TEN2_CHICK
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 03-AUG-2022, entry version 121.
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; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), AND DEVELOPMENTAL 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 pattern
RT 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 IDENTIFICATION
RP 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-m.";
RL Dev. Biol. 216:195-209(1999).
RN [3]
RP FUNCTION IN CELL ADHESION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=12361962; DOI=10.1242/dev.129.20.4697;
RA Rubin B.P., Tucker R.P., Brown-Luedi M., Martin D., Chiquet-Ehrismann R.;
RT "Teneurin 2 is expressed by the neurons of the thalamofugal visual system
RT 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 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 brain
RT 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 proper
CC connectivity within the nervous system. Promotes the formation of
CC filopodia and enlarged growth cone in neuronal cells. Induces
CC homophilic cell-cell adhesion. May also mediate axon guidance and
CC heterophilic cell-cell adhesion. May function as a cellular signal
CC transducer. {ECO:0000250, ECO:0000269|PubMed:10588872,
CC ECO:0000269|PubMed:12361962, ECO:0000269|PubMed:12783990}.
CC -!- FUNCTION: [Ten-2 intracellular domain]: Induces gene transcription
CC inhibition.
CC -!- SUBUNIT: Homodimer; disulfide-linked (Probable). Heterodimer with other
CC teneurins (By similarity). {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC Endoplasmic reticulum. Golgi apparatus. Cell projection, filopodium.
CC Cell projection, growth cone. Cell projection, dendrite. Synapse
CC {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}.
CC Postsynaptic cell membrane {ECO:0000250}; Single-pass membrane protein
CC {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Note=Localized at
CC plasma membrane of neurites and growth cones. Enriched in cell-cell
CC contact areas.
CC -!- SUBCELLULAR LOCATION: [Ten-2 intracellular domain]: Nucleus, PML body.
CC Note=Upon proteolytic cleavage, is translocated into the nucleus and
CC 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 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 laminae
CC 1 and 3 within the inner plexiform layer (at protein level). Expression
CC started to be detectable in 4-day-old embryos, both in the body as well
CC as the head (brain) of the embryos. Expressed in neurons of the inner
CC plexiform layer (IPL), the optic fiber layer (OFL) and the optic nerve
CC at embryonic day (E) 11. Expressed in the neurons of the entire retinal
CC ganglion cell layer at E12. Expressed by the neurons of the
CC thalamofugal visual pathway at E18. Expressed in the developing limb
CC buds, somites, and craniofacial mesenchyme at E19. In the limbs,
CC expressed 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 flank
CC mesoderm. {ECO:0000269|PubMed:11146505, ECO:0000269|PubMed:12361962,
CC ECO:0000269|PubMed:18366734}.
CC -!- DOMAIN: EGF-like domains 2 and 5 which have an odd number of cysteines
CC might enable the formation of intermolecular disulfide bonds.
CC -!- DOMAIN: Cytoplasmic proline-rich regions could serve as docking domains
CC 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 stimulates
CC its proteolytic cleavage and release in the cytoplasmic. Is subjected
CC to rapid degradation by the proteasome pathway.
CC -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC {ECO:0000305}.
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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 PDB; 6FB3; X-ray; 2.38 A; A/B/C/D=955-2802.
DR PDB; 6SKA; X-ray; 3.86 A; A=956-2798.
DR PDB; 6SKE; X-ray; 3.62 A; A/C=1047-2802.
DR PDBsum; 6FB3; -.
DR PDBsum; 6SKA; -.
DR PDBsum; 6SKE; -.
DR SMR; Q9DER5; -.
DR BioGRID; 674934; 4.
DR STRING; 9031.ENSGALP00000002709; -.
DR PaxDb; Q9DER5; -.
DR PRIDE; Q9DER5; -.
DR GeneID; 373854; -.
DR KEGG; gga:373854; -.
DR CTD; 57451; -.
DR VEuPathDB; HostDB:geneid_373854; -.
DR eggNOG; KOG1225; Eukaryota.
DR eggNOG; KOG4659; Eukaryota.
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; 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.
DR InterPro; IPR009471; Ten_N.
DR InterPro; IPR028916; Tox-GHH_dom.
DR InterPro; IPR006530; YD.
DR PANTHER; PTHR11219:SF8; PTHR11219:SF8; 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 membrane;
KW Cell projection; Cleavage on pair of basic residues; Disulfide bond;
KW EGF-like domain; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Membrane; Nucleus; Postsynaptic cell membrane; Reference proteome; Repeat;
KW Repressor; Synapse; Synaptosome; Transcription; Transcription regulation;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..2802
FT /note="Teneurin-2"
FT /id="PRO_0000259504"
FT CHAIN 1..?
FT /note="Ten-2 intracellular domain"
FT /id="PRO_0000421017"
FT CHAIN 557..2802
FT /note="Ten-2, soluble form"
FT /id="PRO_0000421018"
FT TOPO_DOM 1..407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 429..2802
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 1..403
FT /note="Teneurin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00694"
FT DOMAIN 603..631
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 633..662
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 664..696
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 697..729
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 730..763
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 766..794
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 797..825
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 836..869
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1300..1344
FT /note="NHL 1"
FT REPEAT 1370..1414
FT /note="NHL 2"
FT REPEAT 1429..1480
FT /note="NHL 3"
FT REPEAT 1502..1529
FT /note="NHL 4"
FT REPEAT 1558..1601
FT /note="NHL 5"
FT REPEAT 1611..1630
FT /note="YD 1"
FT REPEAT 1647..1667
FT /note="YD 2"
FT REPEAT 1710..1729
FT /note="YD 3"
FT REPEAT 1730..1752
FT /note="YD 4"
FT REPEAT 1923..1942
FT /note="YD 5"
FT REPEAT 1964..1982
FT /note="YD 6"
FT REPEAT 1983..2003
FT /note="YD 7"
FT REPEAT 2010..2027
FT /note="YD 8"
FT REPEAT 2028..2049
FT /note="YD 9"
FT REPEAT 2050..2067
FT /note="YD 10"
FT REPEAT 2070..2090
FT /note="YD 11"
FT REPEAT 2093..2113
FT /note="YD 12"
FT REPEAT 2121..2141
FT /note="YD 13"
FT REPEAT 2147..2164
FT /note="YD 14"
FT REPEAT 2165..2191
FT /note="YD 15"
FT REPEAT 2193..2206
FT /note="YD 16"
FT REPEAT 2207..2230
FT /note="YD 17"
FT REPEAT 2233..2253
FT /note="YD 18"
FT REPEAT 2254..2274
FT /note="YD 19"
FT REPEAT 2276..2296
FT /note="YD 20"
FT REPEAT 2308..2328
FT /note="YD 21"
FT REPEAT 2330..2350
FT /note="YD 22"
FT REPEAT 2376..2417
FT /note="YD 23"
FT REGION 138..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 556..557
FT /note="Cleavage"
FT /evidence="ECO:0000305"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 953
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 976
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1740
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1777
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1801
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1835
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1920
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2021
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 604..614
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 608..619
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 621..630
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 639..650
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 652..661
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 668..679
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 673..684
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 686..695
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 700..711
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 705..716
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 718..727
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 738..751
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 753..762
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 767..777
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 771..782
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 784..793
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 798..808
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 802..813
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 815..824
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 838..848
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 842..857
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 859..868
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 168..196
FT /note="DFHTHLSEKLKDRQTSWQQLAETKNSLIR -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10588872"
FT /id="VSP_021398"
FT VAR_SEQ 829..836
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11146505"
FT /id="VSP_021399"
FT VAR_SEQ 836..859
FT /note="DGCPDLCNGNGRCTLGQNSWQCVC -> SYCFLFINRRDIVTVVYCDRLFL
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11146505"
FT /id="VSP_021400"
FT VAR_SEQ 860..2802
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11146505"
FT /id="VSP_021401"
FT CONFLICT 36
FT /note="A -> T (in Ref. 2; CAB57257)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="G -> D (in Ref. 2; CAB57257)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="S -> R (in Ref. 2; CAB57257)"
FT /evidence="ECO:0000305"
FT CONFLICT 836..859
FT /note="DGCPDLCNGNGRCTLGQNSWQCVC -> GSYCFLFINRRDIVTVVYCDRLFL
FT (in Ref. 2; CAB57257)"
FT /evidence="ECO:0000305"
FT STRAND 957..965
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 967..969
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 976..981
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 984..989
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 995..1011
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1013..1015
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1019..1023
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1026..1031
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1058..1061
FT /evidence="ECO:0007829|PDB:6FB3"
FT TURN 1072..1074
FT /evidence="ECO:0007829|PDB:6FB3"
FT TURN 1079..1082
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1083..1089
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1096..1100
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1103..1107
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1109..1114
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1124..1133
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1136..1143
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1149..1154
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1165..1178
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1181..1195
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1207..1209
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1214..1216
FT /evidence="ECO:0007829|PDB:6FB3"
FT TURN 1217..1220
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1221..1223
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1229..1231
FT /evidence="ECO:0007829|PDB:6FB3"
FT HELIX 1232..1234
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1238..1244
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1246..1248
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1257..1261
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1268..1273
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1279..1283
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1286..1290
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1294..1301
FT /evidence="ECO:0007829|PDB:6FB3"
FT HELIX 1307..1309
FT /evidence="ECO:0007829|PDB:6FB3"
FT HELIX 1313..1315
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1317..1321
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1323..1325
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1328..1332
FT /evidence="ECO:0007829|PDB:6FB3"
FT TURN 1333..1336
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1337..1342
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1354..1358
FT /evidence="ECO:0007829|PDB:6FB3"
FT TURN 1371..1375
FT /evidence="ECO:0007829|PDB:6FB3"
FT TURN 1378..1380
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1386..1391
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1397..1401
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1404..1408
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1413..1418
FT /evidence="ECO:0007829|PDB:6FB3"
FT TURN 1423..1425
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1431..1433
FT /evidence="ECO:0007829|PDB:6FB3"
FT HELIX 1437..1439
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1443..1450
FT /evidence="ECO:0007829|PDB:6FB3"
FT TURN 1452..1454
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1457..1463
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1465..1468
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1473..1478
FT /evidence="ECO:0007829|PDB:6FB3"
FT HELIX 1482..1484
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1486..1488
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1495..1497
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1503..1510
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1516..1521
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1523..1525
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1527..1532
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1536..1542
FT /evidence="ECO:0007829|PDB:6FB3"
FT TURN 1550..1552
FT /evidence="ECO:0007829|PDB:6FB3"
FT TURN 1566..1568
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1574..1579
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1585..1589
FT /evidence="ECO:0007829|PDB:6FB3"
FT HELIX 1590..1592
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1594..1599
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1609..1615
FT /evidence="ECO:0007829|PDB:6FB3"
FT TURN 1616..1619
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1620..1625
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1629..1635
FT /evidence="ECO:0007829|PDB:6FB3"
FT TURN 1636..1638
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1641..1647
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1653..1658
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1663..1668
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1674..1678
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1684..1689
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1695..1699
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1704..1711
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1717..1721
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1727..1732
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1738..1742
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1748..1767
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1772..1778
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1780..1789
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1792..1799
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1804..1807
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1813..1821
FT /evidence="ECO:0007829|PDB:6FB3"
FT TURN 1822..1824
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1825..1837
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1844..1856
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1859..1869
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1872..1880
FT /evidence="ECO:0007829|PDB:6FB3"
FT TURN 1881..1884
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1885..1889
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1896..1901
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1907..1913
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1919..1923
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1929..1934
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1937..1943
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1949..1954
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1959..1965
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1968..1972
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1978..1983
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1989..1993
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 1999..2006
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2008..2016
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2024..2028
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2034..2039
FT /evidence="ECO:0007829|PDB:6FB3"
FT TURN 2040..2043
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2044..2050
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2054..2061
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2064..2070
FT /evidence="ECO:0007829|PDB:6FB3"
FT TURN 2072..2074
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2077..2084
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2087..2096
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2099..2107
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2109..2111
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2115..2121
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2128..2135
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2143..2147
FT /evidence="ECO:0007829|PDB:6FB3"
FT TURN 2149..2151
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2154..2157
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2160..2165
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2168..2172
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2174..2182
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2188..2195
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2198..2207
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2213..2224
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2226..2233
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2239..2244
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2247..2254
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2260..2263
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2272..2276
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2282..2285
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2288..2292
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2298..2301
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2304..2308
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2314..2319
FT /evidence="ECO:0007829|PDB:6FB3"
FT TURN 2320..2323
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2324..2330
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2336..2341
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2346..2350
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2354..2356
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2362..2365
FT /evidence="ECO:0007829|PDB:6FB3"
FT TURN 2366..2369
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2370..2376
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2382..2387
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2392..2397
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2403..2407
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2413..2419
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2425..2429
FT /evidence="ECO:0007829|PDB:6FB3"
FT HELIX 2439..2441
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2442..2445
FT /evidence="ECO:0007829|PDB:6FB3"
FT TURN 2446..2449
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2450..2452
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2457..2459
FT /evidence="ECO:0007829|PDB:6FB3"
FT TURN 2460..2463
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2464..2467
FT /evidence="ECO:0007829|PDB:6FB3"
FT HELIX 2472..2475
FT /evidence="ECO:0007829|PDB:6FB3"
FT TURN 2476..2478
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2485..2488
FT /evidence="ECO:0007829|PDB:6FB3"
FT HELIX 2489..2491
FT /evidence="ECO:0007829|PDB:6FB3"
FT HELIX 2500..2502
FT /evidence="ECO:0007829|PDB:6FB3"
FT HELIX 2507..2513
FT /evidence="ECO:0007829|PDB:6FB3"
FT HELIX 2518..2520
FT /evidence="ECO:0007829|PDB:6FB3"
FT HELIX 2537..2544
FT /evidence="ECO:0007829|PDB:6FB3"
FT HELIX 2553..2566
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2600..2605
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2608..2613
FT /evidence="ECO:0007829|PDB:6FB3"
FT HELIX 2619..2628
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2639..2641
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2644..2653
FT /evidence="ECO:0007829|PDB:6FB3"
FT HELIX 2656..2662
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2665..2670
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2676..2680
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2683..2686
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2689..2692
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2695..2700
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2703..2712
FT /evidence="ECO:0007829|PDB:6FB3"
FT HELIX 2715..2745
FT /evidence="ECO:0007829|PDB:6FB3"
FT HELIX 2755..2763
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2770..2776
FT /evidence="ECO:0007829|PDB:6FB3"
FT TURN 2778..2780
FT /evidence="ECO:0007829|PDB:6FB3"
FT HELIX 2782..2784
FT /evidence="ECO:0007829|PDB:6FB3"
FT HELIX 2788..2790
FT /evidence="ECO:0007829|PDB:6FB3"
FT STRAND 2791..2795
FT /evidence="ECO:0007829|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
