ID NEST_MOUSE Reviewed; 1864 AA. AC Q6P5H2; A1E2I2; Q80X00; Q8BPH7; Q9CV43; Q9R0C4; DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 143. DE RecName: Full=Nestin; GN Name=Nes; 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 2). RC STRAIN=BALB/cJ; RX PubMed=10842089; DOI=10.1016/s0925-4773(00)00301-4; RA Yang J., Bian W., Gao X., Chen L., Jing N.; RT "Nestin expression during mouse eye and lens development."; RL Mech. Dev. 94:287-291(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Brain; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-764 AND 1510-1864. RC STRAIN=C57BL/6J; TISSUE=Tongue; 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-57. RC TISSUE=Heart; RX PubMed=7542682; DOI=10.1177/43.8.7542682; RA Kachinsky A.M., Dominov J.A., Miller J.B.; RT "Intermediate filaments in cardiac myogenesis: nestin in the developing RT mouse heart."; RL J. Histochem. Cytochem. 43:843-847(1995). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1358-1514. RC STRAIN=VM; RA Huysentruyt L.C., Banerjee D., Seyfried T.N.; RT "Novel metastatic mouse tumor cells express multiple properties of RT macrophages."; RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases. RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1541, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic brain; RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200; RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; RT "Phosphoproteomic analysis of the developing mouse brain."; RL Mol. Cell. Proteomics 3:1093-1101(2004). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1837, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-623; SER-731; SER-775; RP SER-862; SER-894; SER-963; SER-1021; SER-1216; SER-1541 AND SER-1565, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and RC Pancreas; 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 [9] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=20963821; DOI=10.1002/stem.541; RA Park D., Xiang A.P., Mao F.F., Zhang L., Di C.G., Liu X.M., Shao Y., RA Ma B.F., Lee J.H., Ha K.S., Walton N., Lahn B.T.; RT "Nestin is required for the proper self-renewal of neural stem cells."; RL Stem Cells 28:2162-2171(2010). CC -!- FUNCTION: Required for brain and eye development. Promotes the CC disassembly of phosphorylated vimentin intermediate filaments (IF) CC during mitosis and may play a role in the trafficking and distribution CC of IF proteins and other cellular factors to daughter cells during CC progenitor cell division (By similarity). Required for survival, CC renewal and mitogen-stimulated proliferation of neural progenitor CC cells. {ECO:0000250, ECO:0000269|PubMed:20963821}. CC -!- SUBUNIT: Forms homodimers and homotetramers in vitro. In mixtures with CC other intermediate filament proteins such as vimentin and alpha- CC internexin, this protein preferentially forms heterodimers which can CC assemble to form intermediate filaments if nestin does not exceed 25%. CC Interacts with FHOD3 (By similarity). {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q6P5H2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6P5H2-2; Sequence=VSP_024923; CC -!- PTM: Constitutively phosphorylated. This increases during mitosis when CC the cytoplasmic intermediate filament network is reorganized (By CC similarity). {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: Embryonic lethality with the neuroepithelium of CC developing neural tube exhibiting low numbers of neural stem cells and CC high levels of apoptosis. No effect on cytoskeletal integrity. CC {ECO:0000269|PubMed:20963821}. CC -!- SIMILARITY: Belongs to the intermediate filament family. CC {ECO:0000255|PROSITE-ProRule:PRU01188}. 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; AF076623; AAF04456.2; -; mRNA. DR EMBL; BC060693; AAH60693.1; -; mRNA. DR EMBL; BC062893; AAH62893.1; -; mRNA. DR EMBL; AK009706; BAB26451.1; -; mRNA. DR EMBL; AK075690; BAC35892.1; -; mRNA. DR EMBL; S78708; AAP32014.1; -; mRNA. DR EMBL; EF101559; ABK96808.1; -; mRNA. DR CCDS; CCDS17461.1; -. [Q6P5H2-1] DR RefSeq; NP_057910.3; NM_016701.3. [Q6P5H2-1] DR AlphaFoldDB; Q6P5H2; -. DR SMR; Q6P5H2; -. DR BioGRID; 201730; 18. DR IntAct; Q6P5H2; 11. DR MINT; Q6P5H2; -. DR STRING; 10090.ENSMUSP00000088493; -. DR GlyGen; Q6P5H2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q6P5H2; -. DR PhosphoSitePlus; Q6P5H2; -. DR EPD; Q6P5H2; -. DR jPOST; Q6P5H2; -. DR MaxQB; Q6P5H2; -. DR PaxDb; 10090-ENSMUSP00000088493; -. DR PeptideAtlas; Q6P5H2; -. DR ProteomicsDB; 252809; -. [Q6P5H2-1] DR ProteomicsDB; 252810; -. [Q6P5H2-2] DR Pumba; Q6P5H2; -. DR Antibodypedia; 1658; 1218 antibodies from 49 providers. DR Ensembl; ENSMUST00000090973.12; ENSMUSP00000088493.6; ENSMUSG00000004891.17. [Q6P5H2-1] DR Ensembl; ENSMUST00000160694.2; ENSMUSP00000125571.2; ENSMUSG00000004891.17. [Q6P5H2-2] DR GeneID; 18008; -. DR KEGG; mmu:18008; -. DR UCSC; uc008ptm.1; mouse. [Q6P5H2-2] DR UCSC; uc008ptn.1; mouse. [Q6P5H2-1] DR AGR; MGI:101784; -. DR MGI; MGI:101784; Nes. DR VEuPathDB; HostDB:ENSMUSG00000004891; -. DR eggNOG; ENOG502RYFK; Eukaryota. DR GeneTree; ENSGT00940000162240; -. DR HOGENOM; CLU_003317_0_0_1; -. DR InParanoid; Q6P5H2; -. DR OMA; RKEGWDP; -. DR OrthoDB; 4204342at2759; -. DR PhylomeDB; Q6P5H2; -. DR TreeFam; TF336633; -. DR BioGRID-ORCS; 18008; 4 hits in 77 CRISPR screens. DR ChiTaRS; Nes; mouse. DR PRO; PR:Q6P5H2; -. DR Proteomes; UP000000589; Chromosome 3. DR RNAct; Q6P5H2; Protein. DR Bgee; ENSMUSG00000004891; Expressed in floor plate of midbrain and 252 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005882; C:intermediate filament; IDA:MGI. DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI. DR GO; GO:0031730; F:CCR5 chemokine receptor binding; ISO:MGI. DR GO; GO:0019215; F:intermediate filament binding; ISS:UniProtKB. DR GO; GO:0007420; P:brain development; ISS:UniProtKB. DR GO; GO:0048858; P:cell projection morphogenesis; IMP:MGI. DR GO; GO:0031076; P:embryonic camera-type eye development; ISS:UniProtKB. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISO:MGI. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI. DR GO; GO:0007399; P:nervous system development; IDA:MGI. DR GO; GO:0051402; P:neuron apoptotic process; IMP:MGI. DR GO; GO:0030844; P:positive regulation of intermediate filament depolymerization; ISS:UniProtKB. DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISS:UniProtKB. DR GO; GO:0072089; P:stem cell proliferation; ISO:MGI. DR Gene3D; 1.20.5.170; -; 1. DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1. DR InterPro; IPR018039; IF_conserved. DR InterPro; IPR039008; IF_rod_dom. DR InterPro; IPR031211; Nestin. DR PANTHER; PTHR47051; NESTIN; 1. DR PANTHER; PTHR47051:SF1; NESTIN; 1. DR Pfam; PF00038; Filament; 1. DR SMART; SM01391; Filament; 1. DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2. DR PROSITE; PS00226; IF_ROD_1; 1. DR PROSITE; PS51842; IF_ROD_2; 1. DR Genevisible; Q6P5H2; MM. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Coiled coil; Developmental protein; KW Intermediate filament; Neurogenesis; Phosphoprotein; Reference proteome. FT CHAIN 1..1864 FT /note="Nestin" FT /id="PRO_0000285856" FT DOMAIN 8..314 FT /note="IF rod" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188" FT REGION 1..7 FT /note="Head" FT REGION 8..43 FT /note="Coil 1A" FT REGION 44..55 FT /note="Linker 1" FT REGION 56..151 FT /note="Coil 1B" FT REGION 152..174 FT /note="Linker 12" FT REGION 175..193 FT /note="Coil 2A" FT REGION 194..196 FT /note="Linker 2" FT REGION 197..314 FT /note="Coil 2B" FT REGION 315..1864 FT /note="Tail" FT REGION 437..492 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 515..625 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 680..845 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 916..1113 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1129..1158 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1175..1344 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1375..1722 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1735..1807 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1841..1864 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 469..484 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 515..534 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 549..571 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 572..597 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 606..624 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 680..841 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 938..978 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 985..1021 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1035..1051 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1059..1087 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1088..1113 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1200..1217 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1254..1277 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1375..1403 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1439..1462 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1512..1534 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1656..1680 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1735..1754 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1787..1801 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P48681" FT MOD_RES 312 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48681" FT MOD_RES 316 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P48681" FT MOD_RES 356 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48681" FT MOD_RES 359 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48681" FT MOD_RES 389 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P48681" FT MOD_RES 565 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48681" FT MOD_RES 575 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48681" FT MOD_RES 623 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 688 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48681" FT MOD_RES 731 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 775 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 841 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48681" FT MOD_RES 862 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 894 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 963 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1010 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P21263" FT MOD_RES 1021 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1106 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48681" FT MOD_RES 1127 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P21263" FT MOD_RES 1177 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48681" FT MOD_RES 1188 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48681" FT MOD_RES 1195 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48681" FT MOD_RES 1216 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1290 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48681" FT MOD_RES 1541 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15345747, FT ECO:0007744|PubMed:21183079" FT MOD_RES 1565 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1656 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48681" FT MOD_RES 1665 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48681" FT MOD_RES 1745 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48681" FT MOD_RES 1747 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48681" FT MOD_RES 1837 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355" FT MOD_RES 1860 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48681" FT MOD_RES 1861 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48681" FT VAR_SEQ 750..793 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10842089" FT /id="VSP_024923" FT CONFLICT 184 FT /note="G -> C (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 257 FT /note="A -> P (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 265 FT /note="V -> L (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 319 FT /note="R -> G (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 458 FT /note="T -> S (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 535 FT /note="M -> K (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 544 FT /note="E -> K (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 558 FT /note="G -> R (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 570 FT /note="S -> L (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 587 FT /note="L -> S (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 673 FT /note="M -> I (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 704 FT /note="Q -> L (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 734 FT /note="E -> D (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 851 FT /note="L -> P (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 855 FT /note="K -> R (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 900 FT /note="E -> D (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 1008..1011 FT /note="RKSL -> GKFF (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 1021 FT /note="S -> F (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 1157 FT /note="C -> S (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 1241 FT /note="E -> EV (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 1382 FT /note="G -> A (in Ref. 5; ABK96808)" FT /evidence="ECO:0000305" FT CONFLICT 1404 FT /note="A -> T (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 1410 FT /note="G -> S (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 1577 FT /note="F -> S (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 1586..1591 FT /note="GWSPAA -> DWGPAV (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 1684 FT /note="T -> A (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" FT CONFLICT 1821 FT /note="G -> D (in Ref. 1; AAF04456)" FT /evidence="ECO:0000305" SQ SEQUENCE 1864 AA; 207124 MW; B9DF21005D977983 CRC64; MEGCVGEESF QMWELNRRLE AYLTRVKTLE EQNQLLSAEL GGLRAQSGDA SWRARADDEL AALRVLVDQR WREKHEAEVQ RDNLAEELES VAGRCQQVRL ARERTIEEAA CSRRALEAEK NARGWLSTQA AELERELEAL RASHEEERAH LNAQAACTPR RPPAPAHASP IRAPEVEELA RRLGEVWRGA VRDYQERVAH MESSLGQARE RLGQAVRGAR ESRLEVQQLQ ADRDSLQERR EALEQRLEGR WQDRLQATEK FQLAVEALEQ EKQGLQSQIA QILEGGQQLA HLKMSLSLEV ATYRTLLEAE NSRLQTPGRS SQASLGFPDP KLKLHFLGIP EDQHLGSVLP VLSPTSFSSP LPNTLETPVT AFLKTQEFLK ARTPTLASTP IPPMSEAPYP KNAEVRAQDV PHSLLQGGRQ QAPEPLWAEA TVPSSTGVLP ELEEPGGEQP DHFPDDPTSL APPLNPHHSI LEAKDRESSE SRVSSIFQEE EGQIWELVKK EAATEVKVEN SLAQEIQESG LDTEEIQDSQ GPLQMETLEA LGDEPLMSLK TQNHETPGKE NCNSSIEENS GTVKSPEKEK QTPLKSLEEK NVEAEKTLEN GVLELSKPLG EEEPRMEDQE LMSPEHTLET VSFLGKENQE VVRSSEEQNL ESLITFKEES QYPLGGPEAE DQMLERLVEK EDQRFPRSPE EDQQAFRPLE KENQEPLRFE EAEDQVLERL IEKERQESLK SPEEEDQQAF RLLEKENQEP LRFEDAEDQV LERLIEKERQ ESLKSPEEED QQAFRLLEKE NQEPLRFEEA EDQVLERLVE KESQESLKSP EEEDQRTGKP LEKENQESLR SLDENQETIV LLESKNQRPL RSLEVEEEEQ RIVKPLEKVS QVSLESLEKE NVQSPRYLEE DDHMIKSLLE DKTHEILGSL EDRNGENFIP PENETQGSLR PPEEEDQRIV NHLEKESQEF LRSPEAEEEE EQVMVRSLEG ENHDPLSSVV KEEQMAESKL ENESQDSRKS LEDESQETFG SLEKENLESL RSLAGQDQEE QKLEQETQQP LRAVEDEQMT VNPPEKVDPE LPKPLRNDQE VVRSLDKENQ ESLVSLNEGG METVKSSETE NIESLETVGE CLGRRKSVDT QEPLWSTEVT SETIEPLEDE TQEPLGCVDE NQEVLTPLER ESQELRSLGK WNPETVESPG GVEDSQQCLE VEEGPEREQH QESLRSLGEV EWELPGSGSQ QRWEDVVEDG EGQEASLGAT GVETEDKAEL HLRGQGGEEK AVEEGELLQD AVGEAWSLGS SEPKEQRVPA EPLDDLEGQP EQTGTLEVPV AQGMPEATEQ DEDRAQAGEQ DSVEVTLGLE AARAGLELEQ EVVGLEDPRH FAREEAIHPS LGEESVKAKI DQGLEEPGKE PKEAGALDSG IPELPKTSSE TLECKGWEES GEGWGEEEAS LETSDHEGSH APQPRPPKTE EDEGLQAALT VPGPKLLEPC SPIPILTDAH ELQPQAEGIQ EAGWQPEAGT EALGRVEDEP EFGRGEIPEG LQDWEEGRED SEADELGETL PDSTPLGLYL KSPASPKWEQ AGEQRLFPQG EARKEGWSPA ALAAQGLSDP PEEEQQGHDS DLSSEEFEDL GTEASLLPGV PKEVSDHLGQ EPPVLQPACW DQGGESDGFA DEEESGEEGE EEDADEEEGA ESGTQWWGPG PSGGGVKVQD VTQRGDLEHE SVGDSGLWDD GLSGAAANVL VTALETVSQD SAEPSGSEGS ESASLEGEEG QAIDHLDAPQ EVTSVVPGAG DTFDISGQGP NLESEQVNGR MENGLEQAEG QVVLHGDEDQ GIPLQEQGTL KAPLVGSPVH LGPSQPLKFT LSGVDGDSWS SGED //