TEN2_RAT
ID TEN2_RAT Reviewed; 2774 AA.
AC Q9R1K2; Q9R1J9; Q9R1K0; Q9R1K1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 141.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 575-911 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 575-911 (ISOFORM 4),
RP NUCLEOTIDE SEQUENCE [MRNA] OF 575-911 (ISOFORM 1), AND DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley; TISSUE=Olfactory bulb;
RX PubMed=10419693; DOI=10.1006/dbio.1999.9310;
RA Otaki J.M., Firestein S.;
RT "Neurestin: putative transmembrane molecule implicated in neuronal
RT development.";
RL Dev. Biol. 212:165-181(1999).
RN [2]
RP FUNCTION AS ADGRL1 LIGAND, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21724987; DOI=10.1073/pnas.1019434108;
RA Silva J.P., Lelianova V.G., Ermolyuk Y.S., Vysokov N., Hitchen P.G.,
RA Berninghausen O., Rahman M.A., Zangrandi A., Fidalgo S., Tonevitsky A.G.,
RA Dell A., Volynski K.E., Ushkaryov Y.A.;
RT "Latrophilin 1 and its endogenous ligand Lasso/teneurin-2 form a high-
RT affinity transsynaptic receptor pair with signaling capabilities.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12113-12118(2011).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-155 AND SER-157, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Involved in neural development, regulating the establishment
CC of proper connectivity within the nervous system. Promotes the
CC formation of filopodia and enlarged growth cone in neuronal cells.
CC Mediates axon guidance and homophilic and heterophilic cell-cell
CC adhesion. May function as a cellular signal transducer (By similarity).
CC Acts as a ligand of the ADGRL1 receptor. {ECO:0000250,
CC ECO:0000269|PubMed:21724987}.
CC -!- FUNCTION: [Ten-2 intracellular domain]: Induces gene transcription
CC inhibition. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (Probable). Heterodimer with
CC either TENM1 or TENM3. May also form heterodimer with TENM4 (By
CC similarity). Interacts with ADGRL1 isoform 2. {ECO:0000250,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21724987};
CC Single-pass membrane protein {ECO:0000269|PubMed:21724987}. Endoplasmic
CC reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Synapse
CC {ECO:0000269|PubMed:21724987}. Cell projection, dendritic spine
CC {ECO:0000269|PubMed:21724987}. Cell projection, filopodium
CC {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Postsynaptic
CC cell membrane {ECO:0000269|PubMed:21724987}; Single-pass membrane
CC protein {ECO:0000269|PubMed:21724987}. Synapse, synaptosome
CC {ECO:0000269|PubMed:21724987}. Note=Colocalizes with ADGRL1 in synaptic
CC junctions.
CC -!- SUBCELLULAR LOCATION: [Ten-2 intracellular domain]: Nucleus, PML body
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Gamma;
CC IsoId=Q9R1K2-1; Sequence=Displayed;
CC Name=2; Synonyms=Alpha;
CC IsoId=Q9R1K2-2; Sequence=VSP_021396;
CC Name=3; Synonyms=Delta;
CC IsoId=Q9R1K2-3; Sequence=VSP_021395;
CC Name=4; Synonyms=Beta;
CC IsoId=Q9R1K2-4; Sequence=VSP_021397;
CC -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level).
CC {ECO:0000269|PubMed:21724987}.
CC -!- DEVELOPMENTAL STAGE: From E17-E18 embryos, a very strong signal
CC appeared and continued throughout the remaining prenatal days. The
CC signal was strongest in the cerebral cortex (including the cingulate
CC cortex, neocortex, and orbital and insular area), thalamus (anterior
CC and intermediate thalamus), and weak in posterior thalamus and
CC midbrain. {ECO:0000269|PubMed:10419693}.
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. {ECO:0000250}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF086607; AAD47383.1; -; mRNA.
DR EMBL; AF086608; AAD47384.1; -; mRNA.
DR EMBL; AF086609; AAD47385.1; -; mRNA.
DR EMBL; AF086610; AAD47386.1; -; mRNA.
DR RefSeq; NP_064473.1; NM_020088.1. [Q9R1K2-2]
DR SMR; Q9R1K2; -.
DR STRING; 10116.ENSRNOP00000011922; -.
DR GlyGen; Q9R1K2; 15 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q9R1K2; -.
DR PhosphoSitePlus; Q9R1K2; -.
DR SwissPalm; Q9R1K2; -.
DR PaxDb; Q9R1K2; -.
DR PRIDE; Q9R1K2; -.
DR GeneID; 117242; -.
DR KEGG; rno:117242; -.
DR UCSC; RGD:727907; rat. [Q9R1K2-1]
DR CTD; 57451; -.
DR RGD; 727907; Tenm2.
DR eggNOG; KOG1225; Eukaryota.
DR eggNOG; KOG4659; Eukaryota.
DR InParanoid; Q9R1K2; -.
DR OrthoDB; 7516at2759; -.
DR PhylomeDB; Q9R1K2; -.
DR PRO; PR:Q9R1K2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0098890; C:extrinsic component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050839; F:cell adhesion molecule binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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; IDA: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; ISS:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; TAS:RGD.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0048666; P:neuron development; IBA:GO_Central.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:0098942; P:retrograde trans-synaptic signaling by trans-synaptic protein complex; ISO:RGD.
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; 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; 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 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 Alternative splicing; Cell adhesion; Cell membrane; Cell projection;
KW Cleavage on pair of basic residues; Disulfide bond; EGF-like domain;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Membrane; Nucleus;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Repeat;
KW Repressor; Synapse; Synaptosome; Transcription; Transcription regulation;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..2774
FT /note="Teneurin-2"
FT /id="PRO_0000259503"
FT CHAIN 1..?
FT /note="Ten-2 intracellular domain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000421015"
FT CHAIN 529..2774
FT /note="Ten-2, soluble form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000421016"
FT TOPO_DOM 1..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..2774
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 1..375
FT /note="Teneurin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00694"
FT DOMAIN 575..603
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 605..634
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 636..668
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 669..701
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 702..735
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 738..766
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 769..797
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 808..841
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1272..1316
FT /note="NHL 1"
FT REPEAT 1342..1386
FT /note="NHL 2"
FT REPEAT 1401..1452
FT /note="NHL 3"
FT REPEAT 1474..1501
FT /note="NHL 4"
FT REPEAT 1530..1573
FT /note="NHL 5"
FT REPEAT 1583..1602
FT /note="YD 1"
FT REPEAT 1619..1639
FT /note="YD 2"
FT REPEAT 1682..1701
FT /note="YD 3"
FT REPEAT 1702..1724
FT /note="YD 4"
FT REPEAT 1895..1914
FT /note="YD 5"
FT REPEAT 1936..1954
FT /note="YD 6"
FT REPEAT 1955..1975
FT /note="YD 7"
FT REPEAT 1982..1999
FT /note="YD 8"
FT REPEAT 2000..2021
FT /note="YD 9"
FT REPEAT 2022..2039
FT /note="YD 10"
FT REPEAT 2042..2062
FT /note="YD 11"
FT REPEAT 2065..2085
FT /note="YD 12"
FT REPEAT 2093..2113
FT /note="YD 13"
FT REPEAT 2119..2136
FT /note="YD 14"
FT REPEAT 2137..2163
FT /note="YD 15"
FT REPEAT 2165..2178
FT /note="YD 16"
FT REPEAT 2179..2202
FT /note="YD 17"
FT REPEAT 2205..2225
FT /note="YD 18"
FT REPEAT 2226..2246
FT /note="YD 19"
FT REPEAT 2248..2268
FT /note="YD 20"
FT REPEAT 2280..2300
FT /note="YD 21"
FT REPEAT 2302..2322
FT /note="YD 22"
FT REPEAT 2348..2389
FT /note="YD 23"
FT REGION 111..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 528..529
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTS5"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHK6"
FT MOD_RES 155
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 925
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 948
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1712
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1773
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1807
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1892
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1993
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2648
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 576..586
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 580..591
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 593..602
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 611..622
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 624..633
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 640..651
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 645..656
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 658..667
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 672..683
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 677..688
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 690..699
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 710..723
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 725..734
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 739..749
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 743..754
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 756..765
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 770..780
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 774..785
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 787..796
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 810..820
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 814..829
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 831..840
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 605..669
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10419693"
FT /id="VSP_021395"
FT VAR_SEQ 737..807
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10419693"
FT /id="VSP_021397"
FT VAR_SEQ 799..807
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10419693"
FT /id="VSP_021396"
SQ SEQUENCE 2774 AA; 307474 MW; 7916D882A6C9E9A1 CRC64;
MDVKDRRHRS LTRGRCGKEC RYTSSSLDSE DCRVPTQKSY SSSETLKAYD HDSRMHYGNR
VTDLVHRESD EFSRQGANFT LAELGICEPS PHRSGYCSDM GILHQGYSLS TGSDADSDTE
GGMSPEHAIR LWGRGIKSRR SSGLSSRENS ALTLTDSDNE NKSDDDNGRP IPPTSSSSLL
PSAQLPSSHN PPPVSCQMPL LDSNTSHQIM DTNPDEEFSP NSYLLRACSG PQQASSSGPP
NHHSQSTLRP PLPPPHNHTL SHHHSSANSL NRNSLTNRRS QIHAPAPAPN DLATTPESVQ
LQDSWVLNSN VPLETRHFLF KTSSGSTPLF SSSSPGYPLT SGTVYTPPPR LLPRNTFSRK
AFKLKKPSKY CSWKCAALSA IAAALLLAIL LAYFIAMHLL GLNWQLQPAD GHTFNNGVRT
GLPGNDDVAT VPSGGKVPWS LKNSSIDSGE AEVGRRVTQE VPPGVFWRSQ IHISQPQFLK
FNISLGKDAL FGVYIRRGLP PSHAQYDFME RLDGKEKWSV VESPRERRSI QTLVQNEAVF
VQYLDVGLWH LAFYNDGKDK EMVSFNTVVL DSVQDCPRNC HGNGECVSGL CHCFPGFLGA
DCAKAACPVL CSGNGQYSKG TCQCYSGWKG AECDVPMNQC IDPSCGGHGS CIDGNCVCAA
GYKGEHCEEV DCLDPTCSSH GVCVNGECLC SPGWGGLNCE LARVQCPDQC SGHGTYLPDS
GLCNCDPNWM GPDCSVEVCS VDCGTHGVCI GGACRCEEGW TGAACDQRVC HPRCIEHGTC
KDGKCECREG WNGEHCTIGR QTAGTETDGC PDLCNGNGRC TLGQNSWQCV CQTGWRGPGC
NVAMETSCAD NKDNEGDGLV DCLDPDCCLQ SACQNSLLCR GSRDPLDIIQ QGQTDWPAVK
SFYDRIKLLA GKDSTHIIPG DNPFNSSLVS LIRGQVVTTD GTPLVGVNVS FVKYPKYGYT
ITRQDGTFDL IANGGSALTL HFERAPFMSR ERTVWPPWNS FYAMDTLVMK TEENSIPSCD
LSGFVRPDPI IISSPLSTFF SASPAANPIV PETQVLHEEI ELPGTNVKLR YLSSRTAGYK
SLLKITMTQS TVPLNLIRVH LMVAVEGHLF QKSFQASPNL AYTFIWDKTD AYGQRVYGLS
DAVVSVGFEY ETCPSLILWE KRTALLQGFE LDPSNLGGWS LDKHHTLNVK SGILLKGTGE
NQFLTQQPAI ITSIMGNGRR RSISCPSCNG LAEGNKLLAP VALAVGIDGS LFVGDFNYIR
RIFPSRNVTS ILELRNKEFK HSNSPGHKYY LAVDPVTGSL YVSDTNSRRI YRVKSLSGAK
DLAGNSEVVA GTGEQCLPFD EARCGDGGKA VDATLMSPRG IAVDKNGLMY FVDATMIRKV
DQNGIISTLL GSNDLTAVRP LSCDSSMDVA QVRLEWPTDL AVNPMDNSLY VLENNVILRI
TENHQVSIIA GRPMHCQVPG IDYSLSKLAI HSALESASAI AISHTGVLYI TETDEKKINR
LRQVTTNGEI CLLAGAASDC DCKNDVNCIC YSGDDAYATD AILNSPSSLA VAPDGTIYIA
DLGNIRIRAV SKNKPVLNAF NQYEAASPGE QELYVFNADG IHQYTVSLVT GEYLYNFTYS
ADNDVTELID NNGNSLKIRR DSSGMPRHLL MPDNQIITLT VGTNGGLKAV STQNLELGLM
TYDGNTGLLA TKSDETGWTT FYDYDHEGRL TNVTRPTGVV TSLHREMEKS ITVDIENSNR
DNDVTVITNL SSVEASYTVV QDQVRNSYQL CSNGTLRVMY ANGMGVSFHS EPHVLAGTLT
PTIGRCNISL PMENGLNSIE WRLRKEQIKG KVTIFGRKLR VHGRNLLSID YDRNIRTEKI
YDDHRKFTLR IIYDQVGRPF LWLPSSGLAA VNVSYFFNGR LAGLQRGAMS ERTDIDKQGR
IVSRMFADGK VWSYSYLDKS MVLLLQSQRQ YIFEYDSSDR LHAVTMPSVA RHSMSTHTSI
GYIRNIYNPP ESNASVIFDY SDDGRILKTS FLGTGRQVFY KYGKLSKLSE IVYDSTAVTF
GYDETTGVLK MVNLQSGGFS CTIRYRKVGP LVDKQIYRFS EEGMINARFD YTYHDNSFRI
ASIKPVISET PLPVDLYRYD EISGKVEHFG KFGVIYYDIN QIITTAVMTL SKHFDTHGRI
KEVQYEMFRS LMYWMTVQYD SMGRVIKREL KLGPYANTTK YTYDYDGDGQ LQSVAVNDRP
TWRYSYDLNG NLHLLNPGNS ARLMPLRYDL RDRITRLGDV QYKIDDDGYL CQRGSDIFEY
NSKGLLTRAY NKASGWSVQY RYDGVSRRAS YKTNLGHHLQ YFYSDLHHPT RITHVYNHSN
SEITSLYYDL QGHLFAMESS SGEEYYVASD NTGTPLAVFS INGLMIKQLQ YTAYGEIYYD
SNPDFQMVIG FHGGLYDPLT KLVHFTQRDY DVLAGRWTSP DYTMWRNVGK EPAPFNLYMF
KNNNPLSNEL DLKNYVTDVK SWLVMFGFQL SNIIPGFPRA KMYFVPPPYE LSESQASENG
QLITGVQQTT ERHNQAFLAL EGQVISKKLH AGIREKAGHW FATTTPIIGK GIMFAIKEGR
VTTGVSSIAS EDSRKVASVL NNAYYLDKMH YSIEGKDTHY FVKIGAADGD LVTLGTTIGR
KVLESGVNVT VSQPTLLVNG RTRRFTNIEF QYSTLLLSIR YGLTPDTLDE EKARVLDQAR
QRALGTAWAK EQQKARDGRE GSRLWTEGEK QQLLSTGRVQ GYEGYYVLPV EQYPELADSS
SNIQFLRQNE MGKR
