TEN3_DANRE
ID TEN3_DANRE Reviewed; 2694 AA.
AC Q9W7R4; E7EYS1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-APR-2018, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Teneurin-3;
DE Short=Ten-3;
DE AltName: Full=Protein Odd Oz/ten-m homolog 3;
DE AltName: Full=Tenascin-M3;
DE Short=Ten-m3;
DE AltName: Full=Teneurin transmembrane protein 3;
GN Name=tenm3; Synonyms=odz3, tnm3;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=10495292; DOI=10.1016/s0925-4773(99)00155-0;
RA Mieda M., Kikuchi Y., Hirate Y., Aoki M., Okamoto H.;
RT "Compartmentalized expression of zebrafish ten-m3 and ten-m4, homologues of
RT the Drosophila tenm /odd Oz gene, in the central nervous system.";
RL Mech. Dev. 87:223-227(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24183672; DOI=10.1016/j.celrep.2013.09.045;
RA Antinucci P., Nikolaou N., Meyer M.P., Hindges R.;
RT "Teneurin-3 specifies morphological and functional connectivity of retinal
RT ganglion cells in the vertebrate visual system.";
RL Cell Rep. 5:582-592(2013).
RN [4]
RP FUNCTION.
RX PubMed=27374343; DOI=10.1016/j.cub.2016.05.035;
RA Antinucci P., Suleyman O., Monfries C., Hindges R.;
RT "Neural Mechanisms Generating Orientation Selectivity in the Retina.";
RL Curr. Biol. 26:1802-1815(2016).
CC -!- FUNCTION: Involved in neural development by regulating the
CC establishment of proper connectivity within the nervous system
CC (PubMed:24183672, PubMed:27374343). Acts in both pre- and postsynaptic
CC neurons in the hippocampus to control the assembly of a precise
CC topographic projection: required in both CA1 and subicular neurons for
CC the precise targeting of proximal CA1 axons to distal subiculum,
CC probably by promoting homophilic cell adhesion (By similarity).
CC Required by retinal ganglion cells for acquisition of their correct
CC morphological and functional connectivity, thereby playing a key role
CC in the development of the visual pathway (PubMed:24183672,
CC PubMed:27374343). {ECO:0000250|UniProtKB:Q9WTS6,
CC ECO:0000269|PubMed:24183672, ECO:0000269|PubMed:27374343}.
CC -!- SUBUNIT: Homodimer; disulfide-linked; to mediate homophilic cell
CC adhesion. {ECO:0000250|UniProtKB:Q9WTS6}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9WTS6};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:Q9WTS6}. Cell
CC projection, axon {ECO:0000250|UniProtKB:Q9WTS6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9W7R4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9W7R4-2; Sequence=VSP_059563;
CC -!- TISSUE SPECIFICITY: Expressed by retinal ganglion cells and their
CC presynaptic amacrine and postsynaptic tectal cell targets.
CC {ECO:0000269|PubMed:24183672}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the notochord and the somite around
CC tailbud stage. At 14 hours post-fertilization (hpf), expressed in the
CC somites, notochord, and the brain. Found in the rhombomere 3 (r3) and
CC r5. Expressed in the optic vesicles and a region covering the caudal
CC diencephalon and the mesencephalon with the strongest expression at its
CC most anterior part. Mesodermal expression is observed in both forming
CC and formed somites. In forming and newly formed somites, transcripts
CC are distributed evenly. In contrast, distribution in somites located on
CC more anterior trunk seems to be uneven, strongest in the ventral,
CC intermediate in the dorsal, and weakest in the medial parts. At 23 hpf,
CC there is no expression in the medial parts of somites. Expression in
CC somites fades away by 36 hpf. At 20 hpf, additional expression is
CC detected in the pharyngeal arches. {ECO:0000269|PubMed:10495292}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes
CC retinal ganglion cell dendrite stratification defects within the inner
CC plexiform layer, as well as mistargeting of dendritic processes into
CC outer portions of the retina. {ECO:0000269|PubMed:24183672}.
CC -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC {ECO:0000305}.
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DR EMBL; AB026979; BAA81892.1; -; mRNA.
DR EMBL; BX005481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX322797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX324137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX324208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_571043.1; NM_130968.1.
DR AlphaFoldDB; Q9W7R4; -.
DR SMR; Q9W7R4; -.
DR STRING; 7955.ENSDARP00000109423; -.
DR PaxDb; Q9W7R4; -.
DR Ensembl; ENSDART00000122700; ENSDARP00000109423; ENSDARG00000005479. [Q9W7R4-2]
DR Ensembl; ENSDART00000137676; ENSDARP00000113440; ENSDARG00000005479. [Q9W7R4-2]
DR GeneID; 30155; -.
DR CTD; 55714; -.
DR ZFIN; ZDB-GENE-990714-19; tenm3.
DR eggNOG; KOG4659; Eukaryota.
DR GeneTree; ENSGT01030000234566; -.
DR InParanoid; Q9W7R4; -.
DR OrthoDB; 7516at2759; -.
DR PhylomeDB; Q9W7R4; -.
DR PRO; PR:Q9W7R4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 1.
DR Bgee; ENSDARG00000005479; Expressed in superior colliculus and 58 other tissues.
DR ExpressionAtlas; Q9W7R4; baseline and differential.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0070983; P:dendrite guidance; IMP:ZFIN.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
DR GO; GO:0048666; P:neuron development; IBA:GO_Central.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:1903385; P:regulation of homophilic cell adhesion; ISS:UniProtKB.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:ZFIN.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0007601; P:visual perception; IMP:ZFIN.
DR Gene3D; 2.120.10.30; -; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR022385; Rhs_assc_core.
DR InterPro; IPR027691; Ten-3/4.
DR InterPro; IPR009471; Ten_N.
DR InterPro; IPR028916; Tox-GHH_dom.
DR InterPro; IPR006530; YD.
DR PANTHER; PTHR11219:SF65; PTHR11219:SF65; 1.
DR Pfam; PF06484; Ten_N; 2.
DR Pfam; PF15636; Tox-GHH; 1.
DR SMART; SM00181; EGF; 8.
DR SUPFAM; SSF49464; SSF49464; 1.
DR TIGRFAMs; TIGR03696; Rhs_assc_core; 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.
DR PROSITE; PS51361; TENEURIN_N; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell adhesion; Cell membrane; Cell projection;
KW Differentiation; Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..2694
FT /note="Teneurin-3"
FT /id="PRO_0000259507"
FT TOPO_DOM 1..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..2694
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 1..306
FT /note="Teneurin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00694"
FT DOMAIN 508..539
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 540..570
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 572..604
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 605..636
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 638..671
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 672..703
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 704..733
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 734..768
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1166..1192
FT /note="NHL 1"
FT REPEAT 1194..1238
FT /note="NHL 2"
FT REPEAT 1264..1308
FT /note="NHL 3"
FT REPEAT 1325..1365
FT /note="NHL 4"
FT REPEAT 1452..1495
FT /note="NHL 5"
FT REPEAT 1505..1524
FT /note="YD 1"
FT REPEAT 1541..1561
FT /note="YD 2"
FT REPEAT 1604..1623
FT /note="YD 3"
FT REPEAT 1624..1646
FT /note="YD 4"
FT REPEAT 1817..1836
FT /note="YD 5"
FT REPEAT 1858..1876
FT /note="YD 6"
FT REPEAT 1877..1897
FT /note="YD 7"
FT REPEAT 1904..1921
FT /note="YD 8"
FT REPEAT 1922..1943
FT /note="YD 9"
FT REPEAT 1944..1961
FT /note="YD 10"
FT REPEAT 1964..1984
FT /note="YD 11"
FT REPEAT 1987..2007
FT /note="YD 12"
FT REPEAT 2015..2034
FT /note="YD 13"
FT REPEAT 2040..2057
FT /note="YD 14"
FT REPEAT 2058..2084
FT /note="YD 15"
FT REPEAT 2086..2099
FT /note="YD 16"
FT REPEAT 2100..2123
FT /note="YD 17"
FT REPEAT 2126..2146
FT /note="YD 18"
FT REPEAT 2147..2167
FT /note="YD 19"
FT REPEAT 2169..2189
FT /note="YD 20"
FT REPEAT 2201..2221
FT /note="YD 21"
FT REPEAT 2223..2243
FT /note="YD 22"
FT REPEAT 2269..2310
FT /note="YD 23"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 664
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 854
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 877
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1048
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1634
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1671
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1729
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1814
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1915
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 512..522
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 516..527
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 529..538
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 547..558
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 560..569
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 576..587
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 581..592
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 594..603
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 608..619
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 613..624
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 626..635
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 646..659
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 661..670
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 675..685
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 679..690
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 692..701
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 706..716
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 710..721
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 723..732
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 737..747
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 741..756
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 758..767
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 1..104
FT /note="Missing (in isoform 2)"
FT /id="VSP_059563"
FT CONFLICT 781
FT /note="N -> S (in Ref. 1; BAA81892)"
FT /evidence="ECO:0000305"
FT CONFLICT 813
FT /note="I -> F (in Ref. 1; BAA81892)"
FT /evidence="ECO:0000305"
FT CONFLICT 892
FT /note="R -> Q (in Ref. 1; BAA81892)"
FT /evidence="ECO:0000305"
FT CONFLICT 1210
FT /note="R -> G (in Ref. 1; BAA81892)"
FT /evidence="ECO:0000305"
FT CONFLICT 1880..1884
FT /note="QDRLS -> HGKQI (in Ref. 1; BAA81892)"
FT /evidence="ECO:0000305"
FT CONFLICT 2520
FT /note="A -> V (in Ref. 1; BAA81892)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2694 AA; 300669 MW; 65C41528CC4B4A10 CRC64;
MDVKERRPYC SLTKSRREKE RRYTGSSGDS EDCRVPTQKS YSSSETLKAF DHDSSRLLYG
GHVKEMVHRE ADEYSRQGQN FNLRQLGICE PATRRGLAFC AEMGMPSSLS SPSVTEHSHS
QPPSPNLHDN QSSILSNATT QAVQDSDSEE EYTAVLYRPV TQPAPSHSCN EQPSNQHQQG
QSTLPPVPPP HKQQPSVTAL NHNSLSSRRN VSPAPPAALP AELQTTPESV PLQDSWVLGS
NVPLESRHFL FKTGTGTTPL FSTATPGYTM ATGAVYSPPT RPLPRNTLSR SAFKFKKSSK
YCSWRCTALS AMAVSILLSV LLCYCIAMHL FGLNWQLQET EGYAFENGQV KSDSTATNAV
TALSTENKVY FQENNTIDTG EVDVGRRAVQ DVPPGTFWRT QLFIDQPQSL KFNISVQRGA
LVGVYGRKGL PPTHTQYDFV ELLDGSRLIA KEKRGLVEVE GAARKARSVN VHEAEFIRFL
DSGTWHLAFY NDGKNAEQVS YNTIIIDTLT ECPHNCHGNG DCRTGTCHCF PGFLGPDCSR
AACPVLCSGN GQYSRGRCLC YSGWKGTECD VPSNQCIDIH CSGHGICIMG TCACNTGYKG
DNCEEVDCLD PSCSSHGVCI HGECHCNPGW GGNNCEILKT MCPDQCSGHG TYQTESGTCT
CDTNWTGPDC SIEVCAVDCG SHGVCIGGSC RCEEGWTGSV CDLKACHPRC TEHGTCKDGK
CECHQGWTGE HCTVEGCPGL CNSNGRCTLD QNGWHCVCQP GWRGAGCDVA METLCADGKD
NEGDGLVDCM DPDCCLQSSC QTQPFCRGSP DPIDIISQNQ PASPQQAAQS FYQQISFLTG
PESTHVINGE NPFNRSLVSI IRGQVLTADG TPLIGVNVSF VHYPDHGYTI TRQDGMFDIL
ANGGASLTLS FERAPFLTQF RTVWIPWNVF YVMDTLVMKK EENDIPSCDL SGFIRPSPLI
VATPLSTFFR SSPENGPIIP ETQVLQEETA IPGSDLNLMY LSSRAAGYRP VLKVTMTQAT
IPFNLMKVHL MVAVVGRLFQ KWFPAEPNLS YTFIWDKTDA YNQRVYGLSE AVVSVGFEYE
SCLDLILWEK RTAILQGYEL DASNMGGWTL DKHHVLDVQN GILYKGNGEN VFVSQQPPVI
STIMGNGRRR SISCPSCNGQ ADGNKLLAPV ALACGSDGSL FVGDFNYIRR IFPSGNVTSV
MELSNNPAHR YYLATDPMTG QLYVSDTNSR RIFRPKALTG TKELLQNAEV VAGTGEQCLP
FDEARCGDGG KATEALLLGP KGIAVDKNGF IYFVDGTMIR KVDRNGIIST LLGSNDLTSA
RPLTCDNSMH IGQVRLEWPT DLAINPMDNS IYVLDNNVVL QITENRQVRI VAGRPMHCQV
PGIEYTMGKR AIQTTLEGAT AISLSYSGVL YIAETDEKKI NRIRQVSTDG EISHLAGAPS
DCDCKNDANC DCYQTGDGYA KDARLNAPSS LVVSPDGTLY VADLGNIRIR AIRHNRPPQG
SSGLFEVASP ASQELYVFDS NGTHQYTMSL VTGDYKYNFS YSNEDDVTAV TDSSGNTLRV
RRDPNRMPVR IVAPDNQVIW LTIGTNGGLK TLTAQGQELV LFTYHGNSGL LATKSIQIGW
TTFYDYDSEG RLTNVTFPTG VITSLIGEMD RALTVDIETS GRDDDVSITT NLSSIDSFYT
LVQDQLRNSY QVGYDNSMRV IYANGMDSHF QTEPHILAGA SNPTVARRNM TLPGENGQNL
VEWRFRKEQN RGKVVVFGRK LRVNGRNLLS VDYDRSLRTE KIYDDHRKFL LKIVYDASGH
PTLWVPSSKL MSVNLTYSST GQVTSLQRGP TTERVEYDSQ GRIVSRTFAD AKIWSYTYLD
KSMVLLLHSQ RQYIFDYDLQ DRLSAITMPS VARHTMQTIR SVGYYRNIYN PPESNASVTV
DYSEDGQLLR VAHLGTGRRV LYKYRRQNKL SEILYDSTRV SFTYDETAGV LKTVNLQSEG
FICSIRYRQI GPLVDRQIFR FSEDGMVNAR FDYTYDNSFR VTSMQGVINE TPLPIDLYQF
DDISGKVEQF GKFGVIYYDI NQIISTAVMT YTKHFDVHGR IKEIQYEIFR SLMYWITIQY
DNMGRVTKRE IKIGPFANTT KYGYEYDVDG QLQTVYLNEK MMWRYNYDLN GNLHLLNPGN
SARLTPLRYD LRDRITRLGD VQYRMDEDGF LRQRGAEIFE YNSKGLLVRV HSKASGWTIQ
YRYDGLGRRL ASRNSLGQHL QFFYADLNYP TRITHVYNHS SSEITSLYYD LQGHLFAMEI
SSGEEFYIAC DNTGTPLAVF SSNGLLLKQV QYTAYGEIYF DSNPDFQLVI GFHGGLYDPL
TRLLHFGERD YDIQAGRWTT PDISTWTRVG KDPAPFNLYM FRNNNPISKI HEVKEYVTDV
NIWLVTFGFH LHNVIPGFPI PKFDLTQPSL EMRKSQLWDD LPSISGVQQE VMRQAKAFLS
FERMPEIQLS RRRSSREKPW LWFATVKSLI GKGVMLAITS KGQVATNALN IANEDCIKVA
TVLNNAFYLE DLHFTVEGRD THYFIKTSLP ESDLGALRLT SGRKSLENGV NVTVSQSTTV
VNGRTRRFAD VELQYGALAL HVRYGMTLDE EKARVLEQAR QRALSSAWAR EQQRVRDGEE
GVRLWTEGEK RQLLSSGKVL GYDGYYVLSV EQYPELADSA NNVQFLRQSE IGKR
