NEST_MOUSE
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 03-AUG-2022, entry version 134.
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}.
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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; 15.
DR IntAct; Q6P5H2; 9.
DR STRING; 10090.ENSMUSP00000088493; -.
DR iPTMnet; Q6P5H2; -.
DR PhosphoSitePlus; Q6P5H2; -.
DR EPD; Q6P5H2; -.
DR jPOST; Q6P5H2; -.
DR MaxQB; Q6P5H2; -.
DR PaxDb; Q6P5H2; -.
DR PeptideAtlas; Q6P5H2; -.
DR PRIDE; Q6P5H2; -.
DR ProteomicsDB; 252809; -. [Q6P5H2-1]
DR ProteomicsDB; 252810; -. [Q6P5H2-2]
DR Antibodypedia; 1658; 1113 antibodies from 49 providers.
DR Ensembl; ENSMUST00000090973; ENSMUSP00000088493; ENSMUSG00000004891. [Q6P5H2-1]
DR Ensembl; ENSMUST00000160694; ENSMUSP00000125571; ENSMUSG00000004891. [Q6P5H2-2]
DR GeneID; 18008; -.
DR KEGG; mmu:18008; -.
DR UCSC; uc008ptm.1; mouse. [Q6P5H2-2]
DR UCSC; uc008ptn.1; mouse. [Q6P5H2-1]
DR CTD; 10763; -.
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; 127811at2759; -.
DR PhylomeDB; Q6P5H2; -.
DR TreeFam; TF336633; -.
DR BioGRID-ORCS; 18008; 4 hits in 72 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 250 other tissues.
DR Genevisible; Q6P5H2; MM.
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:0043086; P:negative regulation of catalytic activity; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO: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 InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR031211; Nestin.
DR PANTHER; PTHR47051; PTHR47051; 4.
DR Pfam; PF00038; Filament; 1.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
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
