ID TENM_DROME Reviewed; 2731 AA.
AC O61307; A8JNW8; O18366; Q24551; Q9TX59; Q9VNU6;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 2.
DT 27-MAR-2024, entry version 160.
DE RecName: Full=Teneurin-m;
DE Short=Tenm;
DE AltName: Full=Odd Oz protein;
DE AltName: Full=Tenascin-like protein;
GN Name=Ten-m; Synonyms=odz; ORFNames=CG5723;
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] (ISOFORM B), AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S;
RX PubMed=8070401; DOI=10.1002/j.1460-2075.1994.tb06682.x;
RA Baumgartner S., Martin D., Hagios C., Chiquet-Ehrismann R.;
RT "Tenm, a Drosophila gene related to tenascin, is a new pair-rule gene.";
RL EMBO J. 13:3728-3740(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM B), AND DEVELOPMENTAL
RP STAGE.
RX PubMed=9373139; DOI=10.1016/s0378-1119(97)00375-2;
RA Levine A., Gartenberg D., Yakov R., Lieberman Y., Budai-Hadrian O.,
RA Bashan-Ahrend A., Wides R.;
RT "The genetics and molecular structure of the Drosophila pair-rule gene odd
RT Oz (odz).";
RL Gene 200:59-74(1997).
RN [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 [4]
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 [5]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PROTEOLYTIC PROCESSING, AND
RP PHOSPHORYLATION.
RX PubMed=7514504; DOI=10.1016/0092-8674(94)90220-8;
RA Levine A., Bashan-Ahrend A., Budai-Hadrian O., Gartenberg D.,
RA Menasherow S., Wides R.;
RT "Odd Oz: a novel Drosophila pair rule gene.";
RL Cell 77:587-598(1994).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-857, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
RN [7]
RP FUNCTION, INTERACTION WITH CHER, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=21857973; DOI=10.1371/journal.pone.0022956;
RA Zheng L., Michelson Y., Freger V., Avraham Z., Venken K.J., Bellen H.J.,
RA Justice M.J., Wides R.;
RT "Drosophila Ten-m and filamin affect motor neuron growth cone guidance.";
RL PLoS ONE 6:E22956-E22956(2011).
RN [8]
RP FUNCTION IN SYNAPSE FORMATION, HOMODIMERIZATION, HETERODIMERIZATION,
RP INTERACTION WITH TEN-A, 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 [9]
RP FUNCTION IN NEUROMUSCULAR SYNAPSE FORMATION, INTERACTION WITH ALPHA-SPEC
RP AND TEN-A, TISSUE SPECIFICITY, AND 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-a
CC to organize neuromuscular synapses. Functions in olfactory synaptic
CC partner matching by promoting homophilic cell adhesion between pre-
CC synaptic olfactory receptor neurons (ORN) axons and post-synaptic
CC projection neurons (PN) dendrites partner in the developing antennal
CC lobe to form stable connections. Also required for peripheral axon
CC growth cone guidance and target recognition of motor neurons.
CC {ECO:0000269|PubMed:21857973, ECO:0000269|PubMed:22425994,
CC ECO:0000269|PubMed:22426000, ECO:0000269|PubMed:7514504}.
CC -!- SUBUNIT: Homodimer. Heterodimer with Ten-a. Interacts with Ten-a; the
CC interaction occurs at the neuromuscular junction. Interacts with alpha-
CC Spec and cher. {ECO:0000269|PubMed:21857973,
CC ECO:0000269|PubMed:22425994, ECO:0000269|PubMed:22426000}.
CC -!- INTERACTION:
CC O61307; Q9VEN1: cher; NbExp=4; IntAct=EBI-118556, EBI-133626;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Postsynaptic cell membrane. Synapse,
CC synaptosome. Membrane {ECO:0000305}; Single-pass membrane protein
CC {ECO:0000305}. Note=Localizes at neuromuscular junction. Localizes in
CC neuron cell bodies. Colocalizes with alpha-Spec at the membranous
CC subsynaptic reticulum (SSR).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B;
CC IsoId=O61307-1; Sequence=Displayed;
CC Name=D;
CC IsoId=O61307-2; Sequence=VSP_054459, VSP_054460;
CC -!- TISSUE SPECIFICITY: Expressed in muscles and motor neurons (at protein
CC level). {ECO:0000269|PubMed:22426000}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the central nervous system and heart.
CC Expressed in the developing antennal lobe. Expressed in subset of
CC matching olfactory receptor neurons (ORN) and projection neurons (PN)
CC in select glomeruli between 12 to 48 hours after puparium formation
CC (apf) (at protein level). Expressed in odd-numbered blastoderm
CC parasegments, the central nervous system, muscle attachment points and
CC tracheal precursor cells. Expressed in the ventral nerve cord, the
CC cardiac mesoderm and epidermis at late embryonic stages. Expressed in
CC all imaginal disks. {ECO:0000269|PubMed:21857973,
CC ECO:0000269|PubMed:22425994, ECO:0000269|PubMed:8070401,
CC ECO:0000269|PubMed:9373139}.
CC -!- PTM: Phosphorylated. Phosphorylation occurs at tyrosine residues.
CC {ECO:0000269|PubMed:7514504}.
CC -!- PTM: Proteolytically cleaved. {ECO:0000269|PubMed:7514504}.
CC -!- DISRUPTION PHENOTYPE: Shows peripheral motor neuron axon guidance
CC defects. {ECO:0000269|PubMed:21857973}.
CC -!- MISCELLANEOUS: The name odz (odd Oz) reflects the odd pair rule nature
CC of the gene and Oz reflects the prominent expression of the gene in the
CC brain, heart and neurons, corresponding to the three gifts that the
CC Wizard of Oz bestowed.
CC -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA51678.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X73154; CAA51678.1; ALT_INIT; mRNA.
DR EMBL; AF008227; AAC05080.1; -; Genomic_DNA.
DR EMBL; AF008224; AAC05080.1; JOINED; Genomic_DNA.
DR EMBL; AF008226; AAC05080.1; JOINED; Genomic_DNA.
DR EMBL; AF008228; AAB88281.1; -; mRNA.
DR EMBL; AE014296; AAF51824.2; -; Genomic_DNA.
DR EMBL; AE014296; ABW08579.2; -; Genomic_DNA.
DR RefSeq; NP_001097661.2; NM_001104191.3. [O61307-2]
DR RefSeq; NP_524215.2; NM_079491.3. [O61307-1]
DR PDB; 8FIA; X-ray; 2.40 A; A=779-2731.
DR PDBsum; 8FIA; -.
DR SMR; O61307; -.
DR BioGRID; 65699; 12.
DR IntAct; O61307; 704.
DR STRING; 7227.FBpp0303192; -.
DR GlyCosmos; O61307; 1 site, No reported glycans.
DR GlyGen; O61307; 1 site.
DR iPTMnet; O61307; -.
DR PeptideAtlas; O61307; -.
DR EnsemblMetazoa; FBtr0078509; FBpp0078161; FBgn0004449. [O61307-1]
DR EnsemblMetazoa; FBtr0306107; FBpp0297244; FBgn0004449. [O61307-2]
DR GeneID; 40464; -.
DR KEGG; dme:Dmel_CG5723; -.
DR UCSC; CG5723-RB; d. melanogaster.
DR UCSC; CG5723-RC; d. melanogaster.
DR AGR; FB:FBgn0004449; -.
DR CTD; 40464; -.
DR FlyBase; FBgn0004449; Ten-m.
DR VEuPathDB; VectorBase:FBgn0004449; -.
DR eggNOG; KOG1225; Eukaryota.
DR eggNOG; KOG4659; Eukaryota.
DR GeneTree; ENSGT01030000234566; -.
DR HOGENOM; CLU_000229_1_0_1; -.
DR InParanoid; O61307; -.
DR OMA; HWTQSAP; -.
DR SignaLink; O61307; -.
DR BioGRID-ORCS; 40464; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Ten-m; fly.
DR GenomeRNAi; 40464; -.
DR PRO; PR:O61307; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0004449; Expressed in embryonic/larval hemocyte (Drosophila) and 26 other cell types or tissues.
DR ExpressionAtlas; O61307; baseline and differential.
DR Genevisible; O61307; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; ISS:FlyBase.
DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR GO; GO:0031005; F:filamin binding; IDA:FlyBase.
DR GO; GO:0042802; F:identical protein binding; IDA:FlyBase.
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:0022416; P:chaeta development; IMP:FlyBase.
DR GO; GO:0048058; P:compound eye corneal lens development; IMP: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:0031122; P:cytoplasmic microtubule organization; IMP:UniProtKB.
DR GO; GO:0099559; P:maintenance of alignment of postsynaptic density and presynaptic active zone; IDA:SynGO.
DR GO; GO:0048790; P:maintenance of presynaptic active zone structure; IMP:UniProtKB.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
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:0099190; P:postsynaptic spectrin-associated cytoskeleton organization; IDA:SynGO.
DR GO; GO:0097090; P:presynaptic membrane organization; IMP:UniProtKB.
DR GO; GO:0045467; P:R7 cell development; IMP:FlyBase.
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 Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 6.
DR Gene3D; 2.180.10.10; RHS repeat-associated core; 2.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR031325; RHS_repeat.
DR InterPro; IPR028916; Tox-GHH_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR006530; YD.
DR NCBIfam; TIGR01643; YD_repeat_2x; 1.
DR PANTHER; PTHR11219; TENEURIN AND N-ACETYLGLUCOSAMINE-1-PHOSPHODIESTER ALPHA-N-ACETYLGLUCOSAMINIDASE; 1.
DR PANTHER; PTHR11219:SF69; TENEURIN-M; 1.
DR Pfam; PF05593; RHS_repeat; 1.
DR Pfam; PF15636; Tox-GHH; 1.
DR SMART; SM00181; EGF; 8.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR PROSITE; PS00022; EGF_1; 8.
DR PROSITE; PS01186; EGF_2; 6.
DR PROSITE; PS50026; EGF_3; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Cytoplasm; Developmental protein; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Neurogenesis; Postsynaptic cell membrane;
KW Reference proteome; Repeat; Synapse; Synaptosome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..2731
FT /note="Teneurin-m"
FT /id="PRO_0000421021"
FT TOPO_DOM 1..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..2731
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 536..572
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 574..606
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 643..676
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 738..774
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1160..1201
FT /note="NHL 1"
FT REPEAT 1202..1246
FT /note="NHL 2"
FT REPEAT 1391..1434
FT /note="NHL 3"
FT REPEAT 1459..1502
FT /note="NHL 4"
FT REPEAT 1618..1652
FT /note="YD"
FT /evidence="ECO:0000255"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2691..2731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2717..2731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 857
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT DISULFID 540..549
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 545..560
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 562..571
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 578..589
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 583..594
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 596..605
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 651..664
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 666..675
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 742..752
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 746..762
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 764..773
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 375
FT /note="G -> GGRAMSTRLSVRGAGERGRRHRRSLNEEQGEDDVATDGTFSDLITNE
FT SLNQQAAEKYLATTLAKSPTDVHGSGNKTLPRMDGVYGTQRSEDTPDTSYDYVYEDEVE
FT PETTPSLIRRTKTGQQFGKSLNSNLRSAAKTLVNKRRKYDHGTVEAEHIKHEEEEEEDE
FT QKLERHEAIGMATELTTESETSTLPAVIDDDNQSDNSSSGPTPETTVRSDTDDIVEINT
FT PPSQTAQRTFAAVSHQPAIEHDFQIKGTDAGGLQTEKPATDDINNERDLADNYEVDSKE
FT PTSPGTPPQGKVSQQTGKASLQSLQSESDLMMNDASHYEDIDIVKLDGLTISHEEEIYK
FT TADKENMAPKNQPSQHIDRSQNEVLKGHQQGDEKQPQLEPLKPYVSERVDLPGKRIFLN
FT LTIATDEGSDSVYTLHVEVPTGGGPHFIKEVLTHEKPTAQADSCVPEPPPRMPDCPCSC
FT LPPPAPIYLDDTVDIDSAPPAKTVTTSTISAPINPFHSEEEDDEDGVRDEEQTPSSSTA
FT TNLPSTEIDNHIAAFTEPAVGAGGVPFACPDVMPVLILE (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_054459"
FT VAR_SEQ 858
FT /note="E -> ESIFWNYFNA (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_054460"
FT CONFLICT 22
FT /note="A -> G (in Ref. 2; AAB88281/AAC05080)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="G -> S (in Ref. 2; AAB88281/AAC05080)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="A -> V (in Ref. 2; AAB88281)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="A -> V (in Ref. 2; AAB88281)"
FT /evidence="ECO:0000305"
FT CONFLICT 1837
FT /note="D -> Y (in Ref. 1; CAA51678)"
FT /evidence="ECO:0000305"
FT CONFLICT 2099
FT /note="A -> G (in Ref. 2; AAB88281/AAC05080)"
FT /evidence="ECO:0000305"
FT CONFLICT 2315
FT /note="A -> T (in Ref. 2; AAB88281)"
FT /evidence="ECO:0000305"
FT CONFLICT 2495
FT /note="M -> T (in Ref. 1; CAA51678)"
FT /evidence="ECO:0000305"
FT CONFLICT 2710
FT /note="K -> R (in Ref. 2; AAB88281/AAC05080)"
FT /evidence="ECO:0000305"
FT HELIX 834..838
FT /evidence="ECO:0007829|PDB:8FIA"
FT HELIX 839..842
FT /evidence="ECO:0007829|PDB:8FIA"
FT HELIX 848..851
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 858..860
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 861..869
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 880..883
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 890..892
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 897..904
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 906..914
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 921..926
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 932..934
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 961..963
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 967..970
FT /evidence="ECO:0007829|PDB:8FIA"
FT HELIX 971..974
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 985..987
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 988..991
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 992..998
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1005..1009
FT /evidence="ECO:0007829|PDB:8FIA"
FT HELIX 1010..1012
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1018..1023
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1033..1042
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1045..1053
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1058..1063
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1077..1089
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1094..1102
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1112..1114
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1121..1124
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 1125..1128
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1129..1132
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1137..1139
FT /evidence="ECO:0007829|PDB:8FIA"
FT HELIX 1140..1142
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1146..1151
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1154..1156
FT /evidence="ECO:0007829|PDB:8FIA"
FT HELIX 1168..1170
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1176..1181
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1187..1191
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1194..1198
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1202..1209
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1220..1223
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 1225..1227
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1230..1234
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 1235..1238
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1239..1242
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 1252..1254
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1257..1260
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 1272..1277
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1278..1282
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1286..1293
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1299..1303
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1306..1310
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1315..1320
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1334..1338
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 1340..1342
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1351..1353
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 1355..1357
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1360..1364
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1367..1372
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 1373..1375
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1376..1381
FT /evidence="ECO:0007829|PDB:8FIA"
FT HELIX 1399..1401
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1405..1412
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1418..1423
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1425..1427
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1429..1434
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1438..1444
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 1467..1469
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1473..1480
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1486..1490
FT /evidence="ECO:0007829|PDB:8FIA"
FT HELIX 1491..1493
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1495..1500
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1512..1516
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 1517..1520
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1521..1525
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1529..1536
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 1537..1539
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1542..1552
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1557..1561
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1563..1565
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1567..1572
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1578..1582
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1588..1593
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1599..1603
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1609..1615
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1621..1626
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1631..1636
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1642..1646
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1652..1660
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1663..1670
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1673..1681
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1684..1689
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1692..1698
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1704..1707
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1711..1719
FT /evidence="ECO:0007829|PDB:8FIA"
FT HELIX 1722..1725
FT /evidence="ECO:0007829|PDB:8FIA"
FT HELIX 1729..1734
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1737..1745
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1748..1761
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1778..1787
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1790..1798
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 1799..1802
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1803..1808
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 1809..1811
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1812..1819
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1825..1830
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1832..1834
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1838..1842
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1848..1853
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1856..1862
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1868..1873
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1878..1882
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1892..1895
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1901..1906
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1912..1916
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1922..1929
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1931..1939
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 1941..1943
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1947..1951
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1956..1961
FT /evidence="ECO:0007829|PDB:8FIA"
FT HELIX 1963..1965
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1968..1973
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1979..1984
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 1987..1993
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 1995..1997
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2000..2007
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2010..2019
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2022..2030
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2039..2045
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2051..2058
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2066..2070
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 2072..2074
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2077..2080
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2083..2088
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 2089..2091
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2092..2097
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2102..2108
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2114..2121
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2124..2133
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2139..2146
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2149..2157
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2163..2176
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2182..2187
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2190..2196
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2202..2205
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2211..2213
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2219..2222
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2225..2229
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2235..2240
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 2241..2243
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2244..2250
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2256..2261
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2266..2270
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2274..2276
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2282..2285
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 2286..2289
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2290..2296
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2302..2307
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2310..2316
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2322..2326
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2332..2338
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2344..2348
FT /evidence="ECO:0007829|PDB:8FIA"
FT HELIX 2358..2360
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 2365..2367
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2370..2372
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2375..2378
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 2379..2382
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2383..2386
FT /evidence="ECO:0007829|PDB:8FIA"
FT HELIX 2391..2394
FT /evidence="ECO:0007829|PDB:8FIA"
FT HELIX 2399..2402
FT /evidence="ECO:0007829|PDB:8FIA"
FT HELIX 2408..2410
FT /evidence="ECO:0007829|PDB:8FIA"
FT HELIX 2425..2431
FT /evidence="ECO:0007829|PDB:8FIA"
FT HELIX 2436..2438
FT /evidence="ECO:0007829|PDB:8FIA"
FT HELIX 2441..2447
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2455..2457
FT /evidence="ECO:0007829|PDB:8FIA"
FT HELIX 2470..2483
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2515..2522
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2525..2530
FT /evidence="ECO:0007829|PDB:8FIA"
FT HELIX 2538..2546
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2555..2558
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2561..2568
FT /evidence="ECO:0007829|PDB:8FIA"
FT HELIX 2573..2581
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2589..2592
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2606..2609
FT /evidence="ECO:0007829|PDB:8FIA"
FT STRAND 2611..2621
FT /evidence="ECO:0007829|PDB:8FIA"
FT HELIX 2623..2634
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 2685..2687
FT /evidence="ECO:0007829|PDB:8FIA"
FT TURN 2689..2693
FT /evidence="ECO:0007829|PDB:8FIA"
SQ SEQUENCE 2731 AA; 304056 MW; 6718B77B8F62D482 CRC64;
MNPYEYESTL DCRDVGGGPT PAHAHPHAQG RTLPMSGHGR PTTDLGPVHG SQTLQHQNQQ
NLQAAQAAAQ SSHYDYEYQH LAHRPPDTAN NTAQRTHGRQ GFLLEGVTPT APPDVPPRNP
TMSRMQNGRL TVNNPNDADF EPSCLVRTPS GNVYIPSGNL NINKGSPIDF KSGSACSTPT
KDTLKGYERS TQGCMGPVLP QRSVMNGLPA HHYSAPMNFR KDLVARCSSP WFGIGSISVL
FAFVVMLILL TTTGVIKWNQ SPPCSVLVGN EASEVTAAKS TNTDLSKLHN SSVRAKNGQG
IGLAQGQSGL GAAGVGSGGG SSAATVTTAT SNSGTAQGLQ STSASAEATS SAATSSSQSS
LTPSLSSSLA NANNGGARTF PARSFPPDGT TFGQITLGQK LTKEIQPYSY WNMQFYQSEP
AYVKFDYTIP RGASIGVYGR RNALPTHTQY HFKEVLSGFS ASTRTARAAH LSITREVTRY
MEPGHWFVSL YNDDGDVQEL TFYAAVAEDM TQNCPNGCSG NGQCLLGHCQ CNPGFGGDDC
SESVCPVLCS QHGEYTNGEC ICNPGWKGKE CSLRHDECEV ADCSGHGHCV SGKCQCMRGY
KGKFCEEVDC PHPNCSGHGF CADGTCICKK GWKGPDCATM DQDALQCLPD CSGHGTFDLD
TQTCTCEAKW SGDDCSKELC DLDCGQHGRC EGDACACDPE WGGEYCNTRL CDVRCNEHGQ
CKNGTCLCVT GWNGKHCTIE GCPNSCAGHG QCRVSGEGQW ECRCYEGWDG PDCGIALELN
CGDSKDNDKD GLVDCEDPEC CASHVCKTSQ LCVSAPKPID VLLRKQPPAI TASFFERMKF
LIDESSLQNY AKLETFNESR SAVIRGRVVT SLGMGLVGVR VSTTTLLEGF TLTRDDGWFD
LMVNGGGAVT LQFGRAPFRP QSRIVQVPWN EVVIIDLVVM SMSEEKGLAV TTTHTCFAHD
YDLMKPVVLA SWKHGFQGAC PDRSAILAES QVIQESLQIP GTGLNLVYHS SRAAGYLSTI
KLQLTPDVIP TSLHLIHLRI TIEGILFERI FEADPGIKFT YAWNRLNIYR QRVYGVTTAV
VKVGYQYTDC TDIVWDIQTT KLSGHDMSIS EVGGWNLDIH HRYNFHEGIL QKGDGSNIYL
RNKPRIILTT MGDGHQRPLE CPDCDGQATK QRLLAPVALA AAPDGSLFVG DFNYIRRIMT
DGSIRTVVKL NATRVSYRYH MALSPLDGTL YVSDPESHQI IRVRDTNDYS QPELNWEAVV
GSGERCLPGD EAHCGDGALA KDAKLAYPKG IAISSDNILY FADGTNIRMV DRDGIVSTLI
GNHMHKSHWK PIPCEGTLKL EEMHLRWPTE LAVSPMDNTL HIIDDHMILR MTPDGRVRVI
SGRPLHCATA STAYDTDLAT HATLVMPQSI AFGPLGELYV AESDSQRINR VRVIGTDGRI
APFAGAESKC NCLERGCDCF EAEHYLATSA KFNTIAALAV TPDSHVHIAD QANYRIRSVM
SSIPEASPSR EYEIYAPDMQ EIYIFNRFGQ HVSTRNILTG ETTYVFTYNV NTSNGKLSTV
TDAAGNKVFL LRDYTSQVNS IENTKGQKCR LRMTRMKMLH ELSTPDNYNV TYEYHGPTGL
LRTKLDSTGR SYVYNYDEFG RLTSAVTPTG RVIELSFDLS VKGAQVKVSE NAQKEMSLLI
QGATVIVRNG AAESRTTVDM DGSTTSITPW GHNLQMEVAP YTILAEQSPL LGESYPVPAK
QRTEIAGDLA NRFEWRYFVR RQQPLQAGKQ SKGPPRPVTE VGRKLRVNGD NVLTLEYDRE
TQSVVVMVDD KQELLNVTYD RTSRPISFRP QSGDYADVDL EYDRFGRLVS WKWGVLQEAY
SFDRNGRLNE IKYGDGSTMV YAFKDMFGSL PLKVTTPRRS DYLLQYDDAG ALQSLTTPRG
HIHAFSLQTS LGFFKYQYYS PINRHPFEIL YNDEGQILAK IHPHQSGKVA FVHDTAGRLE
TILAGLSSTH YTYQDTTSLV KSVEVQEPGF ELRREFKYHA GILKDEKLRF GSKNSLASAR
YKYAYDGNAR LSGIEMAIDD KELPTTRYKY SQNLGQLEVV QDLKITRNAF NRTVIQDSAK
QFFAIVDYDQ HGRVKSVLMN VKNIDVFRLE LDYDLRNRIK SQKTTFGRST AFDKINYNAD
GHVVEVLGTN NWKYLFDENG NTVGVVDQGE KFNLGYDIGD RVIKVGDVEF NNYDARGFVV
KRGEQKYRYN NRGQLIHSFE RERFQSWYYY DDRSRLVAWH DNKGNTTQYY YANPRTPHLV
THVHFPKISR TMKLFYDDRD MLIALEHEDQ RYYVATDQNG SPLAFFDQNG SIVKEMKRTP
FGRIIKDTKP EFFVPIDFHG GLIDPHTKLV YTEQRQYDPH VGQWMTPLWE TLATEMSHPT
DVFIYRYHNN DPINPNKPQN YMIDLDSWLQ LFGYDLNNMQ SSRYTKLAQY TPQASIKSNT
LAPDFGVISG LECIVEKTSE KFSDFDFVPK PLLKMEPKMR NLLPRVSYRR GVFGEGVLLS
RIGGRALVSV VDGSNSVVQD VVSSVFNNSY FLDLHFSIHD QDVFYFVKDN VLKLRDDNEE
LRRLGGMFNI STHEISDHGG SAAKELRLHG PDAVVIIKYG VDPEQERHRI LKHAHKRAVE
RAWELEKQLV AAGFQGRGDW TEEEKEELVQ HGDVDGWNGI DIHSIHKYPQ LADDPGNVAF
QRDAKRKRRK TGSSHRSASN RRQLKFGELS A
//
