TEN4_DANRE
ID TEN4_DANRE Reviewed; 2824 AA.
AC Q9W7R3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Teneurin-4;
DE Short=Ten-4;
DE AltName: Full=Protein Odd Oz/ten-m homolog 4;
DE AltName: Full=Tenascin-M4;
DE Short=Ten-m4;
DE AltName: Full=Teneurin transmembrane protein 4;
GN Name=tenm4; Synonyms=odz4, tnm4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=10495292; DOI=10.1016/s0925-4773(99)00155-0;
RA Mieda M., Kikuchi Y., Hirate Y., Aoki M., Okamoto H.;
RT "Compartmentalized expression of zebrafish ten-m3 and ten-m4, homologues of
RT the Drosophila tenm /odd Oz gene, in the central nervous system.";
RL Mech. Dev. 87:223-227(1999).
RN [2]
RP DISRUPTION PHENOTYPE.
RX PubMed=26188006; DOI=10.1093/hmg/ddv281;
RA Hor H., Francescatto L., Bartesaghi L., Ortega-Cubero S., Kousi M.,
RA Lorenzo-Betancor O., Jimenez-Jimenez F.J., Gironell A., Clarimon J.,
RA Drechsel O., Agundez J.A., Kenzelmann Broz D., Chiquet-Ehrismann R.,
RA Lleo A., Coria F., Garcia-Martin E., Alonso-Navarro H., Marti M.J.,
RA Kulisevsky J., Hor C.N., Ossowski S., Chrast R., Katsanis N., Pastor P.,
RA Estivill X.;
RT "Missense mutations in TENM4, a regulator of axon guidance and central
RT myelination, cause essential tremor.";
RL Hum. Mol. Genet. 24:5677-5686(2015).
CC -!- FUNCTION: Involved in neural development, regulating the establishment
CC of proper connectivity within the nervous system. May play a role in
CC the establishment of the anterior-posterior axis during gastrulation.
CC Regulates the differentiation of oligodendrocytes and myelination of
CC axons. May function as a cellular signal transducer (By similarity).
CC {ECO:0000250|UniProtKB:Q3UHK6}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (Probable). May also form
CC heterodimer with either TENM1 or TENM2 or TENM3 (By similarity).
CC {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6N022};
CC Single-pass membrane protein {ECO:0000255}. Cell projection
CC {ECO:0000250|UniProtKB:Q3UHK6}. Nucleus {ECO:0000250|UniProtKB:Q3UHK6}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q3UHK6}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in the brain.
CC {ECO:0000269|PubMed:10495292}.
CC -!- DEVELOPMENTAL STAGE: During gastrulation, expressed throughout the
CC embryo very faintly. Expressed along the anterior margin of the neural
CC plate. Later, this marginal expression extends caudally, and eventually
CC restricted only to the caudal neural plate. At 14 hours post-
CC fertilization, it is expressed in the brain. Expressed in the
CC rhombomere 5 (r5) and more strongly in r6. Expressed in the rostral
CC diencephalon with weak expression in the optic vesicles, and a region
CC covering the mesencephalon and the midbrain/hindbrain boundary (MHB) in
CC a gradient manner with stronger expression at its posterior end. At 17
CC hpf, expressed weakly in the dorsal edge of the most caudal part of the
CC neural tube. Faint expression is detected in several neurons located at
CC ventral and dorsal parts of the caudal spinal cord.
CC {ECO:0000269|PubMed:10495292}.
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 -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the gene in embryos
CC resulted in a modest reduction of myelin in the brain and an increase
CC in the number of small-diameter neuronal axons with aberrant branching
CC along the notochord. {ECO:0000269|PubMed:26188006}.
CC -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC {ECO:0000305}.
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DR EMBL; AB026980; BAA81893.1; -; mRNA.
DR SMR; Q9W7R3; -.
DR STRING; 7955.ENSDARP00000016395; -.
DR PaxDb; Q9W7R3; -.
DR PRIDE; Q9W7R3; -.
DR ZFIN; ZDB-GENE-990714-20; tenm4.
DR eggNOG; KOG4659; Eukaryota.
DR InParanoid; Q9W7R3; -.
DR PhylomeDB; Q9W7R3; -.
DR PRO; PR:Q9W7R3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS: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:0007411; P:axon guidance; IMP:ZFIN.
DR GO; GO:0032289; P:central nervous system myelin formation; ISS:UniProtKB.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
DR GO; GO:0048666; P:neuron development; ISS:UniProtKB.
DR GO; GO:2000543; P:positive regulation of gastrulation; ISS:UniProtKB.
DR GO; GO:0031643; P:positive regulation of myelination; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0031641; P:regulation of myelination; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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; IPR011041; Quinoprot_gluc/sorb_DH.
DR InterPro; IPR022385; Rhs_assc_core.
DR InterPro; IPR031325; RHS_repeat.
DR InterPro; IPR027691; Ten-3/4.
DR InterPro; IPR009471; Ten_N.
DR InterPro; IPR028916; Tox-GHH_dom.
DR InterPro; IPR006530; YD.
DR PANTHER; PTHR11219:SF65; PTHR11219:SF65; 1.
DR Pfam; PF05593; RHS_repeat; 1.
DR Pfam; PF06484; Ten_N; 1.
DR Pfam; PF15636; Tox-GHH; 1.
DR SMART; SM00181; EGF; 8.
DR SUPFAM; SSF49464; SSF49464; 1.
DR SUPFAM; SSF50952; SSF50952; 1.
DR TIGRFAMs; TIGR03696; Rhs_assc_core; 1.
DR TIGRFAMs; TIGR01643; YD_repeat_2x; 3.
DR PROSITE; PS00022; EGF_1; 8.
DR PROSITE; PS01186; EGF_2; 6.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS51361; TENEURIN_N; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Cytoplasm; Developmental protein;
KW Differentiation; Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW Nucleus; Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..2824
FT /note="Teneurin-4"
FT /id="PRO_0000259510"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1..412
FT /note="Teneurin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00694"
FT DOMAIN 633..664
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 665..695
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 697..729
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 730..761
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 763..796
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 797..828
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 829..858
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 859..893
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1278..1321
FT /note="NHL 1"
FT REPEAT 1326..1363
FT /note="NHL 2"
FT REPEAT 1389..1433
FT /note="NHL 3"
FT REPEAT 1448..1499
FT /note="NHL 4"
FT REPEAT 1522..1552
FT /note="NHL 5"
FT REPEAT 1578..1621
FT /note="NHL 6"
FT REPEAT 1631..1650
FT /note="YD 1"
FT REPEAT 1667..1687
FT /note="YD 2"
FT REPEAT 1730..1749
FT /note="YD 3"
FT REPEAT 1750..1772
FT /note="YD 4"
FT REPEAT 1942..1961
FT /note="YD 5"
FT REPEAT 1983..2001
FT /note="YD 6"
FT REPEAT 2002..2022
FT /note="YD 7"
FT REPEAT 2029..2046
FT /note="YD 8"
FT REPEAT 2047..2068
FT /note="YD 9"
FT REPEAT 2069..2086
FT /note="YD 10"
FT REPEAT 2089..2109
FT /note="YD 11"
FT REPEAT 2112..2132
FT /note="YD 12"
FT REPEAT 2140..2159
FT /note="YD 13"
FT REPEAT 2165..2182
FT /note="YD 14"
FT REPEAT 2183..2209
FT /note="YD 15"
FT REPEAT 2211..2224
FT /note="YD 16"
FT REPEAT 2225..2248
FT /note="YD 17"
FT REPEAT 2251..2271
FT /note="YD 18"
FT REPEAT 2272..2292
FT /note="YD 19"
FT REPEAT 2294..2314
FT /note="YD 20"
FT REPEAT 2326..2346
FT /note="YD 21"
FT REPEAT 2348..2368
FT /note="YD 22"
FT REPEAT 2394..2435
FT /note="YD 23"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 789
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1002
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1647
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1664
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1760
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1796
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1854
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1939
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2040
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2701
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 637..647
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 641..652
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 654..663
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 672..683
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 685..694
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 701..712
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 706..717
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 719..728
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 733..744
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 738..749
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 751..760
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 771..784
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 786..795
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 800..810
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 804..815
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 817..826
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 831..841
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 835..846
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 848..857
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 862..872
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 866..881
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 883..892
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2824 AA; 313506 MW; 27007746DD34E356 CRC64;
MEVKERRPYR SLTSRRDTER RYTSSSADSE DGKINPKSYS SSETLKAFDQ DSRLAYGSRV
KDLVHHEADE FSRQGPDFSL RDMAFGDPVP PHMGAYRTEM GLPHRDYSVS VASDADTETD
GIMSPEHAVR LWGRSNTKSG RSSCLFSRAN SNLTLTDTEH ENTENGPPLH CSSASSSPVD
SPYPPPSHAA NQSQGRLLGN SGAQAGRDSE SEDEFGPNSF LVKTGSGNVC TPAAATANEG
SFQNHSRLRT PPLPLFHSHS PSQHHTASIG SLSRSNYTQR SNPSPAPTDS SAPNEGPTSA
QDSSSAQDNW LLNSNVPLET RNIAKQTFLE TLQDNFIEMD ILATARRDGA YTDGHFLFKP
GGTSPLYCTT SPGYPLTSST VYSPPPRPLP RNTFSRPAFS LKKPYKHCNW KCAALSAILI
SVTLVFLLAY FIAMHLFGLN WHLQPVQRQI YQLTEDNTSG LHLPTDLGLP PLGNTGLEFP
DRGSRDDGKL DGFFPEDSFI DMGEIDVGRK VAQLIPPGIF WRSQVFIDHP MYLKFNVSLS
KDALVGIYGR RGLPPSHTQF DFVELLDGRR LLSQGLPGLD GPPFPAQQRS LVPITSHDTG
CIQYMDSGIW HLAVYNDGKE TEQVSFLTTA IDSIDDCPSN CFGNGDCVSG NCHCFPGFRG
PDCSRASCPV LCSGNGQYLK GRCMCHSGWK GSECDVPTNQ CIDITCSGHG TCIVGTCICN
PSYKGENCEE VDCLDPTCSG RGVCVRGECH CFVGWGGPGC ESPRASCMEQ CSGHGSFLAD
TNTCNCDHNW TGHDCSTELC AADCGGHGIC VAGSCRCDEG WMGTGCEQRA CHPRCSEHGT
CKDGKCECSP GWNGEHCTIE GCPGLCNGNG RCTLGNNGWY CVCQLGWRGA GCDTSMETAC
SDGKDNDGDG LTDCMDPDCC LQASCHTTSL CVGSPDPLDI IQETQISSSL STLQSFYQRI
HFLVGRDSTH VIPDVNPFDG IHACVIRGQV VTSDGTPLVG VNISFINKPA YGYTITRQDG
SFDLVSNGGV AIGLRFERAP FITQEHTLWL PWGRFFVMDT IVMRHEVNDI PSCDLSSFTR
PMPIVLPAPL TAFAGTCPER GIVVPEIQTL QEEVRIPGTD MRLGYLSSRT SGYKSLLRIT
LTHSTIPFSL MKVHLMVAVE GRLFRKWFSA APNLSYDFVW DKTDVYSQKV YGLSEAFVSV
GFEYESCPDL ILWEKRTAVL QGYETTASNL GGWSVDKHHA LNIQSGILHK GNGENIFISQ
QPPVIGSIMG NGRRRSISCP SCNGLADGNK LLAPVALACG SDGSLYVGDF NYVRRIFTTG
NVTSVLELSN SPAHKYYLAT SPVSGWLYLS DTSSRKVFKV KSLYAVKDVA KNLELVAGTG
DQCLPYDETR CGDGGKAVEA TLTNPRGITV DKYGVIFFVD GTMIRRIDQN GIISTLLGFN
DLTSARPLSC DSVMDISQVR LEWPTDLAVS PMDNSLYVLD NNVVLQISEN HQVRIVAGRP
MHCQVPGLDH FLVSKIAIHA TLESANALAV SHNGLLYIAE SDEKKINRVR QVSTNGEISL
LAGAPSGCDC KNDANCDCYS GDDGYAKDAK LNAPSSLAVS PDGELFIADL GNIRIRYVRR
NKAFLNPLNM YEISSPIDDE LYLFDVNASH VFTQSLTTGD YLYNFTYSGE GDLSSITDKN
KNRVSIRRDS TGLPLWLMGP DGQTFWFTMG TNNALKSVAA QGQEIAVMTY HGSSGLLATK
SNEDGWSTFY EYDNYGRLTN VTYPTGRVSS YRTDSDSTVR VQTEGSNKED ITVTTNLSAS
GTFYTLMQDQ VKNSYYIGLD GSLRLVLANG MEVSLHTEPH LLSGTVNPTI SKRNVTLPID
NGLNLVEWRQ RKEQARGQVT VYGRRLRVHN RNLLSMDFDR VTRTEKVYDD HRKFTLRIHY
DHAGRPTLWA PSSRLNGVNV TYSPGGHIAG IQRGTMSVRM EYDQNGRITS KIFADGKSWS
YTYLEKSMVL LLYSQRQYIF EFDKNDRLSS VTMPNVARQT LETTRSIGYY RNTYRPPEGN
ATVLQDYSED GLLLQTIHQG TGRRVIYKYG KLSRLLEILY DTTRIAFSYD ESAGMLKTVG
LQSEGFACTI RYRQIGPLID RQIFRFSEEG MVNARFDYNY DNSFRVTSMQ AVINETPLPI
DLYRYDDVSG KTEQFGKFGV IYYDINQIIT TAVMTHTKHF DAYGRVKEVQ YEIFRSLMYW
MMVQFDNMGR VVAKELKVGP YANTTRYAYE YDADGQLQVV SINDKPLWRY SYDLNGNLHL
LSPGNSARLT PLRYDIRDRI TRLGDVQYRL DEDGFLRQRG NDFFEYNSAG LLVKTYNKVN
GWTIKYRYDG LGRRVSSRST QGHHLQFFYA DLSSPTRVTH MYNHSSSEIT SLYYDLQGHL
FAMELSSGDE FYVACDNIGT PLAVFSGAGL MIKQILHTAF GEVYLDSNPS FQLVIGYQGG
LYEPLTKLVH MGRRDYDVLA GRWTTPDHDI RKRLNSDNIV PFNLYMFKNN NPLSNSQETK
CYMTDVNSWL VTFGFQLYNV IPGYRKPVTD AMEPSYELVH TQIKTQEWDS TKSVLGVQCE
VQRQLKSFVR LERFGQIYSA SDSGCPPTPL HTLFATGTSL FGKGVKVAIR EGRVEADIIS
LANEDGRRIA AVLDKASYLQ DLHFTIAGLD THYFVKSGLV EGDLSLLGMT VGQRTLETGV
NVTVSQVNMV LGGRSRRITD IQMQYGTLSL NVRYGSSVDE EKVRVLELAR QRAVATAWAH
ERHRLRQGEE GSRAWTDGER QQLLSSGRVQ GYEGFYIVSV DQFPELTDNI NNVHFWRQTE
MGRR
