TENR_HUMAN
ID TENR_HUMAN Reviewed; 1358 AA.
AC Q92752; C9J563; Q15568; Q5R3G0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Tenascin-R;
DE Short=TN-R;
DE AltName: Full=Janusin;
DE AltName: Full=Restrictin;
DE Flags: Precursor;
GN Name=TNR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP VARIANT VAL-17.
RC TISSUE=Brain;
RX PubMed=8626505; DOI=10.1074/jbc.271.14.8157;
RA Carnemolla B., Leprini A., Borsi L., Querze G., Urbini S., Zardi L.;
RT "Human tenascin-R: complete primary structure, pre-mRNA alternative
RT splicing and gene localization on chromosome 1q23-q24.";
RL J. Biol. Chem. 271:8157-8160(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-17.
RC TISSUE=Brain;
RA Williams H., Schachner M., Wang B., Goodfellow P., Kenwrick S.;
RT "Isolation of the gene for neural cell adhesion molecule tenascin-R and
RT fine mapping relative to loci in 1q25-31.";
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-36 AND THR-37, AND STRUCTURE OF
RP CARBOHYDRATES.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G.,
RA Larson G.;
RT "Enrichment of glycopeptides for glycan structure and attachment site
RT identification.";
RL Nat. Methods 6:809-811(2009).
CC -!- FUNCTION: Neural extracellular matrix (ECM) protein involved in
CC interactions with different cells and matrix components. These
CC interactions can influence cellular behavior by either evoking a stable
CC adhesion and differentiation, or repulsion and inhibition of neurite
CC growth. Binding to cell surface gangliosides inhibits RGD-dependent
CC integrin-mediated cell adhesion and results in an inhibition of
CC PTK2/FAK1 (FAK) phosphorylation and cell detachment. Binding to
CC membrane surface sulfatides results in a oligodendrocyte adhesion and
CC differentiation. Interaction with CNTN1 induces a repulsion of neurons
CC and an inhibition of neurite outgrowth. Interacts with SCN2B may play a
CC crucial role in clustering and regulation of activity of sodium
CC channels at nodes of Ranvier. TNR-linked chondroitin sulfate
CC glycosaminoglycans are involved in the interaction with FN1 and mediate
CC inhibition of cell adhesion and neurite outgrowth. The highly regulated
CC addition of sulfated carbohydrate structure may modulate the adhesive
CC properties of TNR over the course of development and during synapse
CC maintenance (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms oligomers. Interacts with CNTN1, TNC, and FN1. Interacts
CC with BCAN and ACAN in a calcium-dependent manner. Interacts with SCN2B,
CC PTPRZ1, and CSPG3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92752-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92752-2; Sequence=VSP_012993;
CC -!- TISSUE SPECIFICITY: Brain specific. {ECO:0000269|PubMed:8626505}.
CC -!- DOMAIN: The EGF-like domains mediate interaction with CNTN1. The
CC fibronectin type-III domains 3-5 mediate interaction with BCAN. The
CC fibronectin type-III domains 1-2 and 7-9 mediate interaction with SCN2B
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Contains N-linked oligosaccharides, O-linked sialylated structures
CC and O-linked chondroitin sulfate glycosaminoglycans. Contains N-linked
CC oligosaccharides with a sulfated carbohydrate structure (By
CC similarity). O-glycosylated on Thr-36 or Thr-37 with a core 1 or
CC possibly core 8 glycan. {ECO:0000250, ECO:0000269|PubMed:19838169}.
CC -!- SIMILARITY: Belongs to the tenascin family. {ECO:0000305}.
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DR EMBL; Z67996; CAA91947.1; -; mRNA.
DR EMBL; X98085; CAA66709.1; -; mRNA.
DR EMBL; AL021919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL023285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z94055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z94057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS1318.1; -. [Q92752-1]
DR RefSeq; NP_003276.3; NM_003285.2. [Q92752-1]
DR RefSeq; XP_016857707.1; XM_017002218.1. [Q92752-1]
DR RefSeq; XP_016857708.1; XM_017002219.1. [Q92752-1]
DR AlphaFoldDB; Q92752; -.
DR SMR; Q92752; -.
DR BioGRID; 112997; 13.
DR ComplexPortal; CPX-1019; Tenascin-R complex.
DR IntAct; Q92752; 4.
DR STRING; 9606.ENSP00000356646; -.
DR GlyGen; Q92752; 14 sites.
DR iPTMnet; Q92752; -.
DR PhosphoSitePlus; Q92752; -.
DR SwissPalm; Q92752; -.
DR BioMuta; TNR; -.
DR DMDM; 311033534; -.
DR jPOST; Q92752; -.
DR MassIVE; Q92752; -.
DR PaxDb; Q92752; -.
DR PeptideAtlas; Q92752; -.
DR PRIDE; Q92752; -.
DR ProteomicsDB; 75442; -. [Q92752-1]
DR ProteomicsDB; 75443; -. [Q92752-2]
DR Antibodypedia; 20571; 141 antibodies from 25 providers.
DR DNASU; 7143; -.
DR Ensembl; ENST00000263525.6; ENSP00000263525.2; ENSG00000116147.17. [Q92752-1]
DR Ensembl; ENST00000367674.7; ENSP00000356646.1; ENSG00000116147.17. [Q92752-1]
DR GeneID; 7143; -.
DR KEGG; hsa:7143; -.
DR MANE-Select; ENST00000367674.7; ENSP00000356646.1; NM_003285.3; NP_003276.3.
DR UCSC; uc009wwu.2; human. [Q92752-1]
DR CTD; 7143; -.
DR DisGeNET; 7143; -.
DR GeneCards; TNR; -.
DR HGNC; HGNC:11953; TNR.
DR HPA; ENSG00000116147; Group enriched (brain, retina).
DR MIM; 601995; gene.
DR neXtProt; NX_Q92752; -.
DR OpenTargets; ENSG00000116147; -.
DR PharmGKB; PA36642; -.
DR VEuPathDB; HostDB:ENSG00000116147; -.
DR eggNOG; KOG1225; Eukaryota.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000157761; -.
DR HOGENOM; CLU_001162_0_0_1; -.
DR InParanoid; Q92752; -.
DR OMA; RPYNHRP; -.
DR OrthoDB; 18592at2759; -.
DR PhylomeDB; Q92752; -.
DR TreeFam; TF329915; -.
DR PathwayCommons; Q92752; -.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR SignaLink; Q92752; -.
DR BioGRID-ORCS; 7143; 15 hits in 1070 CRISPR screens.
DR ChiTaRS; TNR; human.
DR GeneWiki; Tenascin-R; -.
DR GenomeRNAi; 7143; -.
DR Pharos; Q92752; Tbio.
DR PRO; PR:Q92752; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q92752; protein.
DR Bgee; ENSG00000116147; Expressed in CA1 field of hippocampus and 82 other tissues.
DR ExpressionAtlas; Q92752; baseline and differential.
DR Genevisible; Q92752; HS.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0072534; C:perineuronal net; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0090733; C:tenascin complex; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0008306; P:associative learning; IEA:Ensembl.
DR GO; GO:0048677; P:axon extension involved in regeneration; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; NAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
DR GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
DR GO; GO:0048692; P:negative regulation of axon extension involved in regeneration; IEA:Ensembl.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0050805; P:negative regulation of synaptic transmission; IEA:Ensembl.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR GO; GO:0007158; P:neuron cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
DR GO; GO:0051971; P:positive regulation of transmission of nerve impulse; IEA:Ensembl.
DR GO; GO:0030334; P:regulation of cell migration; IEA:Ensembl.
DR GO; GO:0050808; P:synapse organization; IEA:Ensembl.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IEA:Ensembl.
DR GO; GO:0022029; P:telencephalon cell migration; IEA:Ensembl.
DR CDD; cd00063; FN3; 9.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 2.60.40.10; -; 9.
DR Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR041161; EGF_Tenascin.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR033079; TNR.
DR PANTHER; PTHR19143:SF254; PTHR19143:SF254; 3.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF18720; EGF_Tenascin; 2.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR Pfam; PF00041; fn3; 9.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00186; FBG; 1.
DR SMART; SM00060; FN3; 9.
DR SUPFAM; SSF49265; SSF49265; 5.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50853; FN3; 9.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Coiled coil; Disulfide bond;
KW EGF-like domain; Extracellular matrix; Glycoprotein; Phosphoprotein;
KW Proteoglycan; Reference proteome; Repeat; Secreted; Sialic acid; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..1358
FT /note="Tenascin-R"
FT /id="PRO_0000007747"
FT DOMAIN 188..199
FT /note="EGF-like 1"
FT DOMAIN 219..230
FT /note="EGF-like 2"
FT DOMAIN 250..261
FT /note="EGF-like 3"
FT DOMAIN 281..292
FT /note="EGF-like 4"
FT DOMAIN 312..323
FT /note="EGF-like 5"
FT DOMAIN 328..420
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 421..505
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 506..595
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 596..687
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 688..777
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 778..865
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 866..955
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 956..1042
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1043..1130
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1129..1344
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT COILED 127..157
FT /evidence="ECO:0000255"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05546"
FT CARBOHYD 36
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305|PubMed:19838169"
FT CARBOHYD 37
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305|PubMed:19838169"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 791
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 874
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1036
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1046
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 292..301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 297..312
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 314..323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT VAR_SEQ 773..862
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8626505"
FT /id="VSP_012993"
FT VARIANT 17
FT /note="I -> V (in dbSNP:rs859398)"
FT /evidence="ECO:0000269|PubMed:8626505, ECO:0000269|Ref.2"
FT /id="VAR_021479"
FT VARIANT 128
FT /note="A -> S (in dbSNP:rs2239819)"
FT /id="VAR_021906"
FT VARIANT 293
FT /note="G -> S (in dbSNP:rs3752516)"
FT /id="VAR_021907"
FT VARIANT 302
FT /note="S -> N (in dbSNP:rs35736986)"
FT /id="VAR_055780"
FT VARIANT 643
FT /note="R -> K (in dbSNP:rs859427)"
FT /id="VAR_030737"
FT CONFLICT 629
FT /note="S -> I (in Ref. 2; CAA66709)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1358 AA; 149562 MW; E4DE356B44D117E7 CRC64;
MGADGETVVL KNMLIGINLI LLGSMIKPSE CQLEVTTERV QRQSVEEEGG IANYNTSSKE
QPVVFNHVYN INVPLDNLCS SGLEASAEQE VSAEDETLAE YMGQTSDHES QVTFTHRINF
PKKACPCASS AQVLQELLSR IEMLEREVSV LRDQCNANCC QESAATGQLD YIPHCSGHGN
FSFESCGCIC NEGWFGKNCS EPYCPLGCSS RGVCVDGQCI CDSEYSGDDC SELRCPTDCS
SRGLCVDGEC VCEEPYTGED CRELRCPGDC SGKGRCANGT CLCEEGYVGE DCGQRQCLNA
CSGRGQCEEG LCVCEEGYQG PDCSAVAPPE DLRVAGISDR SIELEWDGPM AVTEYVISYQ
PTALGGLQLQ QRVPGDWSGV TITELEPGLT YNISVYAVIS NILSLPITAK VATHLSTPQG
LQFKTITETT VEVQWEPFSF SFDGWEISFI PKNNEGGVIA QVPSDVTSFN QTGLKPGEEY
IVNVVALKEQ ARSPPTSASV STVIDGPTQI LVRDVSDTVA FVEWIPPRAK VDFILLKYGL
VGGEGGRTTF RLQPPLSQYS VQALRPGSRY EVSVSAVRGT NESDSATTQF TTEIDAPKNL
RVGSRTATSL DLEWDNSEAE VQEYKVVYST LAGEQYHEVL VPRGIGPTTR ATLTDLVPGT
EYGVGISAVM NSQQSVPATM NARTELDSPR DLMVTASSET SISLIWTKAS GPIDHYRITF
TPSSGIASEV TVPKDRTSYT LTDLEPGAEY IISVTAERGR QQSLESTVDA FTGFRPISHL
HFSHVTSSSV NITWSDPSPP ADRLILNYSP RDEEEEMMEV SLDATKRHAV LMGLQPATEY
IVNLVAVHGT VTSEPIVGSI TTGIDPPKDI TISNVTKDSV MVSWSPPVAS FDYYRVSYRP
TQVGRLDSSV VPNTVTEFTI TRLNPATEYE ISLNSVRGRE ESERICTLVH TAMDNPVDLI
ATNITPTEAL LQWKAPVGEV ENYVIVLTHF AVAGETILVD GVSEEFRLVD LLPSTHYTAT
MYATNGPLTS GTISTNFSTL LDPPANLTAS EVTRQSALIS WQPPRAEIEN YVLTYKSTDG
SRKELIVDAE DTWIRLEGLL ENTDYTVLLQ AAQDTTWSSI TSTAFTTGGR VFPHPQDCAQ
HLMNGDTLSG VYPIFLNGEL SQKLQVYCDM TTDGGGWIVF QRRQNGQTDF FRKWADYRVG
FGNVEDEFWL GLDNIHRITS QGRYELRVDM RDGQEAAFAS YDRFSVEDSR NLYKLRIGSY
NGTAGDSLSY HQGRPFSTED RDNDVAVTNC AMSYKGAWWY KNCHRTNLNG KYGESRHSQG
INWYHWKGHE FSIPFVEMKM RPYNHRLMAG RKRQSLQF
