GenomeNet

Database: UniProt
Entry: Q9W7R4
LinkDB: Q9W7R4
Original site: Q9W7R4 
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   10-APR-2019, entry version 116.
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   Cyprinidae; 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,
RT   homologues of the Drosophila tenm /odd Oz gene, in the central nervous
RT   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.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   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., Eliott D., Threadgold G.,
RA   Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
RA   Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
RA   Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
RA   Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
RA   Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
RA   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.,
RA   Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
RA   Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
RA   Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
RA   Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
RA   Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
RA   Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
RA   Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human 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
RT   retinal 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
CC       postsynaptic neurons in the hippocampus to control the assembly of
CC       a precise topographic projection: required in both CA1 and
CC       subicular neurons for the precise targeting of proximal CA1 axons
CC       to distal subiculum, probably by promoting homophilic cell
CC       adhesion (By similarity). Required by retinal ganglion cells for
CC       acquisition of their correct morphological and functional
CC       connectivity, thereby playing a key role in the development of the
CC       visual pathway (PubMed:24183672, PubMed:27374343).
CC       {ECO:0000250|UniProtKB:Q9WTS6, ECO:0000269|PubMed:24183672,
CC       ECO:0000269|PubMed:27374343}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked; to mediate homophilic cell
CC       adhesion. {ECO:0000250|UniProtKB:Q9WTS6}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:Q9WTS6}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9WTS6}. Cell projection, axon
CC       {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
CC       around tailbud stage. At 14 hours post-fertilization (hpf),
CC       expressed in the somites, notochord, and the brain. Found in the
CC       rhombomere 3 (r3) and r5. Expressed in the optic vesicles and a
CC       region covering the caudal diencephalon and the mesencephalon with
CC       the strongest expression at its most anterior part. Mesodermal
CC       expression is observed in both forming and formed somites. In
CC       forming and newly formed somites, transcripts are distributed
CC       evenly. In contrast, distribution in somites located on more
CC       anterior trunk seems to be uneven, strongest in the ventral,
CC       intermediate in the dorsal, and weakest in the medial parts. At 23
CC       hpf, there is no expression in the medial parts of somites.
CC       Expression in somites fades away by 36 hpf. At 20 hpf, additional
CC       expression is detected in the pharyngeal arches.
CC       {ECO:0000269|PubMed:10495292}.
CC   -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes
CC       retinal ganglion cell dendrite stratification defects within the
CC       inner plexiform layer, as well as mistargeting of dendritic
CC       processes into outer portions of the retina.
CC       {ECO:0000269|PubMed:24183672}.
CC   -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC       {ECO:0000305}.
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   UniGene; Dr.113659; -.
DR   UniGene; Dr.77510; -.
DR   ProteinModelPortal; Q9W7R4; -.
DR   STRING; 7955.ENSDARP00000109423; -.
DR   PaxDb; Q9W7R4; -.
DR   PRIDE; 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   eggNOG; ENOG410XQQD; LUCA.
DR   GeneTree; ENSGT00950000182725; -.
DR   HOGENOM; HOG000231701; -.
DR   HOVERGEN; HBG080306; -.
DR   InParanoid; Q9W7R4; -.
DR   OrthoDB; 7516at2759; -.
DR   PhylomeDB; Q9W7R4; -.
DR   PRO; PR:Q9W7R4; -.
DR   Proteomes; UP000000437; Chromosome 1.
DR   Bgee; ENSDARG00000005479; Expressed in 51 organ(s), highest expression level in multi-cellular organism.
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; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR022385; Rhs_assc_core.
DR   InterPro; IPR027689; Ten-2/3.
DR   InterPro; IPR009471; Ten_N.
DR   InterPro; IPR028916; Tox-GHH_dom.
DR   InterPro; IPR006530; YD.
DR   PANTHER; PTHR11219:SF64; PTHR11219:SF64; 2.
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   Complete proteome; Differentiation; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Membrane; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   2694       Teneurin-3.
FT                                /FTId=PRO_0000259507.
FT   TOPO_DOM      1    312       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    313    333       Helical. {ECO:0000255}.
FT   TOPO_DOM    334   2694       Extracellular. {ECO:0000255}.
FT   DOMAIN        1    306       Teneurin N-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00694}.
FT   DOMAIN      508    539       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      540    570       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      572    604       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      605    636       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      638    671       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      672    703       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      704    733       EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      734    768       EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT     1166   1192       NHL 1.
FT   REPEAT     1194   1238       NHL 2.
FT   REPEAT     1264   1308       NHL 3.
FT   REPEAT     1325   1365       NHL 4.
FT   REPEAT     1452   1495       NHL 5.
FT   REPEAT     1505   1524       YD 1.
FT   REPEAT     1541   1561       YD 2.
FT   REPEAT     1604   1623       YD 3.
FT   REPEAT     1624   1646       YD 4.
FT   REPEAT     1817   1836       YD 5.
FT   REPEAT     1858   1876       YD 6.
FT   REPEAT     1877   1897       YD 7.
FT   REPEAT     1904   1921       YD 8.
FT   REPEAT     1922   1943       YD 9.
FT   REPEAT     1944   1961       YD 10.
FT   REPEAT     1964   1984       YD 11.
FT   REPEAT     1987   2007       YD 12.
FT   REPEAT     2015   2034       YD 13.
FT   REPEAT     2040   2057       YD 14.
FT   REPEAT     2058   2084       YD 15.
FT   REPEAT     2086   2099       YD 16.
FT   REPEAT     2100   2123       YD 17.
FT   REPEAT     2126   2146       YD 18.
FT   REPEAT     2147   2167       YD 19.
FT   REPEAT     2169   2189       YD 20.
FT   REPEAT     2201   2221       YD 21.
FT   REPEAT     2223   2243       YD 22.
FT   REPEAT     2269   2310       YD 23.
FT   CARBOHYD    374    374       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    413    413       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    664    664       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    854    854       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    877    877       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1048   1048       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1196   1196       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1521   1521       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1538   1538       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1634   1634       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1671   1671       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1729   1729       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1814   1814       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1915   1915       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2118   2118       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2258   2258       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2571   2571       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    512    522       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    516    527       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    529    538       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    547    558       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    560    569       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    576    587       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    581    592       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    594    603       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    608    619       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    613    624       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    626    635       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    646    659       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    661    670       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    675    685       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    679    690       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    692    701       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    706    716       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    710    721       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    723    732       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    737    747       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    741    756       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    758    767       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   VAR_SEQ       1    104       Missing (in isoform 2).
FT                                /FTId=VSP_059563.
FT   CONFLICT    781    781       N -> S (in Ref. 1; BAA81892).
FT                                {ECO:0000305}.
FT   CONFLICT    813    813       I -> F (in Ref. 1; BAA81892).
FT                                {ECO:0000305}.
FT   CONFLICT    892    892       R -> Q (in Ref. 1; BAA81892).
FT                                {ECO:0000305}.
FT   CONFLICT   1210   1210       R -> G (in Ref. 1; BAA81892).
FT                                {ECO:0000305}.
FT   CONFLICT   1880   1884       QDRLS -> HGKQI (in Ref. 1; BAA81892).
FT                                {ECO:0000305}.
FT   CONFLICT   2520   2520       A -> V (in Ref. 1; BAA81892).
FT                                {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
//
DBGET integrated database retrieval system