ID TF7L2_MOUSE Reviewed; 459 AA. AC Q924A0; O70574; Q8C834; Q91XP2; Q91XP3; Q91XP4; Q924A1; Q9Z0V3; AC Q9Z0V4; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 25-MAR-2003, sequence version 2. DT 06-MAR-2013, entry version 106. DE RecName: Full=Transcription factor 7-like 2; DE AltName: Full=HMG box transcription factor 4; DE AltName: Full=T-cell-specific transcription factor 4; DE Short=T-cell factor 4; DE Short=TCF-4; DE Short=mTCF-4; GN Name=Tcf7l2; Synonyms=Tcf4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=C57BL/6; TISSUE=Embryo; RX MEDLINE=98147763; PubMed=9488439; RA Korinek V., Barker N., Willert K., Molenaar M., Roose J., Wagenaar G., RA Markman M., Lamers W., Destree O., Clevers H.; RT "Two members of the Tcf family implicated in Wnt/b-catenin signaling RT during embryogenesis in the mouse."; RL Mol. Cell. Biol. 18:1248-1256(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PARTIAL NUCLEOTIDE RP SEQUENCE [MRNA] (ISOFORMS 1 AND 4). RC STRAIN=ICR; TISSUE=Fetal intestine; RX MEDLINE=99098900; PubMed=9880534; DOI=10.1074/jbc.274.3.1566; RA Lee Y.J., Swencki B., Shoichet S., Shivdasani R.A.; RT "A possible role for the high mobility group box transcription factor RT Tcf-4 in vertebrate gut epithelial cell differentiation."; RL J. Biol. Chem. 274:1566-1572(1999). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 6 AND 7), AND RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 5). RC STRAIN=C57BL/6J, and CD-1; TISSUE=Pituitary; RX MEDLINE=21833811; PubMed=11845287; DOI=10.1007/s00335-001-2076-0; RA Douglas K.R., Brinkmeier M.L., Kennell J.A., Eswara P., Harrison T.A., RA Patrianakos A.I., Sprecher B.S., Potok M.A., Lyons R.H. Jr., RA MacDougald O.A., Camper S.A.; RT "Identification of members of the Wnt signaling pathway in the RT embryonic pituitary gland."; RL Mamm. Genome 12:843-851(2001). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8). RA Bayarsaihan D.; RT "A novel isoform of the HMG transcription factor Tcf4."; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9). RC STRAIN=C57BL/6J; TISSUE=Head; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [7] RP FUNCTION. RX MEDLINE=98361166; PubMed=9697701; DOI=10.1038/1270; RA Korinek V., Barker N., Moerer P., van Donselaar E., Huls G., RA Peters P.J., Clevers H.; RT "Depletion of epithelial stem-cell compartments in the small intestine RT of mice lacking Tcf-4."; RL Nat. Genet. 19:379-383(1998). RN [8] RP INTERACTION WITH TGFB1I1. RX PubMed=16291758; DOI=10.1074/jbc.M505869200; RA Ghogomu S.M., van Venrooy S., Ritthaler M., Wedlich D., Gradl D.; RT "HIC-5 is a novel repressor of lymphoid enhancer factor/T-cell factor- RT driven transcription."; RL J. Biol. Chem. 281:1755-1764(2006). RN [9] RP INTERACTION WITH TNIK AND CTNNB1. RX PubMed=19816403; DOI=10.1038/emboj.2009.285; RA Mahmoudi T., Li V.S.W., Ng S.S., Taouatas N., Vries R.G.J., RA Mohammed S., Heck A.J., Clevers H.; RT "The kinase TNIK is an essential activator of Wnt target genes."; RL EMBO J. 28:3329-3340(2009). RN [10] RP FUNCTION. RX PubMed=21856776; DOI=10.1101/gad.17227011; RA Vacik T., Stubbs J.L., Lemke G.; RT "A novel mechanism for the transcriptional regulation of Wnt signaling RT in development."; RL Genes Dev. 25:1783-1795(2011). CC -!- FUNCTION: Participates in the Wnt signaling pathway and modulates CC MYC expression by binding to its promoter in a sequence-specific CC manner. Acts as repressor in the absence of CTNNB1, and as CC activator in its presence. Activates transcription from promoters CC with several copies of the Tcf motif CCTTTGATC in the presence of CC CTNNB1. TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated CC by TCF7L2/TCF4 and CTNNB1. Expression of dominant-negative mutants CC results in cell-cycle arrest in G1 (By similarity). Necessary for CC the maintenance of the epithelial stem-cell compartment of the CC small intestine. CC -!- SUBUNIT: Interacts with TGFB1I1. Interacts with CTNNB1 (via the CC armadillo repeat); forms stable transcription complex. Interacts CC with EP300. Interacts with NLK. Interacts with CCDC85B (probably CC through the HMG box); prevents interaction with CTNNB1. Interacts CC with MAD2L2; prevents TCF7L2/TCF4 binding to promoters, negatively CC modulating its transcriptional activity (By similarity). Interacts CC with TNIK. Interacts with ZIPK/DAPK3 (By similarity). Interacts CC with XIAP/BIRC4 and TLE3 (By similarity). Interacts with CC DDIT3/CHOP (By similarity). CC -!- INTERACTION: CC P39428:Traf1; NbExp=6; IntAct=EBI-646713, EBI-520123; CC -!- SUBCELLULAR LOCATION: Nucleus, PML body. Note=Diffuse pattern. CC Colocalizes with SUMO1 and PIAS4 in a subset of PML (promyelocytic CC leukemia) nuclear bodies (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=9; CC Name=1; CC IsoId=Q924A0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q924A0-2; Sequence=VSP_006976, VSP_006979; CC Name=3; CC IsoId=Q924A0-3; Sequence=VSP_006975; CC Name=4; CC IsoId=Q924A0-4; Sequence=VSP_006978, VSP_006981; CC Name=5; CC IsoId=Q924A0-5; Sequence=VSP_006974, VSP_006977; CC Name=6; CC IsoId=Q924A0-6; Sequence=VSP_006977; CC Name=7; CC IsoId=Q924A0-7; Sequence=VSP_006973, VSP_006975, VSP_006977; CC Name=8; CC IsoId=Q924A0-8; Sequence=VSP_006976, VSP_006980; CC Note=May result from the retention of an intron in the cDNA; CC Name=9; Synonyms=dnTcf7l2 exon1b/c; CC IsoId=Q924A0-9; Sequence=VSP_043205; CC Note=Dominant negative form which cannot bind CTNNB1. Expression CC is VAX2-dependent; CC -!- TISSUE SPECIFICITY: Detected in adult brain and liver, and at CC lower levels in intestine, with a clear increase from the distal CC colon to the duodenum. Detected at low levels in heart, lung, CC kidney, pituitary and testis. CC -!- DEVELOPMENTAL STAGE: First detected at E10.5. Highly expressed at CC E13.5-E16.5 in the central nervous system, in particular in the CC roof of the mesencephalon, at the ditelencephalic junction and in CC dorsal thalamus. At E13.5, detected at low levels in CC gastrointestinal epithelia. CC -!- PTM: Phosphorylated at Thr-178 and/or Thr-189 by NLK. CC Phosphorylation by NLK at these sites inhibits DNA-binding by CC TCF7L2/TCF4, thereby preventing transcriptional activation of CC target genes of the canonical Wnt/beta-catenin signaling pathway CC (By similarity). CC -!- PTM: Polysumoylated. Sumoylation is enhanced by PIAS family CC members and desumoylation is enhanced by SENP2. CC Sumoylation/desumoylation regulates TCF7L2/TCF4 transcription CC activity in the Wnt/beta-catenin signaling pathway without CC altering interaction with CTNNB1 nor binding to DNA (By CC similarity). CC -!- DISEASE: Note=Constitutive activation and subsequent CC transactivation of target genes may lead to the maintenance of CC stem-cell characteristics (cycling and longevity) in cells that CC should normally undergo terminal differentiation and constitute CC the primary transforming event in colorectal cancer (CRC). CC -!- SIMILARITY: Belongs to the TCF/LEF family. CC -!- SIMILARITY: Contains 1 HMG box DNA-binding domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ223070; CAA11071.1; -; mRNA. DR EMBL; AF107298; AAD16967.1; -; mRNA. DR EMBL; AF107299; AAD16968.1; -; mRNA. DR EMBL; AF363722; AAK77485.1; -; Genomic_DNA. DR EMBL; AF363722; AAK77486.1; -; Genomic_DNA. DR EMBL; AF363724; AAK77488.1; -; mRNA. DR EMBL; AF363725; AAK77489.1; -; mRNA. DR EMBL; AF363726; AAK77490.1; -; mRNA. DR EMBL; AY072035; AAL58534.1; -; mRNA. DR EMBL; AK048536; BAC33366.1; -; mRNA. DR EMBL; AC118695; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC137148; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC157916; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR IPI; IPI00129307; -. DR IPI; IPI00224936; -. DR IPI; IPI00224938; -. DR IPI; IPI00224939; -. DR IPI; IPI00224941; -. DR IPI; IPI00830945; -. DR IPI; IPI00831494; -. DR IPI; IPI00831648; -. DR IPI; IPI00918384; -. DR RefSeq; NP_001136390.1; NM_001142918.1. DR RefSeq; NP_001136393.1; NM_001142921.1. DR RefSeq; NP_001136396.1; NM_001142924.1. DR UniGene; Mm.139815; -. DR ProteinModelPortal; Q924A0; -. DR SMR; Q924A0; 12-49, 326-401. DR DIP; DIP-40920N; -. DR IntAct; Q924A0; 1. DR MINT; MINT-421706; -. DR STRING; Q924A0; -. DR PhosphoSite; Q924A0; -. DR PRIDE; Q924A0; -. DR Ensembl; ENSMUST00000111646; ENSMUSP00000107273; ENSMUSG00000024985. DR Ensembl; ENSMUST00000111649; ENSMUSP00000107276; ENSMUSG00000024985. DR Ensembl; ENSMUST00000111651; ENSMUSP00000107278; ENSMUSG00000024985. DR Ensembl; ENSMUST00000111652; ENSMUSP00000107279; ENSMUSG00000024985. DR Ensembl; ENSMUST00000111659; ENSMUSP00000107287; ENSMUSG00000024985. DR GeneID; 21416; -. DR KEGG; mmu:21416; -. DR UCSC; uc008hya.2; mouse. DR UCSC; uc008hyb.2; mouse. DR UCSC; uc008hyh.2; mouse. DR UCSC; uc008hyk.2; mouse. DR UCSC; uc008hyl.2; mouse. DR CTD; 6934; -. DR MGI; MGI:1202879; Tcf7l2. DR eggNOG; NOG252916; -. DR GeneTree; ENSGT00390000009964; -. DR HOGENOM; HOG000116032; -. DR HOVERGEN; HBG000419; -. DR KO; K04491; -. DR OrthoDB; EOG43XV3J; -. DR ChiTaRS; TCF7L2; mouse. DR NextBio; 300716; -. DR Bgee; Q924A0; -. DR CleanEx; MM_TCF4; -. DR Genevestigator; Q924A0; -. DR GermOnline; ENSMUSG00000024985; Mus musculus. DR GO; GO:0071664; C:catenin-TCF7L2 complex; IDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL. DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell. DR GO; GO:0005667; C:transcription factor complex; IDA:MGI. DR GO; GO:0008013; F:beta-catenin binding; IDA:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:BHF-UCL. DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IBA:RefGenome. DR GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:MGI. DR GO; GO:0030282; P:bone mineralization; IGI:MGI. DR GO; GO:0060070; P:canonical Wnt receptor signaling pathway; IMP:MGI. DR GO; GO:0035411; P:catenin import into nucleus; IDA:MGI. DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IGI:MGI. DR GO; GO:0030538; P:embryonic genitalia morphogenesis; IGI:MGI. DR GO; GO:0048619; P:embryonic hindgut morphogenesis; IGI:MGI. DR GO; GO:0060325; P:face morphogenesis; IGI:MGI. DR GO; GO:0048625; P:myoblast cell fate commitment; IMP:MGI. DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IMP:MGI. DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:MGI. DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IMP:MGI. DR GO; GO:0046621; P:negative regulation of organ growth; IMP:MGI. DR GO; GO:0021915; P:neural tube development; IGI:MGI. DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IGI:MGI. DR GO; GO:0014003; P:oligodendrocyte development; IMP:MGI. DR GO; GO:0021983; P:pituitary gland development; IMP:MGI. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI. DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:MGI. DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL. DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:MGI. DR GO; GO:0031641; P:regulation of myelination; IMP:MGI. DR GO; GO:0048713; P:regulation of oligodendrocyte differentiation; IMP:MGI. DR GO; GO:0048641; P:regulation of skeletal muscle tissue development; IMP:MGI. DR GO; GO:0009749; P:response to glucose stimulus; IMP:BHF-UCL. DR GO; GO:0032252; P:secretory granule localization; IMP:MGI. DR GO; GO:0043588; P:skin development; IGI:MGI. DR GO; GO:0035019; P:somatic stem cell maintenance; IMP:MGI. DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. DR Gene3D; 1.10.30.10; -; 1. DR InterPro; IPR013558; CTNNB1-bd_N. DR InterPro; IPR009071; HMG_superfamily. DR InterPro; IPR024940; TCF/LEF. DR PANTHER; PTHR10373; PTHR10373; 1. DR Pfam; PF08347; CTNNB1_binding; 1. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. DR SUPFAM; SSF47095; HMG-box; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. PE 1: Evidence at protein level; KW Activator; Alternative splicing; Complete proteome; DNA-binding; KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; KW Repressor; Transcription; Transcription regulation; Ubl conjugation; KW Wnt signaling pathway. FT CHAIN 1 459 Transcription factor 7-like 2. FT /FTId=PRO_0000048624. FT DNA_BIND 327 395 HMG box. FT REGION 1 53 CTNNB1-binding. FT REGION 178 372 Mediates interaction with MAD2L2 (By FT similarity). FT MOTIF 402 408 Nuclear localization signal (Potential). FT COMPBIAS 155 294 Pro-rich. FT MOD_RES 178 178 Phosphothreonine; by NLK (By similarity). FT MOD_RES 189 189 Phosphothreonine; by NLK (By similarity). FT CROSSLNK 297 297 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO) (By FT similarity). FT VAR_SEQ 1 161 MPQLNGGGGDDLGANDELISFKDEGEQEEKNSENSSAERDL FT ADVKSSLVNESETNQDSSSDSEAERRPPPRSESFRDKSRES FT LEEAAKRQDGGLFKGPPYPGYPFIMIPDLTSPYLPNGSLSP FT TARTYLQMKWPLLDVQAGSLQSRQTLKDARSPSPAHIV -> FT M (in isoform 9). FT /FTId=VSP_043205. FT VAR_SEQ 127 127 T -> TLHFQSGSTHYSAYKTIEHQIAIQ (in isoform FT 7). FT /FTId=VSP_006973. FT VAR_SEQ 161 161 V -> VQSPLPCCTQGHACPHFYTPSDFTVSTQVFRDTKSS FT HSLQKVGEPWYLE (in isoform 5). FT /FTId=VSP_006974. FT VAR_SEQ 237 240 Missing (in isoform 3 and isoform 7). FT /FTId=VSP_006975. FT VAR_SEQ 268 268 S -> SSFLSS (in isoform 2 and isoform 8). FT /FTId=VSP_006976. FT VAR_SEQ 270 459 Missing (in isoform 5, isoform 6 and FT isoform 7). FT /FTId=VSP_006977. FT VAR_SEQ 417 459 EHSECFLNPCLSLPPITDLSAPKKCRARFGLDQQNNWCGPC FT SL -> GEKKSAFATYKVKAAASAHPLQMEAY (in FT isoform 2). FT /FTId=VSP_006979. FT VAR_SEQ 417 459 EHSECFLNPCLSLPPITDLSAPKKCRARFGLDQQNNWCGPC FT SL -> GERGESGRWRLEDHSYVRLPSGGGRRNPRPGHCGE FT PILGSLFCLCVF (in isoform 8). FT /FTId=VSP_006980. FT VAR_SEQ 417 433 Missing (in isoform 4). FT /FTId=VSP_006978. FT VAR_SEQ 457 459 CSL -> ADANTPKKCRALFGLDRQTLWCKPCRRKKKCVRY FT IQGEGSCLSPPSSDGSLLDSPPPSPHLLGSPPQDAKSQTEQ FT TQPLSLSLKPDPLAHLSMMPPPPALLLAEAAHGKASALCPN FT GALDLPPAALQPSMVPSSSLAQPSTSSLHSHNSLAGTQPQP FT LSLVTKSLE (in isoform 4). FT /FTId=VSP_006981. FT CONFLICT 57 57 D -> N (in Ref. 2; AAD16967 and 3; FT AAK77488/AAK77489/AAK77490). FT CONFLICT 236 236 W -> R (in Ref. 4; AAL58534). FT CONFLICT 410 410 K -> Q (in Ref. 2; AAD16968). SQ SEQUENCE 459 AA; 51217 MW; 43BC307DC258E83F CRC64; MPQLNGGGGD DLGANDELIS FKDEGEQEEK NSENSSAERD LADVKSSLVN ESETNQDSSS DSEAERRPPP RSESFRDKSR ESLEEAAKRQ DGGLFKGPPY PGYPFIMIPD LTSPYLPNGS LSPTARTYLQ MKWPLLDVQA GSLQSRQTLK DARSPSPAHI VSNKVPVVQH PHHVHPLTPL ITYSNEHFTP GNPPPHLPAD VDPKTGIPRP PHPPDISPYY PLSPGTVGQI PHPLGWLVPQ QGQPVYPITT GGFRHPYPTA LTVNASMSRF PPHMVPPHHT LHTTGIPHPA IVTPTVKQES SQSDVGSLHS SKHQDSKKEE EKKKPHIKKP LNAFMLYMKE MRAKVVAECT LKESAAINQI LGRRWHALSR EEQAKYYELA RKERQLHMQL YPGWSARDNY GKKKKRKRDK QPGETNEHSE CFLNPCLSLP PITDLSAPKK CRARFGLDQQ NNWCGPCSL //