseline and differential.
DR Genevisible; Q9VYN8; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0048788; C:cytoskeleton of presynaptic active zone; IMP:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; ISS:FlyBase.
DR GO; GO:0005576; C:extracellular region; ISM:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0048786; C:presynaptic active zone; IDA:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0048036; P:central complex development; IMP:FlyBase.
DR GO; GO:0048790; P:maintenance of presynaptic active zone structure; IMP:UniProtKB.
DR GO; GO:0008045; P:motor neuron axon guidance; IBA:GO_Central.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:UniProtKB.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:UniProtKB.
DR GO; GO:0001941; P:postsynaptic membrane organization; IMP:UniProtKB.
DR GO; GO:0097090; P:presynaptic membrane organization; IMP:UniProtKB.
DR GO; GO:0034110; P:regulation of homotypic cell-cell adhesion; IDA:UniProtKB.
DR GO; GO:2000331; P:regulation of terminal button organization; IMP:UniProtKB.
DR GO; GO:0050808; P:synapse organization; IDA:UniProtKB.
DR GO; GO:0051124; P:synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0016200; P:synaptic target attraction; IMP:FlyBase.
DR GO; GO:0008039; P:synaptic target recognition; IDA:UniProtKB.
DR GO; GO:0048499; P:synaptic vesicle membrane organization; IMP:UniProtKB.
DR CDD; cd00055; EGF_Lam; 1.
DR Gene3D; 2.120.10.30; -; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR InterPro; IPR028916; Tox-GHH_dom.
DR InterPro; IPR006530; YD.
DR Pfam; PF07974; EGF_2; 2.
DR Pfam; PF15636; Tox-GHH; 1.
DR SMART; SM00181; EGF; 8.
DR SUPFAM; SSF50952; SSF50952; 1.
DR TIGRFAMs; TIGR01643; YD_repeat_2x; 1.
DR PROSITE; PS00022; EGF_1; 8.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Cell projection;
KW Disulfide bond; EGF-like domain; Membrane; Neurogenesis;
KW Reference proteome; Repeat; Synapse; Synaptosome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..3004
FT /note="Teneurin-a"
FT /id="PRO_0000421020"
FT TOPO_DOM 1..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..3004
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 582..618
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 620..652
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 689..722
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 784..819
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1234..1275
FT /note="NHL 1"
FT REPEAT 1276..1320
FT /note="NHL 2"
FT REPEAT 1406..1451
FT /note="NHL 3"
FT REPEAT 1466..1509
FT /note="NHL 4"
FT REGION 42..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1545..1597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2831..2862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2969..3004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2843..2862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2982..3004
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 586..595
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 591..606
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 608..617
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 624..635
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 642..651
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 697..710
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 712..721
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 788..798
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 792..807
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 809..818
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 1..49
FT /note="MTMKSMKYSDCDTIMDGYNPVPPPLPRRVPPVRNIYAEPFAHEPNHSSR ->
FT MSSSHSGTIGRKRVGSGSAAGSEYYYASGGLGGLTGSSNGGGNGGGEQLRRQRSAEWHS
FT HGRHGHGHGLSHGMGHGMGHGYGSSSEDEYQNTGQATAFDTQLLAQLLLQSQQLASMEH
FT YNSDCEPDYLRQRDRHHEEATPLGDGTPTVTAAAPEVTYAQPHQQRSTMPAGSPLKVST
FT VSAGKYQSNANLGLFPNSSSSGGSSVQNGVTAHTPRSTNPFLNGSTKFASDDGGLENIN
FT MLKPSASSSTAASSSIRSSHRNRNALNRLSGMTSSSSDSQTHHHQQQQQQQQQQQQQQQ
FT QQQLQISQQQQQQIAAVKQQQQMLPPEDSGDDDFVLGLGSLELGNCSSGGESEEPPPEP
FT APPEIPPRTQSLLMSLRKHSDYKLKYEEKGDQKHEEFIPTSQLQKDYILSDNLRSDQQL
FT KPISPGDSNG (in isoform 2)"
FT /id="VSP_058144"
FT VAR_SEQ 904
FT /note="N -> NLFWSSFTPC (in isoform 2)"
FT /id="VSP_058145"
FT CONFLICT 816
FT /note="R -> S (in Ref. 1; CAA48691)"
FT /evidence="ECO:0000305"
FT CONFLICT 1551
FT /note="G -> S (in Ref. 1; CAA48691)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3004 AA; 327437 MW; 1E56738C4F785936 CRC64;
MTMKSMKYSD CDTIMDGYNP VPPPLPRRVP PVRNIYAEPF AHEPNHSSRL GGHPQQMPQS
MSTGSNTIGH GGIDRGGVGL PMGAGTMPGG VGGGPGGVAG GGPQVGVGPP GSGNGGNCQI
SGSQPLVMPG FPLRNSHSAH APHYSPYSPS RFHIDKRCQH RCSWKCLSIA LIFVSVVLTA
MLAYFAAVSS MKPNMDSTNC ILVQDVKSQP HDLRGGLAKS NEKGVATAFP TEESIQTSTS
DHGQNGHGLM NPSAGSGGSN SGIQQQLLLQ QQQPHSINQP LTPLDATNTH LQDHHQLTYG
GALPGGVGGI GMSGGGIMNG GLNGGLGGQL MQQPGGGLNG HHHQALQPQL GGVVELKEFN
EAYHATIPAY QFWTLEFRNK HPAFIRFNFT LPWGAHFAVY SRRNVAPSVT QHDFVEFIKG
GRLDSHLRHR RSSANATTTG QDMELYRQDK DQSAESAQDQ DSEQDESRSF DSSESYDVET
PLDTAKQHLQ RIGKPQSHWV NKRSAGDGLP ALDVDAMTVN VSLLQYLDTG LWFISVYNDE
LVAHSVSLLA EEAEGVSTTC PNDCSGRGSC YLGKCDCIDG YQGVDCSKSV CPVLCSAHGH
YGGGVCHCEE GWKGAECDIP VGECEVPNCS SHGRCIEGEC HCERGWKGPY CDQHDCLDPL
CSGHGTCVAG QCYCKAGWQG EDCGTIDQQV YQCLPGCSEH GTYDLETGQC VCERHWTGPD
CSQAVCSLDC GRNGVCESGK CRCNSGWTGN LCDQLPCDSR CSEHGQCKNG TCVCSQGWNG
RHCTLPGCEN GCSRHGQCTL ENGEYRCDCI EGWAGRDCSI ALELNCKDNI DNDGDGMTDC
SDSECCSHPA CSEHIMCLSS NDPVEVLLRK QPPSVTASFY QRVKFLIEEN SVQSYAHMDE
YSENRVSVMR GQVITPQGLG IVGIRVSVDR DSRFGFTLTR QGGWFDVLVN GGGAVTLQFQ
RSPFRPLTRT VFVPWNRIVV LPPVQMQLSD DDETTSRNIK VAPLNPALTF LNSIHYHTAD
EANDASKVCM DHDHEKLRPQ LISTWMPNGV GAMPGKRVIF AETQIVQESI QIPGSDLHLT
YQSSQASGYL SIVRMRLTGE TIPPTLTHVH VGVEIEGALH VKTYEADPSL VHTFAWNKRN
VYRQKVYGVT VARISVGYQH STCQSPVWIA QTAKLQGYDV DISDIGGWGL DIHHHYNFHE
GILQKGDGST LHMKEYPRTV KVVMGTGLQR PLTCPDYCNG VAKDAKLLTP IALATGPDGS
LYVGDFNLVR RITPDGKVYT ILQLSATQVS YQYYLAVSPA DGHLYISDPE RHQILRLVRL
EKVKDPSINS DPVVGSGQRC IPGDEGNCGD GGPALLARLS HPKGLAIAAD RTMYIADGTN
IRAVDPKGVI HTLIGHHGHH NHWSPAPCSG TLMANQAQLQ WPTGLALSPL DGSLHFIDDR
LVLRLTSDMK IRVVAGTPLH CSNGGQDGRV NKTGADNVLG TVLAMAFSPF GNLYIADSDS
RRVNSIRVVD TAGNMRYFAG KQEGTGSQTC DCAIGGGSNG SATNSGVGGA GGSAYSTTVN
PTRPNGGTTP TTPSGGNGNG NGNGSSATSS GGSVGGSNGS GGGANGGACI CAGGIALSTG
TGSSSGSNGG GTLASIVGSG GLMSTGPTTT TTVLLGAKTT AAGIGAATLN DDGTLSNAET
LLSSNARFQA ISAIAVAQDG VINVADQGSL HVLALEHYLP SHDENGEFHI PFPPSSEIYV
FNRYGQHVAT KDLTSGKTRY SFLYSKNTSF GRLSTVTDAS GNKIQFLRDY SNVVSSIENT
QDHKSEIQIN GIGIMTKLSE KGRQEIELDY DSNTGLLNSR SSGGETYIYQ YDEFGRVTGM
ILPSGEIVRI TSQLADSQGL TVYVHASVES LFSRERIAGE ANELLVLGGV RSTFLKRGQA
HADAELKANN TLVIHGDNGV VVEASAVARH PLLEAALPVE AEMLAMWSHQ SVTMGEGLTN
SMYSVYSLVG DVRNPQQTLN REIWVNQSRV IGVEFDQFTN RETFYDARRT PILIVAYDQS
GLPKSYYPTN GYPVNITYDR FNRVEGWAWG PAELKYSYDR HGLLSEITSQ QDGIVSFVYN
DWNLVSEIGL ASQRKFVLQY DDAGGLRHVV LPSGTRHSFS MQTSIGFIRC TYTPPGSTRA
YLQHYSHAGA LLQTILPGDG ARIVYRYNAA GQLTEVVHGD GRSEFQYNEA TGMPSTVSHT
ERELEYRWDF EYAAGLLAEE RIDYVAKTGL SNAKFSYEYD SQLRVVALQG RIGGQSLPTQ
AFAYDPRTGR PSLIGQFRFS QPAQNQTQLH DGTASFTRTV DGRFQTQRMA LAIHRLEVFR
MEFSYGVHGR ISQTRTYTRN MAVNSYTNVK NYTWDCDGQL VGVEAQEPWG FRYDDNGNLL
SLTYRGNTIP MEYNAQDRIV KFGEGQYKYD ARGLVAQNAR EERFHYNTQG LLVRASKRGR
FDVRYYYDHL KRLTTRKDNF GNVTQFFYTN QQRPYEVSQI YSPRDGKLMS LTYDDVGHLI
YAQVYRHKYY VATDQSGTPL MLFNQYGEGI REIMRSPFGH IVYDSNPYLY LPIDFCGGIL
DQVTTLVHMG DGRVYDPLIG QWMSPDWQRV AERIITPTRL HLYRFNGNDP INVGHERHYP
EDFAAWMRTL GYNVGNLVPQ LARDLWQPPA LWGRPPANPV ALNLRRPFDN IPTMAVESGF
LAHLNVRRMS DFEQLSAPPR SALKCDVMDP SPKTIGSDTE PPFGKGIVVS RTADGQAIVS
SVPAANAIYR DVYTSVFNRS KLLPFTFVVH NAQQDSFFFV KEDAWRATED RQQLKRLQGQ
VNTTFHEITR EATVGSGPAG AANGGAGSSS SSSSSSGGGS SSNTGNYLDV KIHGAHAIIN
LRYGTTVAKE QQRLMHHAKL TAVRKAWHRE KEALRSGLTT ALEWSQQETD EILKQSYANN
YEGEYIHDVN LYPELAEDPY NIKFVKKKGA TGGAAGVPNS RRRRRRSTDL IQEEEEELHR
EADC
