TEN1_CHICK
ID TEN1_CHICK Reviewed; 2705 AA.
AC Q9W6V6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Teneurin-1;
DE Short=Ten-1;
DE AltName: Full=Protein Odd Oz/ten-m homolog 1;
DE AltName: Full=Tenascin-M1;
DE Short=Ten-m1;
DE AltName: Full=Teneurin transmembrane protein 1;
DE Contains:
DE RecName: Full=Ten-1 intracellular domain;
DE Short=IDten-1;
DE Short=Ten-1 ICD;
DE Contains:
DE RecName: Full=Teneurin C-terminal-associated peptide;
DE Short=TCPA-1;
DE AltName: Full=Ten-1 extracellular domain;
DE Short=Ten-1 ECD;
GN Name=TENM1; Synonyms=ODZ1, TNM1;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10341219; DOI=10.1242/jcs.112.12.2019;
RA Minet A.D., Rubin B.P., Tucker R.P., Baumgartner S., Chiquet-Ehrismann R.;
RT "Teneurin-1, a vertebrate homologue of the Drosophila pair-rule gene ten-m,
RT is a neuronal protein with a novel type of heparin-binding domain.";
RL J. Cell Sci. 112:2019-2032(1999).
RN [2]
RP PROTEOLYTIC PROCESSING, FUNCTION OF TEN-1 ICD, INTERACTION WITH MBD1 AND
RP SORBS1, AND SUBCELLULAR LOCATION.
RX PubMed=15777793; DOI=10.1016/j.yexcr.2004.12.020;
RA Nunes S.M., Ferralli J., Choi K., Brown-Luedi M., Minet A.D.,
RA Chiquet-Ehrismann R.;
RT "The intracellular domain of teneurin-1 interacts with MBD1 and CAP/ponsin
RT resulting in subcellular codistribution and translocation to the nuclear
RT matrix.";
RL Exp. Cell Res. 305:122-132(2005).
RN [3]
RP PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP MUTAGENESIS OF 62-ARG--LYS-65.
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: Involved in neural development, regulating the establishment
CC of proper connectivity within the nervous system. May function as a
CC cellular signal transducer (By similarity). {ECO:0000250}.
CC -!- FUNCTION: [Teneurin C-terminal-associated peptide]: Plays a role in the
CC regulation of neuroplasticity in the limbic system. Mediates a rapid
CC reorganization of actin- and tubulin-based cytoskeleton elements with
CC an increase in dendritic arborization and spine density formation of
CC neurons in the hippocampus and amygdala. Induces BDNF transcription
CC inhibition in neurons. Activates the mitogen-activated protein (MAP)
CC kinase 2 (MEK2) and extracellular signal-regulated kinase (ERK) cascade
CC (By similarity). {ECO:0000250}.
CC -!- FUNCTION: [Ten-1 intracellular domain]: Induces gene transcription
CC activation. {ECO:0000269|PubMed:15777793}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Heterodimer with other teneurins
CC (By similarity). Ten-1 ICD interacts with SORBS1 (via third SH3
CC domain). Interacts with MBD1 isoform 2. {ECO:0000250,
CC ECO:0000269|PubMed:15777793}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15777793,
CC ECO:0000269|PubMed:18366734}; Single-pass membrane protein
CC {ECO:0000269|PubMed:15777793, ECO:0000269|PubMed:18366734}.
CC -!- SUBCELLULAR LOCATION: [Ten-1 intracellular domain]: Nucleus. Nucleus
CC speckle. Nucleus matrix. Cytoplasm, cytoskeleton. Note=Colocalizes with
CC SORBS1 in the nucleus and to the cell periphery. Colocalizes with MBD1
CC and PML in foci associated with the nuclear matrix.
CC -!- SUBCELLULAR LOCATION: [Teneurin C-terminal-associated peptide]: Nucleus
CC {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the neurons of the developing visual
CC system and in fetal brain. {ECO:0000269|PubMed:10341219}.
CC -!- DEVELOPMENTAL STAGE: Expressed in mitral cell, glomerular layer of the
CC olfactory bulb, hippocampus, posteromedial cortex piriformis, nucleus
CC rotundu, laminae 2 and 5 within the inner plexiform layer of the
CC retina, stratum griseum, nucleus laminaris and magnocellularis in the
CC hindbrain and Purkinje cells at embryonic day (E) 17 (at protein
CC level). At E14, it is concentrated in the retina, the optic tectum and
CC in specific nuclei in the dorsal diencephalon, it is concentrated in
CC the stratum griseum centrale. Expression is seen in diencephalon,
CC concentrated in the rotund nucleus and in the neighboring ovoid
CC nucleus. Similar expression patterns are seen at E17.
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: [Teneurin C-terminal-associated peptide]: Derives from the plasma
CC membrane form by proteolytic processing. Further proteolytic cleavage
CC may be generated (By similarity). {ECO:0000250}.
CC -!- PTM: [Ten-1 intracellular domain]: Derives from the plasma membrane
CC form by proteolytic cleavage and translocates to the nucleus.
CC {ECO:0000269|PubMed:15777793, ECO:0000269|PubMed:18366734}.
CC -!- MISCELLANEOUS: [Teneurin C-terminal-associated peptide]: Binds to the
CC plasma membrane and may be internalized by a receptor- and caveolae-
CC mediated endocytosis manner to reach cytosolic compartments in a
CC dynamin-dependent manner. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ238613; CAB43098.1; -; mRNA.
DR RefSeq; NP_990193.1; NM_204862.1.
DR SMR; Q9W6V6; -.
DR MINT; Q9W6V6; -.
DR STRING; 9031.ENSGALP00000038367; -.
DR PaxDb; Q9W6V6; -.
DR PRIDE; Q9W6V6; -.
DR GeneID; 395668; -.
DR KEGG; gga:395668; -.
DR CTD; 10178; -.
DR VEuPathDB; HostDB:geneid_395668; -.
DR eggNOG; KOG4659; Eukaryota.
DR InParanoid; Q9W6V6; -.
DR PhylomeDB; Q9W6V6; -.
DR PRO; PR:Q9W6V6; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0048666; P:neuron development; IBA:GO_Central.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IDA:UniProtKB.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0006359; P:regulation of transcription by RNA polymerase III; ISS: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; IPR000742; EGF-like_dom.
DR InterPro; IPR009471; Ten_N.
DR InterPro; IPR028916; Tox-GHH_dom.
DR InterPro; IPR006530; YD.
DR Pfam; PF06484; Ten_N; 2.
DR Pfam; PF15636; Tox-GHH; 1.
DR SMART; SM00181; EGF; 8.
DR SUPFAM; SSF49464; SSF49464; 1.
DR TIGRFAMs; TIGR01643; YD_repeat_2x; 2.
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 1: Evidence at protein level;
KW Cell membrane; Cleavage on pair of basic residues; Cytoplasm; Cytoskeleton;
KW Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Neuropeptide;
KW Nucleus; Reference proteome; Repeat; Repressor; Stress response;
KW Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..2705
FT /note="Teneurin-1"
FT /id="PRO_0000259500"
FT CHAIN 1..?
FT /note="Ten-1 intracellular domain"
FT /id="PRO_0000421009"
FT CHAIN 2576..2705
FT /note="Teneurin C-terminal-associated peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000421010"
FT TOPO_DOM 1..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..2705
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 1..299
FT /note="Teneurin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00694"
FT DOMAIN 509..540
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 541..572
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 573..605
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 606..638
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 639..672
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 673..702
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 703..734
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 735..769
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1167..1192
FT /note="NHL 1"
FT REPEAT 1202..1246
FT /note="NHL 2"
FT REPEAT 1272..1316
FT /note="NHL 3"
FT REPEAT 1331..1382
FT /note="NHL 4"
FT REPEAT 1461..1504
FT /note="NHL 5"
FT REPEAT 1514..1533
FT /note="YD 1"
FT REPEAT 1550..1570
FT /note="YD 2"
FT REPEAT 1588..1612
FT /note="YD 3"
FT REPEAT 1613..1634
FT /note="YD 4"
FT REPEAT 1635..1655
FT /note="YD 5"
FT REPEAT 1825..1844
FT /note="YD 6"
FT REPEAT 1845..1865
FT /note="YD 7"
FT REPEAT 1866..1884
FT /note="YD 8"
FT REPEAT 1885..1905
FT /note="YD 9"
FT REPEAT 1913..1929
FT /note="YD 10"
FT REPEAT 1930..1949
FT /note="YD 11"
FT REPEAT 1950..1969
FT /note="YD 12"
FT REPEAT 1972..1992
FT /note="YD 13"
FT REPEAT 1995..2015
FT /note="YD 14"
FT REPEAT 2065..2085
FT /note="YD 15"
FT REPEAT 2093..2113
FT /note="YD 16"
FT REPEAT 2133..2153
FT /note="YD 17"
FT REPEAT 2154..2174
FT /note="YD 18"
FT REPEAT 2176..2196
FT /note="YD 19"
FT REPEAT 2208..2228
FT /note="YD 20"
FT REPEAT 2230..2250
FT /note="YD 21"
FT REPEAT 2276..2293
FT /note="YD 22"
FT REPEAT 2294..2317
FT /note="YD 23"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 62..65
FT /note="Nuclear localization signal (NLS)"
FT MOTIF 271..278
FT /note="Required for interaction with SORBS1 (Ten-1 ICD
FT form)"
FT COMPBIAS 21..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..187
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 2575..2576
FT /note="Cleavage"
FT /evidence="ECO:0000305"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 878
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1057
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1643
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1737
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1761
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1822
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 513..523
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 517..528
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 530..539
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 548..559
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 561..570
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 577..588
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 582..593
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 595..604
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 609..620
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 614..625
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 627..636
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 647..660
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 662..671
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 676..686
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 680..691
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 693..702
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 707..717
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 711..722
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 724..733
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 738..748
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 742..757
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 759..768
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT MUTAGEN 62..65
FT /note="RKRK->AAAA: Inhibits translocation to the nucleus
FT (Ten-1 ICD form)."
FT /evidence="ECO:0000269|PubMed:18366734"
SQ SEQUENCE 2705 AA; 302388 MW; 230F03D1999037D2 CRC64;
MEQMDCKPYQ PLSKVKHEVD LTYTSSSDES EDGRKQRQSY DSRETLNEYS QELRLNYNSQ
SRKRKNTDQS TQDMEFCETP HILCSGYQTD LHGVSEHSYP LEVGSDVDTE TEGGASPDHA
LRMWMRGMKS EHSSCLSSRA NSALSLTDTD HERKSDGEND MPGSPHNQFT FRPLPPPPPP
PHACTCTRKP PPAADSLQRR SMTTRSQPSP AAPTPPTSTQ DSVHLHNSWV LNSNIPLETR
HFLFKHGSGS SAIFSAASQN YPLTSNTVYS PPPRPLPRNT FSRPAFTFSK PYRCCNWKCT
ALSATAITVT LALLLAYVIA VHLFGLTWQL QPVEGQLYEN GVSKGNKGAE STDTTYSPIG
GKVSDKTEKK VFQKGRAIDT GEVEIGAQVM QTIPPGLFWR FQITIHHPVY LKFNISLAKD
SLLGIYGRRN IPPTHTQFDF VKLMDGKQLI KQEPKNSEEP QQAPRNLILT SLQETGFIEY
MDQGAWHMAF YNDGKKVEQV FVLTTAIEVL DDCSTNCNGN GECISGHCHC FPGFLGPDCA
KDSCPVLCSG NGEYEKGHCV CRNGWKGPEC DVPEEQCIDP TCFGHGTCIM GVCICVPGYK
GEICEEEDCL DPMCSGHGVC VQGECHCSAG WGGVNCETSL PICQEHCSGH GTFLLDVGLC
SCEPQWTGSD CSTELCTLDC GSHGVCSRGI CQCEEGWVGP TCEERTCHSH CAEHGQCKDG
KCECSPGWEG DHCTIDGCPG LCYGNGRCTL DQNGWHCVCQ VGWSGSGCNV VMEMACGDNL
DNDGDGLTDC VDPDCCQQNN CYASPLCQGS PDPLDLIQHS QPPFSQHPPR LFYDRIRFLI
GKESTHVIPG DISFESRRAS VIRGQVVAID GTPLVGVNVS FLHHDEYGYT ISRQDGSFDL
VAVGGISVTL VFDRSPFISE KRTLWLSWNR FVIVDKVVMQ RAESDIPSCD VSSFISPNPI
VLPSPLTAFG GSCPERGTVI PELQVVQEEI PIPSSFVKLS YLSSRTPGYK TLLRVILTHT
TIPSGMTKVH LIIAVEGRLL QKWFPAAANL VYTFAWNKTD IYGQKVSGLA EAMVSVGYEY
ETCPDFILWE KRTVILQGFE MDASNLGGWS INKHHVLNPQ SGIVHKGNGE NMFISQQPPV
ISTMMGNGHQ RSVSCSNCNG LALNSKLFAP VALTSGPDGS VYIGDFNFVR RIFPSGNSIG
ILELRNRDTR HSTSPAHKYY LAVDPVSESL YLSDTNTRRV YKAKSLIETK DLAKNVDVVA
GTGDQCLPFD QSHCGDGGKA SEASLNSPRG ITIDKHGFIY FVDGTMIRKI DENGMITTII
GSNGLTSTQP LSCDSGMDIT QVRLEWPTDL TVNPLDNSLY VLDNNIVLQI SESRRVRIIA
GRPIHCQVPG IDHFIVSKVA IHSTLESARA IAVSHSGIPY IRETDERKIN RIQQVTTNGE
ISIIAGAPSD CDCKIDPNCD CFSGDGGYAK DAKLKAPSSL AVSPDDTLYV ADLGNIRIRA
VSRNKAHLSD TNMYEIASPA DQELYQFTIN GTHLHTLNLI TRDYIYNFTY SGEGDVATIT
SSNGNSVHIR RDTSGLPLWV VVPGGQVYWL TISSNGVLKR VYAQGYNLAL MTYPGNTGLL
ATKSDENGWT TVYEYDSDGH LTNATFPTGE VSSFHSDVEK LTRVELDTSN RENMVTATNF
SATSTIYTLK QDNTQNIYRV SPDGSLRVTF ASGMEITLNT EPHILAGVVS PTLGKCNISL
PGEHNSNLIE WRQRREQTKG NISTFERRLR AHNRNLLSID FDHVTRTGKI YDDHRKFTLR
IMYDQTGRPV LWSPISKYNE VNITYSHSGL VTYIQRGTWT EKMEYDPSGN IISRTWADGK
IWSYTYLEKS VMLLLHSQRR YIFEYDQSDY LLSVTMPSMV RHALQTMLSV GYYRNIYTPP
DSGAAFIQDV TRDGRLLQTL YPGTGRRVLY KYSKQSRLSE ILYDTTQVTF TYEESSGVIK
TIHLMHDGFI CTIRYRQTGP LIGRQIFRFS EEGLVNARFD YSYNNFRVTS MQAMINETPL
PIDLYRYVDV SGRTEQFGKF SVINYDLNQV ITTTVMKHTK IFSANGQVIE VQYEILKSIA
YWMTIQYDNM GRMVICDIRV GVDANITRYF YEYDRDGQLQ TVSVNDKTQW RYSYDLNGNI
NLLSHGNSAR LTPLRYDLRD RITRLGEIQY KMDEDGFLRQ RGNEIFEYNS NGLLNKAYNK
VSGWTVQYCY DGLGRRVASK SSLGQHLQFF YADLSNPIRV THLYNHSSSE ITSLYYDLQG
HLIAMELSSG EEYYVACDNT GTPLAVFSSR GQVIKEILYT PYGEIYQDTN PDFQVVIGFH
GGLYDSLTKL VHLGQRDYDV IAGRWTTPNH HIWKHLNAVP QPFNLYSFEN NYPVGRIQDV
AKYTTDIGSW LELFGFQLHN VLPGFPKPEI EALETTYELL QLQTKTQEWD PGKTILGIQC
ELQKQLRNFI SLDQLPMTPR YSDGKCYEGV KQPRFAAIPS VFGKGIKFAI KDGIVTADII
GVANEDSRRI AAILNNAHYL ENLHFTIEGR DTHYFIKLGS LEEDLSLIGN TGGRRILENG
VNVTVSQMTS VINGRTRRFA DIQLQHGALC FNVRYGTTVE EEKNHVLEVA RQRAVAQAWT
KEQRRLQEGE EGIRAWTDGE KQQLLNTGRV QGYDGYFVLS VEQYLELSDS ANNIHFMRQS
EIGRR
