TENM_DROME
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 03-AUG-2022, entry version 152.
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};
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; 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 SMR; O61307; -.
DR BioGRID; 65699; 12.
DR IntAct; O61307; 704.
DR GlyGen; O61307; 1 site.
DR iPTMnet; O61307; -.
DR PaxDb; O61307; -.
DR PeptideAtlas; O61307; -.
DR PRIDE; 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 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 tissues.
DR ExpressionAtlas; O61307; baseline and differential.
DR Genevisible; O61307; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; ISS:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA: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; HDA: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; 2.120.10.30; -; 1.
DR Gene3D; 2.130.10.10; -; 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 Pfam; PF05593; RHS_repeat; 1.
DR Pfam; PF15636; Tox-GHH; 1.
DR SMART; SM00181; EGF; 8.
DR SUPFAM; SSF49464; SSF49464; 1.
DR TIGRFAMs; TIGR01643; YD_repeat_2x; 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 Alternative splicing; Cell adhesion; Cell membrane; Cytoplasm;
KW Developmental protein; Disulfide bond; EGF-like domain; Glycoprotein;
KW Membrane; Neurogenesis; Postsynaptic cell membrane; Reference proteome;
KW Repeat; Synapse; Synaptosome; Transmembrane; 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"
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
