TNR6B_MOUSE
ID TNR6B_MOUSE Reviewed; 1810 AA.
AC Q8BKI2; Q80TK4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Trinucleotide repeat-containing gene 6B protein;
GN Name=Tnrc6b; Synonyms=Kiaa1093;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1240-1810 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1409; THR-1426; SER-1438 AND
RP THR-1441, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays a role in RNA-mediated gene silencing by both micro-
CC RNAs (miRNAs) and short interfering RNAs (siRNAs). Required for miRNA-
CC dependent translational repression and siRNA-dependent endonucleolytic
CC cleavage of complementary mRNAs by argonaute family proteins. As
CC scaffolding protein associates with argonaute proteins bound to
CC partially complementary mRNAs and simultaneously can recruit CCR4-NOT
CC and PAN deadenylase complexes. {ECO:0000250|UniProtKB:Q9UPQ9}.
CC -!- SUBUNIT: Interacts with AGO1, AGO2, AGO3 and AGO4. Interacts with
CC CNOT1; the interaction mediates the association with the CCR4-NOT
CC complex. Interacts with PAN3; the interaction mediates the association
CC with the PAN complex. Interacts with MOV10; the interaction is direct
CC and RNA-dependent. {ECO:0000250|UniProtKB:Q9UPQ9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q9UPQ9}.
CC Note=Mammalian P-bodies are also known as GW bodies (GWBs).
CC {ECO:0000250|UniProtKB:Q9UPQ9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BKI2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BKI2-2; Sequence=VSP_037294, VSP_037295, VSP_037296,
CC VSP_037297;
CC -!- SIMILARITY: Belongs to the GW182 family. {ECO:0000305}.
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DR EMBL; AC125540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC126682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK051922; BAC34813.1; -; mRNA.
DR EMBL; AK122440; BAC65722.1; -; mRNA.
DR CCDS; CCDS37146.1; -. [Q8BKI2-1]
DR RefSeq; NP_659061.2; NM_144812.2. [Q8BKI2-1]
DR AlphaFoldDB; Q8BKI2; -.
DR SMR; Q8BKI2; -.
DR BioGRID; 229484; 9.
DR DIP; DIP-48568N; -.
DR IntAct; Q8BKI2; 5.
DR MINT; Q8BKI2; -.
DR STRING; 10090.ENSMUSP00000064336; -.
DR iPTMnet; Q8BKI2; -.
DR PhosphoSitePlus; Q8BKI2; -.
DR EPD; Q8BKI2; -.
DR jPOST; Q8BKI2; -.
DR MaxQB; Q8BKI2; -.
DR PaxDb; Q8BKI2; -.
DR PeptideAtlas; Q8BKI2; -.
DR PRIDE; Q8BKI2; -.
DR ProteomicsDB; 260644; -. [Q8BKI2-1]
DR ProteomicsDB; 260645; -. [Q8BKI2-2]
DR Antibodypedia; 294; 105 antibodies from 21 providers.
DR DNASU; 213988; -.
DR Ensembl; ENSMUST00000067689; ENSMUSP00000064336; ENSMUSG00000047888. [Q8BKI2-1]
DR GeneID; 213988; -.
DR KEGG; mmu:213988; -.
DR UCSC; uc007wvt.1; mouse. [Q8BKI2-1]
DR UCSC; uc007wvu.2; mouse. [Q8BKI2-2]
DR CTD; 23112; -.
DR MGI; MGI:2443730; Tnrc6b.
DR VEuPathDB; HostDB:ENSMUSG00000047888; -.
DR eggNOG; ENOG502QQIH; Eukaryota.
DR GeneTree; ENSGT00940000155813; -.
DR HOGENOM; CLU_001298_1_0_1; -.
DR InParanoid; Q8BKI2; -.
DR OMA; NASWPPX; -.
DR PhylomeDB; Q8BKI2; -.
DR TreeFam; TF329702; -.
DR Reactome; R-MMU-426496; Post-transcriptional silencing by small RNAs.
DR BioGRID-ORCS; 213988; 3 hits in 57 CRISPR screens.
DR ChiTaRS; Tnrc6b; mouse.
DR PRO; PR:Q8BKI2; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8BKI2; protein.
DR Bgee; ENSMUSG00000047888; Expressed in animal zygote and 232 other tissues.
DR ExpressionAtlas; Q8BKI2; baseline and differential.
DR Genevisible; Q8BKI2; MM.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:gene silencing by RNA; ISO:MGI.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; IBA:GO_Central.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; ISS:UniProtKB.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISO:MGI.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISO:MGI.
DR CDD; cd12712; RRM_TNRC6B; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR019486; Argonaute_hook_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR032226; TNRC6_PABC-bd.
DR InterPro; IPR033500; TNRC6B.
DR InterPro; IPR034925; TNRC6B_RRM.
DR PANTHER; PTHR13020:SF32; PTHR13020:SF32; 1.
DR Pfam; PF10427; Ago_hook; 1.
DR Pfam; PF16608; TNRC6-PABC_bdg; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Phosphoprotein;
KW Reference proteome; RNA-binding; RNA-mediated gene silencing;
KW Translation regulation.
FT CHAIN 1..1810
FT /note="Trinucleotide repeat-containing gene 6B protein"
FT /id="PRO_0000373981"
FT DOMAIN 1625..1697
FT /note="RRM"
FT REGION 1..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..1028
FT /note="Interaction with argonaute proteins"
FT /evidence="ECO:0000250"
FT REGION 235..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1700
FT /note="Silencing domain; interaction with CNOT1 and PAN3"
FT /evidence="ECO:0000250"
FT REGION 1293..1329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1449..1467
FT /note="PABPC1-interacting motif-2 (PAM2)"
FT /evidence="ECO:0000250"
FT REGION 1568..1619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1706..1740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1786..1810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 33..75
FT /evidence="ECO:0000255"
FT COMPBIAS 30..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..885
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1587..1619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1717..1736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 913
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPQ9"
FT MOD_RES 1409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1426
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1441
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1793
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPQ9"
FT MOD_RES 1809
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPQ9"
FT VAR_SEQ 1..36
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_037294"
FT VAR_SEQ 37..38
FT /note="KQ -> MR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_037295"
FT VAR_SEQ 970..979
FT /note="VWSKSTPPAP -> GRYQLFSHRS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_037296"
FT VAR_SEQ 980..1810
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_037297"
FT CONFLICT 904
FT /note="D -> Y (in Ref. 2; BAC34813)"
FT /evidence="ECO:0000305"
FT CONFLICT 1576
FT /note="T -> P (in Ref. 3; BAC65722)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1810 AA; 191963 MW; 70F0A3A88CE7C7C5 CRC64;
MQTNEGEVEE ESSSQVEQED FVMEGHGKTP PPGEESKQEK EQEREEQLME DKKRKKEDKK
KKEATQKVTE QKTKVPEVTK PSLSQPTAAS PIGSSPSPPV NGGNNAKRVA VPNGQPPSAA
RYMPREVPPR FRCQQDHKVL LKRGQPPPPS CMLLGGGAGP PPCTAPGANP NNNAQVTGAL
LQSESGTAPE STLGGAAASN YANSTWGPGA SSNSGASPNP IHIWDKVIVD GSDMEEWPCI
ASKDTESSSE NTTDNNSASN PGSEKSSLPG STTSNKGKGS QCQAASSGNE CNLGVWKSDP
KAKSVQPPNS TSDSNNGLGN WRSTSGQDRI GPGSGFSNFN PNSNPSAWPA LVQEGTSRKG
ALETESSSSS AQVSTVGQAS REQQSKMENA GVNFVVSGRE QAQIHNTDGP KNGNTNSLNL
SSPNPMENKG MPFGMGLGNT SRSTDAPSQS TGDRKTGSVG SWGAARGPSG TDTVSGQSNS
GNNGNNGKDR EDSWKGASVP KPTGSKSDSW DNNNRSTGGS WNFGPQDNND NKWGEGNKMT
SGVSQGEWKQ PTGSDELKIG EWSGPNQPNS STGAWDNQKG HPLPENQGNA QAPCWGRSSS
SAGSEVGGQS TGSNHKAGSS DSHNSGRRSY RPTHPDCQAV LQTLLSRTDL DPRVLSNTGW
GQTQIKQDTV WDIEEVPRPE GKSDKGTEGW ESAATQTKNS GGWGDAPSQS NQMKSGWGEL
SASTEWKDPK STGGWNDYKN NNSSNWGGGR ADEKTPSSWN ESSCKDQGWG GGRQPNQGWT
SGKNGWGEEV DQVKNNNWES SANKPVSGWG EGGQNEIGTW GNGGNTNLAS KGGWEDCKRS
PAWNETGRQP NSWNKQHQQQ QQPPPPQPEA SGSWGGPPPP PQGNVRPSNS NWSSGPQPTT
PKDDEPSGWE EPSPQSISRK MDIDDGTSAW GDPNSYNYKN VNLWDKNSQG GPAPREPNLP
TPMTGKSASV WSKSTPPAPD NGTSAWGEPN ESSPGWGEMD DAGASTTGWG NTPANAPNAM
KPNSKSMQDG WGESDGPVTG ARHPSWEEED DGGVWNTAGS QGSTSSHNSA SWGQGGKKQM
KCSLKGGNND SWMNPLAKQF SNMGLLSQTE DNPSSKMDLS VDKKFDVDKR TMNLGDFNDI
MRKDRPGFRP PNSKDLGTTD SGPYFEKGGS HGLFGNSTAQ SRGLHTPVQP LSSSPGLRAQ
VPPQFISPQV SASMLKQFPN SGLNPGLFNV GPQLSPQQIA MLSQLPQIPQ FQLACQLLLQ
QQQQQQQLLQ NQRKISQAVR QQQEQQLARM VSALQQQQQQ QQQQQRQPSM KHSPSHPVGP
KPHLDNMVPN ALNVGLPDLP TKGPIPGYGS GFSSGGMDYG MVGGKEAGTE SRFKQWTSMM
EGLPSVATQE ATMHKNGAIV APGKTRGGSP YNQFDIIPGD TLGGHTGPAG DSWLPAKSPP
TNKIGSKSSN ASWPPEFQPG VPWKGIQNID PESDPYVTPG SVLGGTTTSP IVDTDHQLLR
DNTTGSNSSL NTSLPSPGAW PYSASDNSFT NVHSTSAKFP DYKSTWSPDP IGHNPTHLSN
KMWKNHISSR NTTPLTRPPP GLTNPKPASP WSSTAPRSVR GWGTQDSRIA SASTWSDGGS
VRPSYWLVLH NLTPQIDGST LRTICMQHGP LLTFHLNLTQ GTALIRYSTK QEAAKAQTAL
HMCVLGNTTI LAEFATEDEV SRFLAQAQPP TPAATPSAPA TGWQSLETSQ NQADPVGPAL
NLFGGSTGLG QWSSSAGGSS GADLAGTSLW GPPNYSSSLW GVPTVEDPHR MGSPAPLLPG
DLLGGGSDSI
