FREM2_MOUSE
ID FREM2_MOUSE Reviewed; 3160 AA.
AC Q6NVD0; Q4W2Q5; Q5H8C0; Q811G9; Q8C4G5; Q8CD46;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=FRAS1-related extracellular matrix protein 2;
DE AltName: Full=ECM3 homolog;
DE AltName: Full=NV domain-containing protein 1;
DE Flags: Precursor;
GN Name=Frem2; Synonyms=Nv1;
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 [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=15838507; DOI=10.1038/ng1549;
RA Jadeja S., Smyth I., Pitera J.E., Taylor M.S., van Haelst M., Bentley E.,
RA McGregor L., Hopkins J., Chalepakis G., Philip N., Perez Aytes A.,
RA Watt F.M., Darling S.M., Jackson I., Woolf A.S., Scambler P.J.;
RT "Identification of a new gene mutated in Fraser syndrome and mouse
RT myelencephalic blebs.";
RL Nat. Genet. 37:520-525(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Testis;
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 2277-3160.
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Head, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-291.
RA Kiyozumi D., Osada A., Sugimoto N., Weber C.N., Ono Y., Imai T., Okada A.,
RA Sekiguchi K.;
RT "QBRICK, a novel cell-adhesive protein expressed in the basement membrane
RT of the developing hair follicle.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, and Spleen;
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).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=30802441; DOI=10.1016/j.exer.2019.02.013;
RA Zhang X., Wang D., Dongye M., Zhu Y., Chen C., Wang R., Long E., Liu Z.,
RA Wu X., Lin D., Chen J., Lin Z., Wang J., Li W., Li Y., Li D., Lin H.;
RT "Loss-of-function mutations in FREM2 disrupt eye morphogenesis.";
RL Exp. Eye Res. 181:302-312(2019).
CC -!- FUNCTION: Extracellular matrix protein required for maintenance of the
CC integrity of the skin epithelium and for maintenance of renal epithelia
CC (By similarity). Required for epidermal adhesion (PubMed:15838507).
CC Involved in the development of eyelids and the anterior segment of the
CC eyeballs (PubMed:30802441). {ECO:0000250|UniProtKB:Q5SZK8,
CC ECO:0000269|PubMed:15838507, ECO:0000269|PubMed:30802441}.
CC -!- SUBUNIT: Interacts with FREM1. {ECO:0000250|UniProtKB:Q5SZK8}.
CC -!- INTERACTION:
CC Q6NVD0; Q80T14: Fras1; NbExp=2; IntAct=EBI-15594269, EBI-15594303;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5SZK8};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6NVD0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NVD0-2; Sequence=VSP_015038, VSP_015039;
CC Name=3;
CC IsoId=Q6NVD0-3; Sequence=VSP_015037;
CC -!- TISSUE SPECIFICITY: First expressed from 10 dpc in the mesodermal core
CC of the branchial arches, developing lens, otic vesicle and limb apical
CC ectodermal ridge. Later, it is expressed in the vibrissae and vibrissae
CC pad, eyelids ear and pelage follicles and, at low levels, in the
CC epidermis (PubMed:15838507). Also expressed in caudal somites and, in
CC later embryos, in facial, limb and intercostal muscles
CC (PubMed:15838507). In contrast to Frem1, it is not expressed in the
CC developing mammary glands or in the caecum (PubMed:15838507).
CC Restricted to the epithelia in a pattern complementary to that of Frem1
CC (which is generally expressed in the dermis and mesenchyme)
CC (PubMed:15838507). In the developing kidney, it is expressed At in the
CC mesonephric and metanephric epithelia at 11.5 dpc, with a highest
CC expression at the tips of the developing ureteric buds
CC (PubMed:15838507). At 12.5 and 13.5 dpc, it is still expressed
CC throughout the epithelial components of the kidney, including epithelia
CC fated to form nephrons, which are induced by the ureter tips to
CC differeintiate from the mesenchymal condensations that surround them
CC (PubMed:15838507). Expressed in retinal neuron-containing outer
CC plexiform layer (PubMed:30802441). {ECO:0000269|PubMed:15838507,
CC ECO:0000269|PubMed:30802441}.
CC -!- DOMAIN: The Calx-beta domains bind calcium with high affinity and
CC undergo a major conformational shift upon binding. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice display cryptophthalmos, syndactyly and
CC renal defects. Frem2 corresponds to the X-ray irradiated-induced allele
CC 'myelencephalic blebs' (my). {ECO:0000269|PubMed:15838507}.
CC -!- SIMILARITY: Belongs to the FRAS1 family. {ECO:0000305}.
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DR EMBL; AJ833643; CAH55760.1; -; mRNA.
DR EMBL; AK031494; BAC27425.1; -; mRNA.
DR EMBL; AK082256; BAC38448.1; -; mRNA.
DR EMBL; BC046388; AAH46388.1; -; mRNA.
DR EMBL; BC068185; AAH68185.1; -; mRNA.
DR EMBL; AB160988; BAD89016.1; -; mRNA.
DR CCDS; CCDS17348.1; -. [Q6NVD0-1]
DR RefSeq; NP_766450.2; NM_172862.3. [Q6NVD0-1]
DR SMR; Q6NVD0; -.
DR DIP; DIP-61241N; -.
DR IntAct; Q6NVD0; 2.
DR STRING; 10090.ENSMUSP00000088670; -.
DR GlyGen; Q6NVD0; 5 sites.
DR iPTMnet; Q6NVD0; -.
DR PhosphoSitePlus; Q6NVD0; -.
DR EPD; Q6NVD0; -.
DR MaxQB; Q6NVD0; -.
DR PaxDb; Q6NVD0; -.
DR PRIDE; Q6NVD0; -.
DR ProteomicsDB; 266859; -. [Q6NVD0-1]
DR ProteomicsDB; 266860; -. [Q6NVD0-2]
DR ProteomicsDB; 266861; -. [Q6NVD0-3]
DR Antibodypedia; 23253; 121 antibodies from 29 providers.
DR DNASU; 242022; -.
DR Ensembl; ENSMUST00000091137; ENSMUSP00000088670; ENSMUSG00000037016. [Q6NVD0-1]
DR GeneID; 242022; -.
DR KEGG; mmu:242022; -.
DR UCSC; uc008pex.1; mouse. [Q6NVD0-3]
DR UCSC; uc008pey.1; mouse. [Q6NVD0-1]
DR CTD; 341640; -.
DR MGI; MGI:2444465; Frem2.
DR VEuPathDB; HostDB:ENSMUSG00000037016; -.
DR eggNOG; KOG1306; Eukaryota.
DR eggNOG; KOG2090; Eukaryota.
DR eggNOG; KOG3597; Eukaryota.
DR GeneTree; ENSGT00940000155313; -.
DR HOGENOM; CLU_000394_0_0_1; -.
DR InParanoid; Q6NVD0; -.
DR OMA; WRKQGAF; -.
DR OrthoDB; 13258at2759; -.
DR PhylomeDB; Q6NVD0; -.
DR TreeFam; TF316876; -.
DR BioGRID-ORCS; 242022; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Frem2; mouse.
DR PRO; PR:Q6NVD0; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q6NVD0; protein.
DR Bgee; ENSMUSG00000037016; Expressed in molar tooth and 151 other tissues.
DR Genevisible; Q6NVD0; MM.
DR GO; GO:0005604; C:basement membrane; IDA:BHF-UCL.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR GO; GO:0001654; P:eye development; IMP:UniProtKB.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0048839; P:inner ear development; IDA:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:MGI.
DR Gene3D; 2.60.40.2030; -; 5.
DR InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR039005; CSPG_rpt.
DR InterPro; IPR045658; FRAS1-rel_N.
DR Pfam; PF03160; Calx-beta; 5.
DR Pfam; PF19309; Frem_N; 1.
DR SMART; SM00237; Calx_beta; 5.
DR SUPFAM; SSF141072; SSF141072; 5.
DR PROSITE; PS51854; CSPG; 12.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Developmental protein; Glycoprotein; Membrane; Metal-binding;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..3160
FT /note="FRAS1-related extracellular matrix protein 2"
FT /id="PRO_0000010125"
FT TOPO_DOM 40..3105
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 3106..3126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3127..3160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 312..406
FT /note="CSPG 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 431..530
FT /note="CSPG 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 553..664
FT /note="CSPG 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 689..796
FT /note="CSPG 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 817..908
FT /note="CSPG 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 934..1026
FT /note="CSPG 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1055..1157
FT /note="CSPG 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1178..1271
FT /note="CSPG 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1292..1388
FT /note="CSPG 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1409..1501
FT /note="CSPG 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1521..1610
FT /note="CSPG 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1644..1741
FT /note="CSPG 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT DOMAIN 1748..1847
FT /note="Calx-beta 1"
FT DOMAIN 1860..1971
FT /note="Calx-beta 2"
FT DOMAIN 1986..2092
FT /note="Calx-beta 3"
FT DOMAIN 2107..2209
FT /note="Calx-beta 4"
FT DOMAIN 2227..2331
FT /note="Calx-beta 5"
FT REGION 3130..3160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3136..3160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1730
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..2851
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015037"
FT VAR_SEQ 1..2287
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015038"
FT VAR_SEQ 2288..2297
FT /note="SGEDYHPVSE -> MVGPGNFRKR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015039"
FT CONFLICT 2437
FT /note="S -> N (in Ref. 2; BAC27425)"
FT /evidence="ECO:0000305"
FT CONFLICT 2851
FT /note="H -> N (in Ref. 2; BAC27425)"
FT /evidence="ECO:0000305"
FT CONFLICT 3031
FT /note="P -> H (in Ref. 3; AAH46388)"
FT /evidence="ECO:0000305"
FT CONFLICT 3040
FT /note="S -> G (in Ref. 3; AAH46388)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3160 AA; 350640 MW; 579F20BD79957E06 CRC64;
MASRARRTAK FSSFQPILAQ SPRLLLLLLL LSLVSYVSTQ AAGPGAALQS LGLSGTSGVP
TEEAIVVANR GLRVPFGREV WLDPLRDLVL QVQPGDRCTV TVLDNDALAQ RPGHLSPKRF
ACDYGPGEVR YSHLGARSPS RDRVRLQLRY DAPGGAIVLP LALEVEVVFT QLEIVTRNLP
LVVEELLGTS NALDDRSLEF AYQPETEECR VGILSGLSAL PRYGELLHYP QVQGGAGDRG
TSKTLLMDCK AFQELGVRYR HTAPSRSPNR DWLPMVVELH SRGAPEGSPA LKREHFQVLV
RIRGGAENTA PKPSFVAMMM MEVDQFVLTA LTPDMLAAED AESDPDLLIF NLTSAFQPGQ
GYLVSTDDRS LPLSSFTQRD LRLLKIAYQP PSEDSDQERL FELELEIVDP EGAASDPFAF
MVVVKPMNTL APVVTRNTGL ILYEGQYRPL TGPIGSGPQN LVISDEDDLE AVRLEVVAGL
RHGHLVILGS PSSDSAPKTF TVAELAAGQV VYQHDDKDGS LSDNLVLRMS DGGGRHQVQF
LFPITLVPVD DQPPVLNANT GLTVAEGETV PIPPLTLSAT DIDSDDSQLV FVLLPPFSSL
GHLLLRQRHV PQEEQGLWQK QGSFYERTVT EWRQQDITEG KLFYRHSGPH SPGPVMDQFM
FRVQDNHDPP NQSGIQRFVI RIHPVDRLPP ELGSGCPLRM VVQESQLTPL RKRWLHYTDL
DTDDRELQYT VTQPPTDTDE NHSPAPLGTL VFTDNPSVVV SHFTQAQVNH HKIAYRPPGQ
ELGVAARVAQ FQFQVEDRAG NVAPGTFTLY LQPVDNQPPE IVNTGFTVEE KGHHILRETE
LHVSDVDTDV THISFTLTQA PKHGHMQISG RPLHVGGQFH LEDIKHGRIS YWNSGDESLT
DSCSLEVSDR HHVVPITLRV NVRPGDREGP MSVLPAGTLE SYLDVLENGA TEVTANIIKG
AYQGTDDLML TFLLEGPPSY GEILVNGAPA EQFTQRDILE GSVVYAHTSG EIGLLPKADS
FNLSLSAMSQ EWRIGSSIVQ GVTVWVTILP VDSQAPEISL GEQFVVLEGD KSVISLTHLS
AEDMDSLKDD LLCTIVIQPT SGYVENISPA PGSEKSRAGV AISAFTLKDL RQGHINYVQS
VHRGVEPVED RFIFRCSDGI NFSERQIFPI VIIPTNDEQP EMFMREFMVM EGMSLVVNRL
ILNAADADIP RDDLTFTITR FPTHGHVMNQ LINGTVLVES FTLDQIIESS SIIYEHDDSE
TQEDSFVIKL TDGKHSVEKM VLIVVIPVDD ETPRMTINNG LEIEIGETKV INNKVLMATD
LDSDDKSLVY IIRYGPGHGL LQRQKPLGAF ENITLGMNFT QDEVDRNLIQ YVHFGQEGIR
DLIKFDVTDG TNALIDRYFY VTIGSVDIVF PDVVSKGVSL KEGGKVTLTT DLLSTSDLNS
PDENLVFTIT RAPMRGHLEC TDRRGLSITS FTQLQLAGNK IYYIHTAEDE VKMDSFEFQV
TDGRNPVFRT FRISISDVDN KKPVVTIHNL VVSESESKLI TPFELTVEDR DTPDRLLKFI
VTQVPVHGHL LFNNTRSVMV FTKQDLNENL ISYKHDGTES TEDSFSFTVT DGTHSDFYVF
PDTVFETRRP QVMKIQVLPV DNSVPQIVVN KGASTLRTLA TGHLGFMITS KILKVEDRDS
LHFSLRFIVT EAPQHGYLLN LGQGNHSVTQ FTQADIDDMK ICYVLRERAN ATSDMFHFIV
EDDGGNRLTN QHFRLNWAWI SFEKEYYLIN EDSKFLDIVL TRRGYLGETS FISIGTRDGT
AEKDRDFKGK AQKQVQFNPG QTRASWRVRI LSDGEHEHSE TFQVVLSEPV LAILEFPTVT
TVEIIDPGDE STVFIPQSEY SVEEDVGELF IPIRRSGDIS RELMVICYTQ QGTATSTVRT
SVLSYSDYIS RPEDHSSVIR FDKDEREKMC RILVIDDSLY EEEETFQVLL SMPMGGRIGD
KFPGANVTIL TDRDDEPAFY FGDTQYSVDE SAGYVELQVW RTGTDLSKPS SVTVRSRKTE
SLSADAGTDY VGISRNLDFA PGVNMQTVRV VILDDLGRPI LEGIEKFELV LRMPMNAALG
EPSKATVSIN DSASDLPKMQ FKERVYTCNE NDGRVVAMIY RSGDIQHRSS VRCYTRQGSA
QVMMDFEERP NTDVSTVTFL PGEMEKPCVL ELMDDAVYED VEELRLVLGT PQGSSAFGAA
VGEQNETLIK IQDEADKAVI KFGETKFSVT EPSRPGESVV VKIPVIRQGD TSKVSIVRVH
TKDGSATSGE DYHPVSEEIE FKEGETQHTV EIEVIFDGVR EMREAFTVHL KPDENMVAET
QATKAIVYIE EIHSMADVTF PSVPHIVSLL IYDDPSKGRE DTGPVSGYPV VCITACNPKY
PDYEKTGSIC ASENINDTLT RYRWLISAPA GPDGVTSPMR EVDFDTFFTS SKMITLDSIY
FQPGSRVQCA ARAVNTNGNE GLELMSPIVT IGREEGLCQP RVPGVVGAEP FSAKLRYTGP
EDPDFANLIK LTVTMPHIDG MLPAISTREL SNFELTLSPD GTRVGNHKCS NLLDYNEVKT
HHGFLTNATK NPEVIGETYP YQYSVPVRGS STLRFYRNLN LEACLWEFVS YYDMTELLAD
CGGTIGTDGQ VLNLVQSYVT LRVPLYVSYV FHSPVGVGGW QHFDLKSELR LTFVYDTAIL
WNHGIGSPPE AELQGSLYPT SMRIGEEGRL AVNFKTEAQF HGLFVLSHPA SFTSSLIVSA
DHPGLTFSLR LIRSEPTYNQ PVQQWSFVSD FAVRDYSGTY TVKLVPCTTP SNQEYRLPVT
CNPREPVTFD LDIRFQQVSD PVATEFSLNT HMYLLSKKNL WLSDGSMGFG QESDVAFAEG
DVIYGRVMVD PVQNLGDSFY CSIEKVFLCT GDDGYVPKYS PANAEYGCLA DSPSLLHRFK
IVDKAQPETQ ATSFGDVLFN AKLAVDDPEA VLLVNQPGSD GFKVDSTPLF QVALGREWYI
HTIYTVKSKD NTHRGIGKRS LEYQYHSVVH PGPPQATTKS WKKRAVRSTP SLAGEIGAEN
NRGTNIQHIS LNRRGKRQVP HGRIPPDGIL PWELNSPSSE VSLVTVLGGL TVGLLTVCLA
VAAAVMCRNR STKGKDTPKG SGSTEPMMSP QSHYNDSSEV
