NDE1_MOUSE
ID NDE1_MOUSE Reviewed; 344 AA.
AC Q9CZA6; Q3UBS6; Q3UIC1; Q9ERR0;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Nuclear distribution protein nudE homolog 1;
DE Short=NudE;
DE Short=mNudE;
GN Name=Nde1; Synonyms=Nude;
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), INTERACTION WITH CENPF; CNTRL;
RP DYNEIN; LIS1; TUBULIN GAMMA; PAFAH1B1; PCNT; SLMAP AND TCP1, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11163258; DOI=10.1016/s0896-6273(00)00145-8;
RA Feng Y., Olson E.C., Stukenberg P.T., Flanagan L.A., Kirschner M.W.,
RA Walsh C.A.;
RT "LIS1 regulates CNS lamination by interacting with mNudE, a central
RT component of the centrosome.";
RL Neuron 28:665-679(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), INTERACTION WITH PAFAH1B1, AND
RP TISSUE SPECIFICITY.
RX PubMed=11163259; DOI=10.1016/s0896-6273(00)00146-x;
RA Sasaki S., Shionoya A., Ishida M., Gambello M.J., Yingling J.,
RA Wynshaw-Boris A., Hirotsune S.;
RT "A LIS1/NUDEL/cytoplasmic dynein heavy chain complex in the developing and
RT adult nervous system.";
RL Neuron 28:681-696(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Embryo, Embryonic kidney, and Thymus;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=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 [5]
RP FUNCTION, SELF-ASSOCIATION, INTERACTION WITH PAFAH1B1, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=15473967; DOI=10.1016/j.neuron.2004.09.023;
RA Feng Y., Walsh C.A.;
RT "Mitotic spindle regulation by Nde1 controls cerebral cortical size.";
RL Neuron 44:279-293(2004).
RN [6]
RP INTERACTION WITH CENPF, AND SUBCELLULAR LOCATION.
RX PubMed=15939891; DOI=10.1073/pnas.0502303102;
RA Soukoulis V., Reddy S., Pooley R.D., Feng Y., Walsh C.A., Bader D.M.;
RT "Cytoplasmic LEK1 is a regulator of microtubule function through its
RT interaction with the LIS1 pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:8549-8554(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [8]
RP PHOSPHORYLATION AT THR-246.
RX PubMed=21529751; DOI=10.1016/j.ajhg.2011.04.003;
RA Alkuraya F.S., Cai X., Emery C., Mochida G.H., Al-Dosari M.S., Felie J.M.,
RA Hill R.S., Barry B.J., Partlow J.N., Gascon G.G., Kentab A., Jan M.,
RA Shaheen R., Feng Y., Walsh C.A.;
RT "Human mutations in NDE1 cause extreme microcephaly with lissencephaly.";
RL Am. J. Hum. Genet. 88:536-547(2011).
RN [9]
RP ERRATUM OF PUBMED:21529751.
RA Alkuraya F.S., Cai X., Emery C., Mochida G.H., Al-Dosari M.S., Felie J.M.,
RA Hill R.S., Barry B.J., Partlow J.N., Gascon G.G., Kentab A., Jan M.,
RA Shaheen R., Feng Y., Walsh C.A.;
RL Am. J. Hum. Genet. 88:677-677(2011).
CC -!- FUNCTION: Required for centrosome duplication and formation and
CC function of the mitotic spindle. Essential for the development of the
CC cerebral cortex. May regulate the production of neurons by controlling
CC the orientation of the mitotic spindle during division of cortical
CC neuronal progenitors of the proliferative ventricular zone of the
CC brain. Orientation of the division plane perpendicular to the layers of
CC the cortex gives rise to two proliferative neuronal progenitors whereas
CC parallel orientation of the division plane yields one proliferative
CC neuronal progenitor and a post-mitotic neuron. A premature shift
CC towards a neuronal fate within the progenitor population may result in
CC an overall reduction in the final number of neurons and an increase in
CC the number of neurons in the deeper layers of the cortex.
CC {ECO:0000269|PubMed:15473967}.
CC -!- SUBUNIT: Interacts with dynactin and PCM1 (By similarity). Self-
CC associates. Interacts with CENPF, LIS1, CNTRL, dynein, tubulin gamma,
CC PAFAH1B1, PCNT, SLMAP and TCP1. Interacts with ZNF365 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9CZA6; Q155P7: Cenpf; NbExp=8; IntAct=EBI-309934, EBI-2211248;
CC Q9CZA6; Q9NRI5: DISC1; Xeno; NbExp=2; IntAct=EBI-309934, EBI-529989;
CC Q9CZA6; O14576: DYNC1I1; Xeno; NbExp=2; IntAct=EBI-309934, EBI-366267;
CC Q9CZA6; P43034: PAFAH1B1; Xeno; NbExp=6; IntAct=EBI-309934, EBI-720620;
CC Q9CZA6-1; P11531: Dmd; NbExp=2; IntAct=EBI-15949673, EBI-295928;
CC Q9CZA6-1; E9Q6R7: Utrn; NbExp=4; IntAct=EBI-15949673, EBI-15949679;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome. Cytoplasm, cytoskeleton,
CC spindle. Chromosome, centromere, kinetochore. Cleavage furrow.
CC Note=Localizes to the interphase and S phase centrosome. During
CC mitosis, partially associated with the mitotic spindle. Concentrates at
CC the plus ends of microtubules coincident with kinetochores in metaphase
CC and anaphase in a CENPF-dependent manner. Also localizes to the
CC cleavage furrow during cytokinesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9CZA6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CZA6-2; Sequence=VSP_019307, VSP_019309;
CC Name=3;
CC IsoId=Q9CZA6-3; Sequence=VSP_019308, VSP_019309;
CC Name=4;
CC IsoId=Q9CZA6-4; Sequence=VSP_019306;
CC -!- TISSUE SPECIFICITY: Highly expressed in ovary. Also expressed in brain,
CC heart, kidney, large intestine, liver, lung, small intestine and
CC testis. {ECO:0000269|PubMed:11163258, ECO:0000269|PubMed:11163259}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed in the developing brain,
CC particularly in the neural progenitor cells of ventricular zone and the
CC intermediate zone of the cerebral cortex. Expression peaks at 11 dpc
CC and declines at 15 dpc and 17 dpc. After completion of neuronal
CC migration expression is reduced in the cortex.
CC {ECO:0000269|PubMed:11163258, ECO:0000269|PubMed:15473967}.
CC -!- PTM: Phosphorylated in mitosis (By similarity). Phosphorylation at Thr-
CC 246 is essential for the G2/M transition. {ECO:0000250,
CC ECO:0000269|PubMed:21529751}.
CC -!- MISCELLANEOUS: Homozygous loss of this protein results in microcephaly
CC that preferentially affects the cerebral cortex. Affected animals have
CC a smaller cortex with reduced superficial cortical layers, although
CC cortical lamination is mostly preserved. The smaller cortex size seems
CC to reflect both reduced progenitor cell division and altered
CC specification of cell fates following progenitor cell division.
CC -!- SIMILARITY: Belongs to the nudE family. {ECO:0000305}.
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DR EMBL; AF322073; AAK08067.1; -; mRNA.
DR EMBL; AF290473; AAG10062.1; -; mRNA.
DR EMBL; AK012830; BAB28499.1; -; mRNA.
DR EMBL; AK037289; BAE20509.1; -; mRNA.
DR EMBL; AK146982; BAE27585.1; -; mRNA.
DR EMBL; AK150826; BAE29888.1; -; mRNA.
DR EMBL; AK169743; BAE41342.1; -; mRNA.
DR EMBL; BC023267; AAH23267.1; -; mRNA.
DR CCDS; CCDS37263.2; -. [Q9CZA6-1]
DR CCDS; CCDS49770.1; -. [Q9CZA6-3]
DR CCDS; CCDS70688.1; -. [Q9CZA6-2]
DR RefSeq; NP_001107557.1; NM_001114085.1. [Q9CZA6-3]
DR RefSeq; NP_001272432.1; NM_001285503.1. [Q9CZA6-2]
DR RefSeq; NP_001272433.1; NM_001285504.1. [Q9CZA6-4]
DR RefSeq; NP_075806.2; NM_023317.2. [Q9CZA6-1]
DR RefSeq; XP_011244302.1; XM_011246000.1.
DR AlphaFoldDB; Q9CZA6; -.
DR SMR; Q9CZA6; -.
DR BioGRID; 212013; 21.
DR DIP; DIP-54638N; -.
DR IntAct; Q9CZA6; 20.
DR MINT; Q9CZA6; -.
DR STRING; 10090.ENSMUSP00000023359; -.
DR iPTMnet; Q9CZA6; -.
DR PhosphoSitePlus; Q9CZA6; -.
DR SwissPalm; Q9CZA6; -.
DR EPD; Q9CZA6; -.
DR jPOST; Q9CZA6; -.
DR MaxQB; Q9CZA6; -.
DR PaxDb; Q9CZA6; -.
DR PeptideAtlas; Q9CZA6; -.
DR PRIDE; Q9CZA6; -.
DR ProteomicsDB; 287619; -. [Q9CZA6-1]
DR ProteomicsDB; 287620; -. [Q9CZA6-2]
DR ProteomicsDB; 287621; -. [Q9CZA6-3]
DR ProteomicsDB; 287622; -. [Q9CZA6-4]
DR Antibodypedia; 11751; 283 antibodies from 31 providers.
DR Ensembl; ENSMUST00000023359; ENSMUSP00000023359; ENSMUSG00000022678. [Q9CZA6-1]
DR Ensembl; ENSMUST00000115795; ENSMUSP00000111461; ENSMUSG00000022678. [Q9CZA6-2]
DR Ensembl; ENSMUST00000117958; ENSMUSP00000112817; ENSMUSG00000022678. [Q9CZA6-3]
DR GeneID; 67203; -.
DR KEGG; mmu:67203; -.
DR UCSC; uc007ygy.2; mouse. [Q9CZA6-1]
DR UCSC; uc007yha.2; mouse. [Q9CZA6-3]
DR UCSC; uc007yhb.3; mouse. [Q9CZA6-2]
DR CTD; 54820; -.
DR MGI; MGI:1914453; Nde1.
DR VEuPathDB; HostDB:ENSMUSG00000022678; -.
DR eggNOG; KOG1853; Eukaryota.
DR GeneTree; ENSGT00390000000111; -.
DR HOGENOM; CLU_057872_1_0_1; -.
DR InParanoid; Q9CZA6; -.
DR OMA; EQTVNRR; -.
DR OrthoDB; 1082224at2759; -.
DR PhylomeDB; Q9CZA6; -.
DR TreeFam; TF325693; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 67203; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Nde1; mouse.
DR PRO; PR:Q9CZA6; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9CZA6; protein.
DR Bgee; ENSMUSG00000022678; Expressed in ventricular zone and 265 other tissues.
DR ExpressionAtlas; Q9CZA6; baseline and differential.
DR Genevisible; Q9CZA6; MM.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:MGI.
DR GO; GO:0031616; C:spindle pole centrosome; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0008017; F:microtubule binding; IMP:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0051298; P:centrosome duplication; IMP:UniProtKB.
DR GO; GO:0051642; P:centrosome localization; IBA:GO_Central.
DR GO; GO:0021987; P:cerebral cortex development; IGI:MGI.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0051303; P:establishment of chromosome localization; ISO:MGI.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISO:MGI.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0007020; P:microtubule nucleation; IDA:MGI.
DR GO; GO:0031023; P:microtubule organizing center organization; IMP:UniProtKB.
DR GO; GO:0007100; P:mitotic centrosome separation; IBA:GO_Central.
DR GO; GO:0007405; P:neuroblast proliferation; IMP:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:UniProtKB.
DR GO; GO:0047496; P:vesicle transport along microtubule; IGI:MGI.
DR InterPro; IPR033494; NUDE.
DR InterPro; IPR006964; NUDE_dom.
DR PANTHER; PTHR10921; PTHR10921; 1.
DR Pfam; PF04880; NUDE_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; Kinetochore; Lipoprotein; Microtubule; Mitosis;
KW Neurogenesis; Palmitate; Phosphoprotein; Reference proteome.
FT CHAIN 1..344
FT /note="Nuclear distribution protein nudE homolog 1"
FT /id="PRO_0000240203"
FT REGION 1..93
FT /note="Self-association"
FT REGION 88..156
FT /note="Interaction with PAFAH1B1"
FT REGION 167..290
FT /note="Interaction with CENPF"
FT REGION 181..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 18..188
FT /evidence="ECO:0000255"
FT COMPBIAS 202..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXR1"
FT MOD_RES 215
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXR1"
FT MOD_RES 228
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXR1"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXR1"
FT MOD_RES 243
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXR1"
FT MOD_RES 246
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:21529751"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXR1"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXR1"
FT LIPID 274
FT /note="S-palmitoyl cysteine; by ZDHHC2, ZDHHC3 and ZDHHC7"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..132
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11163259"
FT /id="VSP_019306"
FT VAR_SEQ 315..317
FT /note="SGK -> REN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019307"
FT VAR_SEQ 316..317
FT /note="GK -> LP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019308"
FT VAR_SEQ 318..344
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019309"
SQ SEQUENCE 344 AA; 38523 MW; C0A339C4F51EF8D9 CRC64;
MEDSGKTFES EEEETNYWRD LAMTYKQRAE NTQEELREFQ EGSREYEAEL EAQLQQIETR
NRDLLSENNR LRMELESVKE KFEMQHSEGY RQISALEDDL AQTKAIKDQL QKYIRELEQA
NDDLERAKRA TIMSLEDFEQ RLNQAIERNA FLESELDEKE NLLESVQRLK DEARDLRQEL
AVQQKQDKPR TPMPGSGQAK RTDMAVQATG SVPSTPVAHR GPSSGLNTPG MFRRGLDSST
SGTPLTPAAR ISALNIVGDL LRKVGALESK LASCRNFMYD QSPSRTSGPA SGRGTKNRDG
VDRRPGSTSV GDKGSGKRLE FGKPASEPAS PALPSAQGVV KLLL
