NDEL1_HUMAN
ID NDEL1_HUMAN Reviewed; 345 AA.
AC Q9GZM8; B3KP93; D3DTS0; J3QT32; Q86T80; Q8TAR7; Q9UH50;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Nuclear distribution protein nudE-like 1;
DE Short=Protein Nudel;
DE AltName: Full=Mitosin-associated protein 1;
GN Name=NDEL1; Synonyms=EOPA, MITAP1, NUDEL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DYNEIN AND
RP PAFAH1B1, SUBCELLULAR LOCATION, PHOSPHORYLATION BY CDK5, AND MUTAGENESIS OF
RP SER-198; THR-219 AND SER-231.
RC TISSUE=Brain;
RX PubMed=11163260; DOI=10.1016/s0896-6273(00)00147-1;
RA Niethammer M., Smith D.S., Ayala R., Peng J., Ko J., Lee M.-S.,
RA Morabito M., Tsai L.-H.;
RT "NUDEL is a novel cdk5 substrate that associates with LIS1 and cytoplasmic
RT dynein.";
RL Neuron 28:697-711(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
RP PAFAH1B1, SUBCELLULAR LOCATION, PHOSPHORYLATION BY CDK1 AND MAPK1, AND
RP MUTAGENESIS OF SER-198; THR-219; SER-231; SER-242 AND THR-245.
RX PubMed=12556484; DOI=10.1128/mcb.23.4.1239-1250.2003;
RA Yan X., Li F., Liang Y., Shen Y., Zhao X., Huang Q., Zhu X.;
RT "Human Nudel and NudE as regulators of cytoplasmic dynein in poleward
RT protein transport along the mitotic spindle.";
RL Mol. Cell. Biol. 23:1239-1250(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PUTATIVE FUNCTION AS AN
RP OLIGOPEPTIDASE, INTERACTION WITH DISC1, AND MUTAGENESIS OF CYS-273.
RC TISSUE=Brain;
RX PubMed=15728732; DOI=10.1073/pnas.0500330102;
RA Hayashi M.A.F., Portaro F.C.V., Bastos M.F., Guerreiro J.R., Oliveira V.,
RA Gorrao S.S., Tambourgi D.V., Sant'Anna O.A., Whiting P.J., Camargo L.M.,
RA Konno K., Brandon N.J., de Camargo A.C.M.;
RT "Inhibition of NUDEL (nuclear distribution element-like)-oligopeptidase
RT activity by disrupted-in-schizophrenia 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3828-3833(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 152-328 (ISOFORM 3).
RC TISSUE=Caudate nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spinal cord;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC 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 [9]
RP INTERACTION WITH DISC1, AND SUBCELLULAR LOCATION.
RX PubMed=12812986; DOI=10.1093/hmg/ddg162;
RA Morris J.A., Kandpal G., Ma L., Austin C.P.;
RT "DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein
RT that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of
RT interaction with mutation.";
RL Hum. Mol. Genet. 12:1591-1608(2003).
RN [10]
RP INTERACTION WITH DISC1.
RX PubMed=12506198; DOI=10.1073/pnas.0136913100;
RA Ozeki Y., Tomoda T., Kleiderlein J., Kamiya A., Bord L., Fujii K.,
RA Okawa M., Yamada N., Hatten M.E., Snyder S.H., Ross C.A., Sawa A.;
RT "Disrupted-in-Schizophrenia-1 (DISC-1): mutant truncation prevents binding
RT to NudE-like (NUDEL) and inhibits neurite outgrowth.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:289-294(2003).
RN [11]
RP ERRATUM OF PUBMED:12506198.
RA Ozeki Y., Tomoda T., Kleiderlein J., Kamiya A., Bord L., Fujii K.,
RA Okawa M., Yamada N., Hatten M.E., Snyder S.H., Ross C.A., Sawa A.;
RL Proc. Natl. Acad. Sci. U.S.A. 101:13969-13969(2004).
RN [12]
RP FUNCTION, SELF-ASSOCIATION, INTERACTION WITH DYNACTIN; DYNEIN AND PAFAH1B1,
RP AND SUBCELLULAR LOCATION.
RX PubMed=14970193; DOI=10.1083/jcb.200308058;
RA Liang Y., Yu W., Li Y., Yang Z., Yan X., Huang Q., Zhu X.;
RT "Nudel functions in membrane traffic mainly through association with Lis1
RT and cytoplasmic dynein.";
RL J. Cell Biol. 164:557-566(2004).
RN [13]
RP INTERACTION WITH DISC1.
RX PubMed=14962739; DOI=10.1016/j.mcn.2003.09.009;
RA Brandon N.J., Handford E.J., Schurov I., Rain J.-C., Pelling M.,
RA Duran-Jimeniz B., Camargo L.M., Oliver K.R., Beher D., Shearman M.S.,
RA Whiting P.J.;
RT "Disrupted in Schizophrenia 1 and Nudel form a neurodevelopmentally
RT regulated protein complex: implications for schizophrenia and other major
RT neurological disorders.";
RL Mol. Cell. Neurosci. 25:42-55(2004).
RN [14]
RP SELF-ASSOCIATION, AND INTERACTION WITH PAFAH1B1.
RX PubMed=15572112; DOI=10.1016/j.neuron.2004.11.019;
RA Tarricone C., Perrina F., Monzani S., Massimiliano L., Kim M.-H.,
RA Derewenda Z.S., Knapp S., Tsai L.-H., Musacchio A.;
RT "Coupling PAF signaling to dynein regulation: structure of LIS1 in complex
RT with PAF-acetylhydrolase.";
RL Neuron 44:809-821(2004).
RN [15]
RP TISSUE SPECIFICITY.
RX PubMed=16005531; DOI=10.1016/j.bbaexp.2005.06.001;
RA Guerreiro J.R., Winnischofer S.M.B., Bastos M.F., Portaro F.C.V.,
RA Sogayar M.C., de Camargo A.C.M., Hayashi M.A.F.;
RT "Cloning and characterization of the human and rabbit NUDEL-oligopeptidase
RT promoters and their negative regulation.";
RL Biochim. Biophys. Acta 1730:77-84(2005).
RN [16]
RP INTERACTION WITH KATNA1 AND KATNB1, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND PHOSPHORYLATION.
RX PubMed=16203747; DOI=10.1093/hmg/ddi339;
RA Toyo-Oka K., Sasaki S., Yano Y., Mori D., Kobayashi T., Toyoshima Y.Y.,
RA Tokuoka S.M., Ishii S., Shimizu T., Muramatsu M., Hiraiwa N., Yoshiki A.,
RA Wynshaw-Boris A., Hirotsune S.;
RT "Recruitment of katanin p60 by phosphorylated NDEL1, an LIS1 interacting
RT protein, is essential for mitotic cell division and neuronal migration.";
RL Hum. Mol. Genet. 14:3113-3128(2005).
RN [17]
RP INTERACTION WITH DISC1, AND MUTAGENESIS OF LEU-266 AND GLU-267.
RX PubMed=17035248; DOI=10.1093/hmg/ddl407;
RA Kamiya A., Tomoda T., Chang J., Takaki M., Zhan C., Morita M., Cascio M.B.,
RA Elashvili S., Koizumi H., Takanezawa Y., Dickerson F., Yolken R., Arai H.,
RA Sawa A.;
RT "DISC1-NDEL1/NUDEL protein interaction, an essential component for neurite
RT outgrowth, is modulated by genetic variations of DISC1.";
RL Hum. Mol. Genet. 15:3313-3323(2006).
RN [18]
RP FUNCTION, INTERACTION WITH DYNACTIN; TUBULIN GAMMA; PAFAH1B1; PCM1; PCNT,
RP AND SUBCELLULAR LOCATION.
RX PubMed=16291865; DOI=10.1091/mbc.e05-04-0360;
RA Guo J., Yang Z., Song W., Chen Q., Wang F., Zhang Q., Zhu X.;
RT "Nudel contributes to microtubule anchoring at the mother centriole and is
RT involved in both dynein-dependent and -independent centrosomal protein
RT assembly.";
RL Mol. Biol. Cell 17:680-689(2006).
RN [19]
RP INTERACTION WITH ZNF365.
RX PubMed=16682949; DOI=10.1038/sj.onc.1209637;
RA Hirohashi Y., Wang Q., Liu Q., Li B., Du X., Zhang H., Furuuchi K.,
RA Masuda K., Sato N., Greene M.I.;
RT "Centrosomal proteins Nde1 and Su48 form a complex regulated by
RT phosphorylation.";
RL Oncogene 25:6048-6055(2006).
RN [20]
RP FUNCTION, INTERACTION WITH CENPF, AND SUBCELLULAR LOCATION.
RX PubMed=17600710; DOI=10.1016/j.cub.2007.05.077;
RA Vergnolle M.A.S., Taylor S.S.;
RT "Cenp-F links kinetochores to Ndel1/Nde1/Lis1/dynein microtubule motor
RT complexes.";
RL Curr. Biol. 17:1173-1179(2007).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; THR-219 AND THR-245, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [23]
RP PALMITOYLATION AT CYS-273 BY ZDHHC2; ZDHHC3 AND ZDHHC7.
RX PubMed=19927128; DOI=10.1038/emboj.2009.325;
RA Shmueli A., Segal M., Sapir T., Tsutsumi R., Noritake J., Bar A.,
RA Sapoznik S., Fukata Y., Orr I., Fukata M., Reiner O.;
RT "Ndel1 palmitoylation: a new mean to regulate cytoplasmic dynein
RT activity.";
RL EMBO J. 29:107-119(2010).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; THR-219; SER-242 AND
RP THR-245, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215 AND SER-231, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Required for organization of the cellular microtubule array
CC and microtubule anchoring at the centrosome. May regulate microtubule
CC organization at least in part by targeting the microtubule severing
CC protein KATNA1 to the centrosome. Also positively regulates the
CC activity of the minus-end directed microtubule motor protein dynein.
CC May enhance dynein-mediated microtubule sliding by targeting dynein to
CC the microtubule plus ends. Required for several dynein- and
CC microtubule-dependent processes such as the maintenance of Golgi
CC integrity, the centripetal motion of secretory vesicles and the
CC coupling of the nucleus and centrosome. Also required during brain
CC development for the migration of newly formed neurons from the
CC ventricular/subventricular zone toward the cortical plate. Plays a
CC role, together with DISC1, in the regulation of neurite outgrowth.
CC Required for mitosis in some cell types but appears to be dispensible
CC for mitosis in cortical neuronal progenitors, which instead requires
CC NDE1. Facilitates the polymerization of neurofilaments from the
CC individual subunits NEFH and NEFL. Positively regulates lysosome
CC peripheral distribution and ruffled border formation in osteoclasts (By
CC similarity). {ECO:0000250|UniProtKB:Q9ERR1,
CC ECO:0000269|PubMed:12556484, ECO:0000269|PubMed:14970193,
CC ECO:0000269|PubMed:16291865, ECO:0000269|PubMed:17600710}.
CC -!- SUBUNIT: Interacts with PLEKHM1 (via N- and C-terminus) (By
CC similarity). Interacts with YWHAE. Interacts directly with NEFL and
CC indirectly with NEFH. Interacts with microtubules (By similarity).
CC Self-associates. Interacts with DISC1, dynein, dynactin, tubulin gamma,
CC KATNA1, KATNB1, PAFAH1B1, PCM1 and PCNT. Interacts (via C-terminus)
CC with CENPF. Interacts with ZNF365. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9ERR1, ECO:0000269|PubMed:11163260,
CC ECO:0000269|PubMed:12506198, ECO:0000269|PubMed:12556484,
CC ECO:0000269|PubMed:12812986, ECO:0000269|PubMed:14962739,
CC ECO:0000269|PubMed:14970193, ECO:0000269|PubMed:15572112,
CC ECO:0000269|PubMed:15728732, ECO:0000269|PubMed:16203747,
CC ECO:0000269|PubMed:16291865, ECO:0000269|PubMed:16682949,
CC ECO:0000269|PubMed:17035248, ECO:0000269|PubMed:17600710}.
CC -!- INTERACTION:
CC Q9GZM8; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-928842, EBI-742038;
CC Q9GZM8; Q13155: AIMP2; NbExp=3; IntAct=EBI-928842, EBI-745226;
CC Q9GZM8; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-928842, EBI-2548012;
CC Q9GZM8; P35226: BMI1; NbExp=3; IntAct=EBI-928842, EBI-2341576;
CC Q9GZM8; Q96GS4: BORCS6; NbExp=3; IntAct=EBI-928842, EBI-10193358;
CC Q9GZM8; Q8WUW1: BRK1; NbExp=7; IntAct=EBI-928842, EBI-2837444;
CC Q9GZM8; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-928842, EBI-10175300;
CC Q9GZM8; P49454: CENPF; NbExp=6; IntAct=EBI-928842, EBI-968343;
CC Q9GZM8; P28329-3: CHAT; NbExp=3; IntAct=EBI-928842, EBI-25837549;
CC Q9GZM8; Q5SYC1: CLVS2; NbExp=3; IntAct=EBI-928842, EBI-12357161;
CC Q9GZM8; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-928842, EBI-5453285;
CC Q9GZM8; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-928842, EBI-742054;
CC Q9GZM8; Q9NRI5: DISC1; NbExp=12; IntAct=EBI-928842, EBI-529989;
CC Q9GZM8; Q9NRI5-1: DISC1; NbExp=4; IntAct=EBI-928842, EBI-15881455;
CC Q9GZM8; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-928842, EBI-11988027;
CC Q9GZM8; O60941: DTNB; NbExp=3; IntAct=EBI-928842, EBI-740402;
CC Q9GZM8; P22607: FGFR3; NbExp=3; IntAct=EBI-928842, EBI-348399;
CC Q9GZM8; Q08379: GOLGA2; NbExp=3; IntAct=EBI-928842, EBI-618309;
CC Q9GZM8; P06396: GSN; NbExp=3; IntAct=EBI-928842, EBI-351506;
CC Q9GZM8; P01112: HRAS; NbExp=3; IntAct=EBI-928842, EBI-350145;
CC Q9GZM8; Q16891-1: IMMT; NbExp=4; IntAct=EBI-928842, EBI-11614103;
CC Q9GZM8; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-928842, EBI-2125614;
CC Q9GZM8; Q6A162: KRT40; NbExp=3; IntAct=EBI-928842, EBI-10171697;
CC Q9GZM8; Q9NS73-5: MBIP; NbExp=3; IntAct=EBI-928842, EBI-10182361;
CC Q9GZM8; Q9P086: MED11; NbExp=3; IntAct=EBI-928842, EBI-394704;
CC Q9GZM8; Q9NYP9: MIS18A; NbExp=5; IntAct=EBI-928842, EBI-1104552;
CC Q9GZM8; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-928842, EBI-742948;
CC Q9GZM8; O14777: NDC80; NbExp=4; IntAct=EBI-928842, EBI-715849;
CC Q9GZM8; Q9NXR1: NDE1; NbExp=2; IntAct=EBI-928842, EBI-941227;
CC Q9GZM8; Q9GZM8: NDEL1; NbExp=14; IntAct=EBI-928842, EBI-928842;
CC Q9GZM8; P43034: PAFAH1B1; NbExp=3; IntAct=EBI-928842, EBI-720620;
CC Q9GZM8; Q9HBI0: PARVG; NbExp=3; IntAct=EBI-928842, EBI-3921217;
CC Q9GZM8; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-928842, EBI-79165;
CC Q9GZM8; Q99959: PKP2; NbExp=4; IntAct=EBI-928842, EBI-702235;
CC Q9GZM8; Q99959-2: PKP2; NbExp=3; IntAct=EBI-928842, EBI-10987518;
CC Q9GZM8; P49023-2: PXN; NbExp=5; IntAct=EBI-928842, EBI-11954250;
CC Q9GZM8; O75971: SNAPC5; NbExp=3; IntAct=EBI-928842, EBI-749483;
CC Q9GZM8; O75971-2: SNAPC5; NbExp=3; IntAct=EBI-928842, EBI-12004298;
CC Q9GZM8; Q9Y6A5: TACC3; NbExp=3; IntAct=EBI-928842, EBI-2554984;
CC Q9GZM8; Q9Y228: TRAF3IP3; NbExp=6; IntAct=EBI-928842, EBI-765817;
CC Q9GZM8; P14373: TRIM27; NbExp=7; IntAct=EBI-928842, EBI-719493;
CC Q9GZM8; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-928842, EBI-741480;
CC Q9GZM8; O75604: USP2; NbExp=6; IntAct=EBI-928842, EBI-743272;
CC Q9GZM8; P23025: XPA; NbExp=6; IntAct=EBI-928842, EBI-295222;
CC Q9GZM8; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-928842, EBI-14104088;
CC Q9GZM8; P17014: ZNF12; NbExp=3; IntAct=EBI-928842, EBI-11278550;
CC Q9GZM8; Q9UJW8: ZNF180; NbExp=4; IntAct=EBI-928842, EBI-10322527;
CC Q9GZM8; P15622-3: ZNF250; NbExp=5; IntAct=EBI-928842, EBI-10177272;
CC Q9GZM8; Q3ZCT1: ZNF260; NbExp=3; IntAct=EBI-928842, EBI-10241410;
CC Q9GZM8; Q14C61: ZNF264; NbExp=3; IntAct=EBI-928842, EBI-2826570;
CC Q9GZM8; P17036: ZNF3; NbExp=3; IntAct=EBI-928842, EBI-1640965;
CC Q9GZM8; P13682: ZNF35; NbExp=3; IntAct=EBI-928842, EBI-11041653;
CC Q9GZM8; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-928842, EBI-740727;
CC Q9GZM8; Q9ULM2: ZNF490; NbExp=6; IntAct=EBI-928842, EBI-1105370;
CC Q9GZM8; Q6NX49: ZNF544; NbExp=5; IntAct=EBI-928842, EBI-2841978;
CC Q9GZM8; Q68EA5: ZNF57; NbExp=3; IntAct=EBI-928842, EBI-8490788;
CC Q9GZM8; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-928842, EBI-10172590;
CC Q9GZM8; Q96NL3: ZNF599; NbExp=6; IntAct=EBI-928842, EBI-8653994;
CC Q9GZM8; Q6ZS27-3: ZNF662; NbExp=3; IntAct=EBI-928842, EBI-10255155;
CC Q9GZM8; Q96C28: ZNF707; NbExp=3; IntAct=EBI-928842, EBI-748111;
CC Q9GZM8; Q08AG5: ZNF844; NbExp=6; IntAct=EBI-928842, EBI-10225757;
CC Q9GZM8; P63005: Pafah1b1; Xeno; NbExp=4; IntAct=EBI-928842, EBI-917499;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome. Chromosome, centromere,
CC kinetochore. Cytoplasm, cytoskeleton, spindle. Note=Localizes to the
CC cell body of the motor neurons and colocalizes with assembled
CC neurofilaments within axonal processes. Localizes to the microtubules
CC of the manchette in elongated spermatids. Colocalizes with DISC1 in the
CC perinuclear region, including the centrosome (By similarity). Localizes
CC to the interphase centrosome and the mitotic spindle. Localizes to the
CC kinetochore in a CENPF-dependent manner. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9GZM8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9GZM8-2; Sequence=VSP_019310;
CC Name=3;
CC IsoId=Q9GZM8-3; Sequence=VSP_047509;
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung,
CC pancreas, placenta and skeletal muscle. {ECO:0000269|PubMed:16005531}.
CC -!- DEVELOPMENTAL STAGE: Expression peaks in mitosis.
CC {ECO:0000269|PubMed:16203747}.
CC -!- PTM: Phosphorylated in mitosis. Can be phosphorylated by CDK1, CDK5 and
CC MAPK1. Phosphorylation by CDK5 promotes interaction with KATNA1 and
CC YWHAE. {ECO:0000269|PubMed:11163260, ECO:0000269|PubMed:12556484,
CC ECO:0000269|PubMed:16203747}.
CC -!- PTM: Palmitoylation at Cys-273 reduces affinity for dynein.
CC {ECO:0000269|PubMed:19927128}.
CC -!- SIMILARITY: Belongs to the nudE family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to function as an oligopeptidase
CC (NUDEL-oligopeptidase or endooligopeptidase A) which could regulate
CC peptide levels relevant to brain function.
CC {ECO:0000305|PubMed:15728732}.
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DR EMBL; AY004871; AAF97497.1; -; mRNA.
DR EMBL; AF182078; AAG43425.1; -; mRNA.
DR EMBL; AF217798; AAF24516.3; -; mRNA.
DR EMBL; AK056014; BAG51605.1; -; mRNA.
DR EMBL; DA256375; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL832648; CAD89957.3; -; mRNA.
DR EMBL; AC026130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471108; EAW90051.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90052.1; -; Genomic_DNA.
DR EMBL; BC026101; AAH26101.1; -; mRNA.
DR CCDS; CCDS11143.1; -. [Q9GZM8-1]
DR CCDS; CCDS32564.1; -. [Q9GZM8-3]
DR RefSeq; NP_001020750.1; NM_001025579.2. [Q9GZM8-3]
DR RefSeq; NP_110435.1; NM_030808.4. [Q9GZM8-1]
DR RefSeq; XP_016880674.1; XM_017025185.1. [Q9GZM8-1]
DR RefSeq; XP_016880676.1; XM_017025187.1. [Q9GZM8-3]
DR PDB; 2V66; X-ray; 2.10 A; B/C/D/E=58-168.
DR PDBsum; 2V66; -.
DR AlphaFoldDB; Q9GZM8; -.
DR SMR; Q9GZM8; -.
DR BioGRID; 123527; 156.
DR DIP; DIP-29554N; -.
DR IntAct; Q9GZM8; 163.
DR MINT; Q9GZM8; -.
DR STRING; 9606.ENSP00000333982; -.
DR MoonDB; Q9GZM8; Predicted.
DR iPTMnet; Q9GZM8; -.
DR PhosphoSitePlus; Q9GZM8; -.
DR SwissPalm; Q9GZM8; -.
DR BioMuta; NDEL1; -.
DR DMDM; 74725006; -.
DR EPD; Q9GZM8; -.
DR jPOST; Q9GZM8; -.
DR MassIVE; Q9GZM8; -.
DR MaxQB; Q9GZM8; -.
DR PaxDb; Q9GZM8; -.
DR PeptideAtlas; Q9GZM8; -.
DR PRIDE; Q9GZM8; -.
DR ProteomicsDB; 80092; -. [Q9GZM8-1]
DR ProteomicsDB; 80093; -. [Q9GZM8-2]
DR Antibodypedia; 12558; 511 antibodies from 38 providers.
DR DNASU; 81565; -.
DR Ensembl; ENST00000334527.12; ENSP00000333982.7; ENSG00000166579.16. [Q9GZM8-1]
DR Ensembl; ENST00000402554.7; ENSP00000384963.3; ENSG00000166579.16. [Q9GZM8-3]
DR GeneID; 81565; -.
DR KEGG; hsa:81565; -.
DR MANE-Select; ENST00000334527.12; ENSP00000333982.7; NM_030808.5; NP_110435.1.
DR UCSC; uc002gli.5; human. [Q9GZM8-1]
DR CTD; 81565; -.
DR DisGeNET; 81565; -.
DR GeneCards; NDEL1; -.
DR HGNC; HGNC:17620; NDEL1.
DR HPA; ENSG00000166579; Low tissue specificity.
DR MIM; 607538; gene.
DR neXtProt; NX_Q9GZM8; -.
DR OpenTargets; ENSG00000166579; -.
DR PharmGKB; PA134887314; -.
DR VEuPathDB; HostDB:ENSG00000166579; -.
DR eggNOG; KOG1853; Eukaryota.
DR GeneTree; ENSGT00390000000111; -.
DR HOGENOM; CLU_057872_1_0_1; -.
DR InParanoid; Q9GZM8; -.
DR OMA; KTYREHA; -.
DR OrthoDB; 1082224at2759; -.
DR PhylomeDB; Q9GZM8; -.
DR TreeFam; TF325693; -.
DR PathwayCommons; Q9GZM8; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q9GZM8; -.
DR SIGNOR; Q9GZM8; -.
DR BioGRID-ORCS; 81565; 16 hits in 1086 CRISPR screens.
DR ChiTaRS; NDEL1; human.
DR EvolutionaryTrace; Q9GZM8; -.
DR GeneWiki; NDEL1; -.
DR GenomeRNAi; 81565; -.
DR Pharos; Q9GZM8; Tbio.
DR PRO; PR:Q9GZM8; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9GZM8; protein.
DR Bgee; ENSG00000166579; Expressed in adrenal tissue and 203 other tissues.
DR ExpressionAtlas; Q9GZM8; baseline and differential.
DR Genevisible; Q9GZM8; HS.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0043203; C:axon hillock; IEA:Ensembl.
DR GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
DR GO; GO:0090724; C:central region of growth cone; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0060053; C:neurofilament cytoskeleton; IEA:Ensembl.
DR GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
DR GO; GO:0043014; F:alpha-tubulin binding; IEA:Ensembl.
DR GO; GO:0048487; F:beta-tubulin binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0070012; F:oligopeptidase activity; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0090630; P:activation of GTPase activity; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0021955; P:central nervous system neuron axonogenesis; IEA:Ensembl.
DR GO; GO:0051642; P:centrosome localization; IBA:GO_Central.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IEA:Ensembl.
DR GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR GO; GO:0051303; P:establishment of chromosome localization; IBA:GO_Central.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central.
DR GO; GO:0001833; P:inner cell mass cell proliferation; IEA:Ensembl.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
DR GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central.
DR GO; GO:0007100; P:mitotic centrosome separation; IBA:GO_Central.
DR GO; GO:0060052; P:neurofilament cytoskeleton organization; IEA:Ensembl.
DR GO; GO:1990138; P:neuron projection extension; IEA:Ensembl.
DR GO; GO:0051081; P:nuclear membrane disassembly; IEA:Ensembl.
DR GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
DR GO; GO:0048680; P:positive regulation of axon regeneration; IEA:Ensembl.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:CACAO.
DR GO; GO:1900029; P:positive regulation of ruffle assembly; ISS:UniProtKB.
DR GO; GO:0140650; P:radial glia-guided pyramidal neuron migration; IEA:Ensembl.
DR GO; GO:0033157; P:regulation of intracellular protein transport; IMP:CACAO.
DR GO; GO:0010975; P:regulation of neuron projection development; IBA:GO_Central.
DR GO; GO:0008090; P:retrograde axonal transport; IEA:Ensembl.
DR GO; GO:0047496; P:vesicle transport along microtubule; IBA:GO_Central.
DR InterPro; IPR033493; NDEL1.
DR InterPro; IPR033494; NUDE.
DR InterPro; IPR006964; NUDE_dom.
DR PANTHER; PTHR10921; PTHR10921; 1.
DR PANTHER; PTHR10921:SF0; PTHR10921:SF0; 1.
DR Pfam; PF04880; NUDE_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Centromere; Chromosome; Coiled coil;
KW Cytoplasm; Cytoskeleton; Developmental protein; Differentiation;
KW Kinetochore; Lipoprotein; Microtubule; Neurogenesis; Palmitate;
KW Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..345
FT /note="Nuclear distribution protein nudE-like 1"
FT /id="PRO_0000240210"
FT REGION 56..166
FT /note="Self-association"
FT /evidence="ECO:0000250"
FT REGION 64..189
FT /note="Interaction with KATNB1"
FT /evidence="ECO:0000250"
FT REGION 114..133
FT /note="Required for interaction with PAFAH1B1"
FT REGION 175..345
FT /note="Interaction with CENPF"
FT /evidence="ECO:0000269|PubMed:17600710"
FT REGION 189..256
FT /note="Interaction with YWHAE"
FT /evidence="ECO:0000250"
FT REGION 191..345
FT /note="Interaction with NEFL"
FT /evidence="ECO:0000250"
FT REGION 195..256
FT /note="Interaction with KATNA1"
FT /evidence="ECO:0000250"
FT REGION 241..280
FT /note="Interaction with DISC1"
FT REGION 256..291
FT /note="Required for localization to the centrosome and
FT interaction with dynein, dynactin, tubulin gamma, PCM1 and
FT PCNT"
FT /evidence="ECO:0000269|PubMed:16291865"
FT REGION 315..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 28..190
FT /evidence="ECO:0000255"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 219
FT /note="Phosphothreonine; by CDK1 and MAPK1"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 242
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 245
FT /note="Phosphothreonine; by CDK1 and MAPK1"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q78PB6"
FT LIPID 273
FT /note="S-palmitoyl cysteine; by ZDHHC2, ZDHHC3 and ZDHHC7"
FT /evidence="ECO:0000269|PubMed:19927128"
FT VAR_SEQ 316..345
FT /note="AVNGFDPAPPPPGLGSSRPSSAPGMLPLSV -> SSSSCAIRASRRRFSSSS
FT ADLAGRGGGDGSIPAQHSTGASGKAPPPTLLLET (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_019310"
FT VAR_SEQ 316..345
FT /note="AVNGFDPAPPPPGLGSSRPSSAPGMLPLSV -> QEKVIFPTLFMGQ (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047509"
FT MUTAGEN 198
FT /note="S->A: Abrogates mitotic phosphorylation; when
FT associated with V-219; A-231; A-242 and V-245. Abrogates
FT phosphorylation by CDK5; when associated with A-219 and A-
FT 231."
FT /evidence="ECO:0000269|PubMed:11163260,
FT ECO:0000269|PubMed:12556484"
FT MUTAGEN 198
FT /note="S->E: Enhances interaction with PAFAH1B1 and impairs
FT centrosomal localization; when associated with E-219; E-
FT 231; E-242 and E-245."
FT /evidence="ECO:0000269|PubMed:11163260,
FT ECO:0000269|PubMed:12556484"
FT MUTAGEN 219
FT /note="T->A: Abrogates phosphorylation by CDK5; when
FT associated with A-198 and A-231."
FT /evidence="ECO:0000269|PubMed:11163260,
FT ECO:0000269|PubMed:12556484"
FT MUTAGEN 219
FT /note="T->E: Enhances interaction with PAFAH1B1 and impairs
FT centrosomal localization; when associated with E-198; E-
FT 231; E-242 and E-245."
FT /evidence="ECO:0000269|PubMed:11163260,
FT ECO:0000269|PubMed:12556484"
FT MUTAGEN 219
FT /note="T->V: Abrogates mitotic phosphorylation; when
FT associated with A-198; A-231; A-242 and V-245."
FT /evidence="ECO:0000269|PubMed:11163260,
FT ECO:0000269|PubMed:12556484"
FT MUTAGEN 231
FT /note="S->A: Abrogates mitotic phosphorylation; when
FT associated with A-198; V-219; A-242 and V-245. Abrogates
FT phosphorylation by CDK5; when associated with A-198 and A-
FT 219."
FT /evidence="ECO:0000269|PubMed:11163260,
FT ECO:0000269|PubMed:12556484"
FT MUTAGEN 231
FT /note="S->E: Enhances interaction with PAFAH1B1 and impairs
FT centrosomal localization; when associated with E-198; E-
FT 219; E-242 and E-245."
FT /evidence="ECO:0000269|PubMed:11163260,
FT ECO:0000269|PubMed:12556484"
FT MUTAGEN 242
FT /note="S->A: Abrogates mitotic phosphorylation; when
FT associated with A-198; V-219; A-231 and V-245."
FT /evidence="ECO:0000269|PubMed:12556484"
FT MUTAGEN 242
FT /note="S->E: Enhances interaction with PAFAH1B1 and impairs
FT centrosomal localization; when associated with E-198; E-
FT 219; E-231 and E-245."
FT /evidence="ECO:0000269|PubMed:12556484"
FT MUTAGEN 245
FT /note="T->E: Enhances interaction with PAFAH1B1 and impairs
FT centrosomal localization; when associated with E-198; E-
FT 219; E-231 and E-242."
FT /evidence="ECO:0000269|PubMed:12556484"
FT MUTAGEN 245
FT /note="T->V: Abrogates mitotic phosphorylation; when
FT associated with A-198; V-219; A-231 and A-242."
FT /evidence="ECO:0000269|PubMed:12556484"
FT MUTAGEN 266
FT /note="L->A: Abolishes interaction with DISC1; when
FT associated with A-267."
FT /evidence="ECO:0000269|PubMed:17035248"
FT MUTAGEN 267
FT /note="E->A: Abolishes interaction with DISC1; when
FT associated with A-266."
FT /evidence="ECO:0000269|PubMed:17035248"
FT MUTAGEN 273
FT /note="C->A: Abolishes oligopeptidase activity."
FT /evidence="ECO:0000269|PubMed:15728732"
FT CONFLICT 322
FT /note="P -> T (in Ref. 8; AAH26101)"
FT /evidence="ECO:0000305"
FT HELIX 59..165
FT /evidence="ECO:0007829|PDB:2V66"
SQ SEQUENCE 345 AA; 38375 MW; E91EA053FCA315D7 CRC64;
MDGEDIPDFS SLKEETAYWK ELSLKYKQSF QEARDELVEF QEGSRELEAE LEAQLVQAEQ
RNRDLQADNQ RLKYEVEALK EKLEHQYAQS YKQVSVLEDD LSQTRAIKEQ LHKYVRELEQ
ANDDLERAKR ATIVSLEDFE QRLNQAIERN AFLESELDEK ESLLVSVQRL KDEARDLRQE
LAVRERQQEV TRKSAPSSPT LDCEKMDSAV QASLSLPATP VGKGTENTFP SPKAIPNGFG
TSPLTPSARI SALNIVGDLL RKVGALESKL AACRNFAKDQ ASRKSYISGN VNCGVLNGNG
TKFSRSGHTS FFDKGAVNGF DPAPPPPGLG SSRPSSAPGM LPLSV
