GenomeNet

Database: UniProt
Entry: Q9DER5
LinkDB: Q9DER5
Original site: Q9DER5 
ID   TEN2_CHICK              Reviewed;        2802 AA.
AC   Q9DER5; Q9PU49;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   16-JAN-2019, entry version 107.
DE   RecName: Full=Teneurin-2;
DE            Short=Ten-2;
DE   AltName: Full=Neurestin;
DE   AltName: Full=Protein Odd Oz/ten-m homolog 2;
DE   AltName: Full=Tenascin-M2;
DE            Short=Ten-m2;
DE   AltName: Full=Teneurin transmembrane protein 2;
DE   Contains:
DE     RecName: Full=Ten-2, soluble form;
DE   Contains:
DE     RecName: Full=Ten-2 intracellular domain;
DE              Short=Ten-2 ICD;
GN   Name=TENM2; Synonyms=ODZ2, TNM2;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=11146505;
RX   DOI=10.1002/1097-0177(2000)9999:9999<::AID-DVDY1084>3.0.CO;2-B;
RA   Tucker R.P., Chiquet-Ehrismann R., Chevron M.P., Martin D., Hall R.J.,
RA   Rubin B.P.;
RT   "Teneurin-2 is expressed in tissues that regulate limb and somite
RT   pattern formation and is induced in vitro and in situ by FGF8.";
RL   Dev. Dyn. 220:27-39(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-936 (ISOFORM 2), FUNCTION IN FILOPODIA
RP   FORMATION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=10588872; DOI=10.1006/dbio.1999.9503;
RA   Rubin B.P., Tucker R.P., Martin D., Chiquet-Ehrismann R.;
RT   "Teneurins: a novel family of neuronal cell surface proteins in
RT   vertebrates, homologous to the Drosophila pair-rule gene product Ten-
RT   m.";
RL   Dev. Biol. 216:195-209(1999).
RN   [3]
RP   FUNCTION IN CELL ADHESION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=12361962;
RA   Rubin B.P., Tucker R.P., Brown-Luedi M., Martin D.,
RA   Chiquet-Ehrismann R.;
RT   "Teneurin 2 is expressed by the neurons of the thalamofugal visual
RT   system in situ and promotes homophilic cell-cell adhesion in vitro.";
RL   Development 129:4697-4705(2002).
RN   [4]
RP   PROTEOLYTIC PROCESSING, FUNCTION OF TEN-2 ICD, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=12783990; DOI=10.1242/jcs.00603;
RA   Bagutti C., Forro G., Ferralli J., Rubin B., Chiquet-Ehrismann R.;
RT   "The intracellular domain of teneurin-2 has a nuclear function and
RT   represses zic-1-mediated transcription.";
RL   J. Cell Sci. 116:2957-2966(2003).
RN   [5]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=18366734; DOI=10.1186/1471-213X-8-30;
RA   Kenzelmann D., Chiquet-Ehrismann R., Leachman N.T., Tucker R.P.;
RT   "Teneurin-1 is expressed in interconnected regions of the developing
RT   brain and is processed in vivo.";
RL   BMC Dev. Biol. 8:30-30(2008).
CC   -!- FUNCTION: Acts as a ligand of the ADGRL1 receptor (By similarity).
CC       Involved in neural development, regulating the establishment of
CC       proper connectivity within the nervous system. Promotes the
CC       formation of filopodia and enlarged growth cone in neuronal cells.
CC       Induces homophilic cell-cell adhesion. May also mediates axon
CC       guidance and heterophilic cell-cell adhesion. May function as a
CC       cellular signal transducer. {ECO:0000250,
CC       ECO:0000269|PubMed:10588872, ECO:0000269|PubMed:12361962,
CC       ECO:0000269|PubMed:12783990}.
CC   -!- FUNCTION: Ten-2 intracellular domain: Induces gene transcription
CC       inhibition.
CC   -!- SUBUNIT: Homodimer; disulfide-linked (Probable). Heterodimer with
CC       other teneurins (By similarity). {ECO:0000250, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC       Endoplasmic reticulum. Golgi apparatus. Cell projection,
CC       filopodium. Cell projection, growth cone. Cell projection,
CC       dendrite. Cell junction, synapse {ECO:0000250}. Cell projection,
CC       dendritic spine {ECO:0000250}. Cell junction, synapse,
CC       postsynaptic cell membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000250}. Cell junction, synapse, synaptosome
CC       {ECO:0000250}. Note=Localized at plasma membrane of neurites and
CC       growth cones. Enriched in cell-cell contact areas.
CC   -!- SUBCELLULAR LOCATION: Ten-2 intracellular domain: Nucleus, PML
CC       body. Note=Upon proteolytic cleavage, is translocated into the
CC       nucleus and accumulates within PML bodies.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9DER5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9DER5-2; Sequence=VSP_021398;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=Q9DER5-3; Sequence=VSP_021399;
CC       Name=4;
CC         IsoId=Q9DER5-4; Sequence=VSP_021400, VSP_021401;
CC   -!- DEVELOPMENTAL STAGE: Expressed in external plexiform layer and
CC       laminae 1 and 3 within the inner plexiform layer (at protein
CC       level). Expression started to be detectable in 4-day-old embryos,
CC       both in the body as well as the head (brain) of the embryos.
CC       Expressed in neurons of the inner plexiform layer (IPL), the optic
CC       fiber layer (OFL) and the optic nerve at embryonic day (E) 11.
CC       Expressed in the neurons of the entire retinal ganglion cell layer
CC       at E12. Expressed by the neurons of the thalamofugal visual
CC       pathway at E18. Expressed in the developing limb buds, somites,
CC       and craniofacial mesenchyme at E19. In the limbs, expressed
CC       transiently in the apical ectodermal ridge (AER) and later at
CC       sites of tendon morphogenesis. Also found in the notochord, dorsal
CC       neural tube, and dorsomedial lip of the somite as well as the
CC       flank mesoderm. {ECO:0000269|PubMed:11146505,
CC       ECO:0000269|PubMed:12361962, ECO:0000269|PubMed:18366734}.
CC   -!- DOMAIN: EGF-like domains 2 and 5 which have an odd number of
CC       cysteines might enable the formation of intermolecular disulfide
CC       bonds.
CC   -!- DOMAIN: Cytoplasmic proline-rich regions could serve as docking
CC       domains for intracellular SH3-containing proteins.
CC   -!- PTM: Ten-2, soluble form: Derives from the membrane form by
CC       proteolytic processing.
CC   -!- PTM: Ten-2 intracellular domain: Derives from the plasma membrane
CC       form by proteolytic cleavage and translocates to the nucleus.
CC       Homophilic binding of the C-terminal extracellular domain
CC       stimulates its proteolytic cleavage and release in the
CC       cytoplasmic. Is subjected to rapid degradation by the proteasome
CC       pathway.
CC   -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC       {ECO:0000305}.
DR   EMBL; AJ279031; CAC09416.1; -; mRNA.
DR   EMBL; AJ245711; CAB57257.1; -; mRNA.
DR   RefSeq; NP_001003718.1; NM_001003718.1.
DR   RefSeq; NP_989428.2; NM_204097.2.
DR   UniGene; Gga.2983; -.
DR   PDB; 6FB3; X-ray; 2.38 A; A/B/C/D=955-2802.
DR   PDBsum; 6FB3; -.
DR   ProteinModelPortal; Q9DER5; -.
DR   SMR; Q9DER5; -.
DR   STRING; 9031.ENSGALP00000002709; -.
DR   PaxDb; Q9DER5; -.
DR   PRIDE; Q9DER5; -.
DR   GeneID; 373854; -.
DR   KEGG; gga:373854; -.
DR   CTD; 57451; -.
DR   eggNOG; KOG1225; Eukaryota.
DR   eggNOG; KOG4659; Eukaryota.
DR   eggNOG; ENOG410XQQD; LUCA.
DR   HOGENOM; HOG000231701; -.
DR   HOVERGEN; HBG080306; -.
DR   InParanoid; Q9DER5; -.
DR   OrthoDB; 7516at2759; -.
DR   PhylomeDB; Q9DER5; -.
DR   PRO; PR:Q9DER5; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0030054; C:cell junction; IDA:UniProtKB.
DR   GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR   GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0050839; F:cell adhesion molecule binding; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0005102; F:signaling receptor binding; ISS:UniProtKB.
DR   GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR   GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISS:UniProtKB.
DR   GO; GO:0098609; P:cell-cell adhesion; IDA:UniProtKB.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0048666; P:neuron development; IBA:GO_Central.
DR   GO; GO:0051491; P:positive regulation of filopodium assembly; IDA:UniProtKB.
DR   Gene3D; 2.120.10.30; -; 2.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
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; 1.
DR   Pfam; PF07974; EGF_2; 1.
DR   Pfam; PF06484; Ten_N; 1.
DR   Pfam; PF15636; Tox-GHH; 1.
DR   SMART; SM00181; EGF; 8.
DR   SMART; SM00179; EGF_CA; 2.
DR   SUPFAM; SSF49464; SSF49464; 1.
DR   SUPFAM; SSF50998; SSF50998; 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; 5.
DR   PROSITE; PS51361; TENEURIN_N; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell adhesion; Cell junction;
KW   Cell membrane; Cell projection; Cleavage on pair of basic residues;
KW   Complete proteome; Disulfide bond; EGF-like domain;
KW   Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Membrane;
KW   Nucleus; Postsynaptic cell membrane; Reference proteome; Repeat;
KW   Repressor; Synapse; Synaptosome; Transcription;
KW   Transcription regulation; Transmembrane; Transmembrane helix.
FT   CHAIN         1   2802       Teneurin-2.
FT                                /FTId=PRO_0000259504.
FT   CHAIN         1      ?       Ten-2 intracellular domain.
FT                                /FTId=PRO_0000421017.
FT   CHAIN       557   2802       Ten-2, soluble form.
FT                                /FTId=PRO_0000421018.
FT   TOPO_DOM      1    407       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    408    428       Helical. {ECO:0000255}.
FT   TOPO_DOM    429   2802       Extracellular. {ECO:0000255}.
FT   DOMAIN        1    403       Teneurin N-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00694}.
FT   DOMAIN      603    631       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      633    662       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      664    696       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      697    729       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      730    763       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      766    794       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      797    825       EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      836    869       EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT     1300   1344       NHL 1.
FT   REPEAT     1370   1414       NHL 2.
FT   REPEAT     1429   1480       NHL 3.
FT   REPEAT     1502   1529       NHL 4.
FT   REPEAT     1558   1601       NHL 5.
FT   REPEAT     1611   1630       YD 1.
FT   REPEAT     1647   1667       YD 2.
FT   REPEAT     1710   1729       YD 3.
FT   REPEAT     1730   1752       YD 4.
FT   REPEAT     1923   1942       YD 5.
FT   REPEAT     1964   1982       YD 6.
FT   REPEAT     1983   2003       YD 7.
FT   REPEAT     2010   2027       YD 8.
FT   REPEAT     2028   2049       YD 9.
FT   REPEAT     2050   2067       YD 10.
FT   REPEAT     2070   2090       YD 11.
FT   REPEAT     2093   2113       YD 12.
FT   REPEAT     2121   2141       YD 13.
FT   REPEAT     2147   2164       YD 14.
FT   REPEAT     2165   2191       YD 15.
FT   REPEAT     2193   2206       YD 16.
FT   REPEAT     2207   2230       YD 17.
FT   REPEAT     2233   2253       YD 18.
FT   REPEAT     2254   2274       YD 19.
FT   REPEAT     2276   2296       YD 20.
FT   REPEAT     2308   2328       YD 21.
FT   REPEAT     2330   2350       YD 22.
FT   REPEAT     2376   2417       YD 23.
FT   COMPBIAS    203    206       Poly-Ser.
FT   COMPBIAS    359    362       Poly-Ser.
FT   SITE        556    557       Cleavage. {ECO:0000305}.
FT   CARBOHYD    471    471       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    510    510       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    953    953       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    976    976       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1295   1295       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1644   1644       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1740   1740       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1777   1777       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1801   1801       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1835   1835       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1920   1920       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2021   2021       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2225   2225       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2365   2365       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2676   2676       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    604    614       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    608    619       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    621    630       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    639    650       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    652    661       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    668    679       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    673    684       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    686    695       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    700    711       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    705    716       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    718    727       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    738    751       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    753    762       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    767    777       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    771    782       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    784    793       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    798    808       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    802    813       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    815    824       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    838    848       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    842    857       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    859    868       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   VAR_SEQ     168    196       DFHTHLSEKLKDRQTSWQQLAETKNSLIR -> G (in
FT                                isoform 2).
FT                                {ECO:0000303|PubMed:10588872}.
FT                                /FTId=VSP_021398.
FT   VAR_SEQ     829    836       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:11146505}.
FT                                /FTId=VSP_021399.
FT   VAR_SEQ     836    859       DGCPDLCNGNGRCTLGQNSWQCVC -> SYCFLFINRRDIV
FT                                TVVYCDRLFL (in isoform 4).
FT                                {ECO:0000303|PubMed:11146505}.
FT                                /FTId=VSP_021400.
FT   VAR_SEQ     860   2802       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:11146505}.
FT                                /FTId=VSP_021401.
FT   CONFLICT     36     36       A -> T (in Ref. 2; CAB57257).
FT                                {ECO:0000305}.
FT   CONFLICT     50     50       G -> D (in Ref. 2; CAB57257).
FT                                {ECO:0000305}.
FT   CONFLICT    139    139       S -> R (in Ref. 2; CAB57257).
FT                                {ECO:0000305}.
FT   CONFLICT    836    859       DGCPDLCNGNGRCTLGQNSWQCVC -> GSYCFLFINRRDI
FT                                VTVVYCDRLFL (in Ref. 2; CAB57257).
FT                                {ECO:0000305}.
FT   STRAND      957    965       {ECO:0000244|PDB:6FB3}.
FT   STRAND      967    969       {ECO:0000244|PDB:6FB3}.
FT   STRAND      976    981       {ECO:0000244|PDB:6FB3}.
FT   STRAND      984    989       {ECO:0000244|PDB:6FB3}.
FT   STRAND      995   1011       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1013   1015       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1019   1023       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1026   1031       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1058   1061       {ECO:0000244|PDB:6FB3}.
FT   TURN       1072   1074       {ECO:0000244|PDB:6FB3}.
FT   TURN       1079   1082       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1083   1089       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1096   1100       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1103   1107       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1109   1114       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1124   1133       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1136   1143       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1149   1154       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1165   1178       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1181   1195       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1207   1209       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1214   1216       {ECO:0000244|PDB:6FB3}.
FT   TURN       1217   1220       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1221   1223       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1229   1231       {ECO:0000244|PDB:6FB3}.
FT   HELIX      1232   1234       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1238   1244       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1246   1248       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1257   1261       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1268   1273       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1279   1283       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1286   1290       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1294   1301       {ECO:0000244|PDB:6FB3}.
FT   HELIX      1307   1309       {ECO:0000244|PDB:6FB3}.
FT   HELIX      1313   1315       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1317   1321       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1323   1325       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1328   1332       {ECO:0000244|PDB:6FB3}.
FT   TURN       1333   1336       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1337   1342       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1354   1358       {ECO:0000244|PDB:6FB3}.
FT   TURN       1371   1375       {ECO:0000244|PDB:6FB3}.
FT   TURN       1378   1380       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1386   1391       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1397   1401       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1404   1408       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1413   1418       {ECO:0000244|PDB:6FB3}.
FT   TURN       1423   1425       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1431   1433       {ECO:0000244|PDB:6FB3}.
FT   HELIX      1437   1439       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1443   1450       {ECO:0000244|PDB:6FB3}.
FT   TURN       1452   1454       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1457   1463       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1465   1468       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1473   1478       {ECO:0000244|PDB:6FB3}.
FT   HELIX      1482   1484       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1486   1488       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1495   1497       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1503   1510       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1516   1521       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1523   1525       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1527   1532       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1536   1542       {ECO:0000244|PDB:6FB3}.
FT   TURN       1550   1552       {ECO:0000244|PDB:6FB3}.
FT   TURN       1566   1568       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1574   1579       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1585   1589       {ECO:0000244|PDB:6FB3}.
FT   HELIX      1590   1592       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1594   1599       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1609   1615       {ECO:0000244|PDB:6FB3}.
FT   TURN       1616   1619       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1620   1625       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1629   1635       {ECO:0000244|PDB:6FB3}.
FT   TURN       1636   1638       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1641   1647       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1653   1658       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1663   1668       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1674   1678       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1684   1689       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1695   1699       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1704   1711       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1717   1721       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1727   1732       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1738   1742       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1748   1767       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1772   1778       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1780   1789       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1792   1799       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1804   1807       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1813   1821       {ECO:0000244|PDB:6FB3}.
FT   TURN       1822   1824       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1825   1837       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1844   1856       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1859   1869       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1872   1880       {ECO:0000244|PDB:6FB3}.
FT   TURN       1881   1884       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1885   1889       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1896   1901       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1907   1913       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1919   1923       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1929   1934       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1937   1943       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1949   1954       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1959   1965       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1968   1972       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1978   1983       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1989   1993       {ECO:0000244|PDB:6FB3}.
FT   STRAND     1999   2006       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2008   2016       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2024   2028       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2034   2039       {ECO:0000244|PDB:6FB3}.
FT   TURN       2040   2043       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2044   2050       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2054   2061       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2064   2070       {ECO:0000244|PDB:6FB3}.
FT   TURN       2072   2074       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2077   2084       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2087   2096       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2099   2107       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2109   2111       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2115   2121       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2128   2135       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2143   2147       {ECO:0000244|PDB:6FB3}.
FT   TURN       2149   2151       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2154   2157       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2160   2165       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2168   2172       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2174   2182       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2188   2195       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2198   2207       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2213   2224       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2226   2233       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2239   2244       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2247   2254       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2260   2263       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2272   2276       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2282   2285       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2288   2292       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2298   2301       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2304   2308       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2314   2319       {ECO:0000244|PDB:6FB3}.
FT   TURN       2320   2323       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2324   2330       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2336   2341       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2346   2350       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2354   2356       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2362   2365       {ECO:0000244|PDB:6FB3}.
FT   TURN       2366   2369       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2370   2376       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2382   2387       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2392   2397       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2403   2407       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2413   2419       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2425   2429       {ECO:0000244|PDB:6FB3}.
FT   HELIX      2439   2441       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2442   2445       {ECO:0000244|PDB:6FB3}.
FT   TURN       2446   2449       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2450   2452       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2457   2459       {ECO:0000244|PDB:6FB3}.
FT   TURN       2460   2463       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2464   2467       {ECO:0000244|PDB:6FB3}.
FT   HELIX      2472   2475       {ECO:0000244|PDB:6FB3}.
FT   TURN       2476   2478       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2485   2488       {ECO:0000244|PDB:6FB3}.
FT   HELIX      2489   2491       {ECO:0000244|PDB:6FB3}.
FT   HELIX      2500   2502       {ECO:0000244|PDB:6FB3}.
FT   HELIX      2507   2513       {ECO:0000244|PDB:6FB3}.
FT   HELIX      2518   2520       {ECO:0000244|PDB:6FB3}.
FT   HELIX      2537   2544       {ECO:0000244|PDB:6FB3}.
FT   HELIX      2553   2566       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2600   2605       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2608   2613       {ECO:0000244|PDB:6FB3}.
FT   HELIX      2619   2628       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2639   2641       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2644   2653       {ECO:0000244|PDB:6FB3}.
FT   HELIX      2656   2662       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2665   2670       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2676   2680       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2683   2686       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2689   2692       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2695   2700       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2703   2712       {ECO:0000244|PDB:6FB3}.
FT   HELIX      2715   2745       {ECO:0000244|PDB:6FB3}.
FT   HELIX      2755   2763       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2770   2776       {ECO:0000244|PDB:6FB3}.
FT   TURN       2778   2780       {ECO:0000244|PDB:6FB3}.
FT   HELIX      2782   2784       {ECO:0000244|PDB:6FB3}.
FT   HELIX      2788   2790       {ECO:0000244|PDB:6FB3}.
FT   STRAND     2791   2795       {ECO:0000244|PDB:6FB3}.
SQ   SEQUENCE   2802 AA;  310749 MW;  B1FBC2C84EDFA4B3 CRC64;
     MDIKDRRHRS LTRGRCGKEC RYTSSSLDSE DCRVPAQKSY SSSETLKAYG HDTRMHYGNR
     VSDLVHRESD EFPRQGTNFT LAELGICEPS PHRSGYCSDI GILHQGYSLS TGSDADSDTE
     GGMSPEHAIR LWGRGIKSSR SSGLSSRENS ALTLTDSDNE NKSDEENDFH THLSEKLKDR
     QTSWQQLAET KNSLIRRPIP PTSSSSLLPS AQLPSSHNPP PVSCQMPLLD SNTSHQIMDT
     NPDEEFSPNS YLLRACSGPQ QASSSGPSNH HSQSTLRPPL PPPHNHSLSH HHSSANSLNR
     NSLTNRRNQI HAPAPAPNDL ATTPESVQLQ DSWVLNSNVP LETRHFLFKT SSGTTPLFSS
     SSPGYPLTSG TVYTPPPRLL PRNTFSRNAF KLKKPSKYCS WKCAALSAIA AAVLLAILLA
     YFIAMHLLGL NWQLQPADGH TFSNGLRPGA AGAEDGAAAP PAGRGPWVTR NSSIDSGETE
     VGRKVTQEVP PGVFWRSQIH ISQPQFLKFN ISLGKDALFG VYIRRGLPPS HAQYDFMERL
     DGKEKWSVVE SPRERRSIQT LVQNEAVFVQ YLDVGLWHLA FYNDGKDKEV VSFSTVILDS
     VQDCPRNCHG NGECVSGVCH CFPGFHGADC AKAACPVLCS GNGQYSKGTC LCYSGWKGPE
     CDVPISQCID PSCGGHGSCI EGNCVCSIGY KGENCEEVDC LDPTCSNHGV CVNGECLCSP
     GWGGINCELP RAQCPDQCSG HGTYLSDTGL CSCDPNWMGP DCSVEVCSVD CGTHGVCIGG
     ACRCEEGWTG VACDQRVCHP RCTEHGTCKD GKCECREGWN GEHCTIGRQT TGTETDGCPD
     LCNGNGRCTL GQNSWQCVCQ TGWRGPGCNV AMETSCADNK DNEGDGLVDC LVPDCCLQST
     CQNSLLCRGS RDPLDIIQQS HSGSPAVKSF YDRIKLLVGK DSTHIIPGEN PFNSSLVSLI
     RGQVVTTDGT PLVGVNVSFV KYPKYGYTIT RQDGMFDLVA NGGSSLTLHF ERAPFMSQER
     TVWLPWNSFY AMDTLVMKTE ENSIPSCDLS GFVRPDPVII SSPLSTFFSD APGRNPIVPE
     TQVLHEEIEV PGSSIKLIYL SSRTAGYKSL LKIIMTQSLV PLNLIKVHLM VAVEGHLFQK
     SFLASPNLAY TFIWDKTDAY GQKVYGLSDA VVSVGFEYET CPSLILWEKR TALLQGFELD
     PSNLGGWSLD KHHVLNVKSG ILHKGNGENQ FLTQQPAVIT SIMGNGRRRS ISCPSCNGLA
     EGNKLLAPVA LAVGIDGSLF VGDFNYIRRI FPSRNVTSIL ELRNKEFKHS NNPAHKYYLA
     VDPVSGSLYV SDTNSRRIYK VKSLTGTKDL AGNSEVVAGT GEQCLPFDEA RCGDGGKAVD
     ATLMSPRGIA VDKYGLMYFV DATMIRKVDQ NGIISTLLGS NDLTAVRPLS CDSSMDVSQV
     RLEWPTDLAV DPMDNSLYVL ENNVILRITE NHQVSIIAGR PMHCQVPGID YSLSKLAIHS
     ALESASAIAI SHTGVLYISE TDEKKINRLR QVTTNGEICL LAGAASDCDC KNDVNCNCYS
     GDDGYATDAI LNSPSSLAVA PDGTIYIADL GNIRIRAVSK NRPILNSFNQ YEAASPGEQE
     LYVFNADGIH QYTLSLVTGE YLYNFTYSSD NDVTEVMDSN GNSLKVRRDA SGMPRHLLMP
     DNQIVTLAVG TNGGLKLVST QTLELGLMTY NGNSGLLATK SDETGWTTFY DYDHEGRLTN
     VTRPTGVVTS LHREMEKSIT IDIENSNRDD DVTVITNLSS VEASYTVVQD QVRNSYQLCN
     NGTLRVMYAN GMSISFHSEP HVLAGTVTPT IGRCNISLPM ENGLNSIEWR LRKEQIKGKV
     TVFGRKLRVH GRNLLSIDYD RNIRTEKIYD DHRKFTLRII YDQLGRPFLW LPSSGLAAVN
     VSYFFNGRLA GLQRGAMSER TDIDKQGRII SRMFADGKVW SYTYLEKSMV LLLQSQRQYI
     FEYDSSDRLH AVTMPSVARH SMSTHTSVGY IRNIYNPPES NASVIFDYSD DGRILKTSFL
     GTGRQVFYKY GKLSKLSEIV YDSTAVTFGY DETTGVLKMV NLQSGGFSCT IRYRKIGPLV
     DKQIYRFSEE GMVNARFDYT YHDNSFRIAS IKPIISETPL PVDLYRYDEI SGKVEHFGKF
     GVIYYDINQI ITTAVMTLSK HFDTHGRIKE VQYEMFRSLM YWMTVQYDSM GRVTKRELKL
     GPYANTTKYT YDYDGDGQLQ SVAVNDRPTW RYSYDLNGNL HLLNPGNSVR LMPLRYDLRD
     RITRLGDIPY KIDDDGFLCQ RGSDVFEYNS KGLLTRAYNK ANGWNVQYRY DGLGRRASCK
     TNLGHHLQYF YADLHNPTRV THVYNHSNSE ITSLYYDLQG HLFAMESSSG EEYYVASDNT
     GTPLAVFSIN GLMIKQLQYT AYGEIYYDSN PDFQLVIGFH GGLYDPLTKL VHFTQRDYDV
     LAGRWTSPDY TMWKNIGREP APFNLYMFKS NNPLSNELDL KNYVTDVKSW LVMFGFQLSN
     IIPGFPRAKM YFVSPPYELT ESQACENGQL ITGVQQTTER HNQAFMALEG QVISKRLHAS
     IREKAGHWFA TSTPIIGKGI MFAVKKGRVT TGISSIATDD SRKIASVLNS AHYLEKMHYS
     IEGKDTHYFV KIGSADSDLV TLAMTSGRKV LDSGVNVTVS QPTLLINGRT RRFTNIEFQY
     STLLINIRYG LTADTLDEEK ARVLDQARQR ALGSAWAKEQ QKARDGREGS RVWTDGEKQQ
     LLNTGRVQGY EGYYVLPVEQ YPELADSSSN IQFLRQNEMG KR
//
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