CENPE_MOUSE
ID CENPE_MOUSE Reviewed; 2474 AA.
AC Q6RT24; O35059; Q3KQQ6; Q3V044; Q6PD00; Q7TPX4; Q80YB4; Q8BWX6;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Centromere-associated protein E {ECO:0000312|EMBL:AAR85498.1};
DE AltName: Full=Centromere protein E;
DE Short=CENP-E {ECO:0000250|UniProtKB:Q02224};
DE AltName: Full=Kinesin superfamily protein 10 {ECO:0000303|PubMed:9275178};
DE Short=KIF10 {ECO:0000303|PubMed:9275178};
DE AltName: Full=Motor domain of KIF10 {ECO:0000312|EMBL:BAA22386.1};
DE Flags: Precursor;
GN Name=Cenpe {ECO:0000312|MGI:MGI:1098230};
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] {ECO:0000305, ECO:0000312|EMBL:AAR85498.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH BUB1B, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12925705; DOI=10.1083/jcb.200303167;
RA Weaver B.A., Bonday Z.Q., Putkey F.R., Kops G.J., Silk A.D.,
RA Cleveland D.W.;
RT "Centromere-associated protein-E is essential for the mammalian mitotic
RT checkpoint to prevent aneuploidy due to single chromosome loss.";
RL J. Cell Biol. 162:551-563(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH52843.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-546 AND 1652-2474.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH52843.1}, and
RC Czech II {ECO:0000312|EMBL:AAI06097.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH59032.1},
RC Egg {ECO:0000312|EMBL:AAH52843.1},
RC Mammary tumor {ECO:0000312|EMBL:AAI06097.1}, and
RC Olfactory epithelium {ECO:0000312|EMBL:AAH49989.1};
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] {ECO:0000305, ECO:0000312|EMBL:BAE21661.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-520 AND 1705-2474.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE21661.1};
RC TISSUE=Spinal cord {ECO:0000312|EMBL:BAC33868.1}, and
RC Testis {ECO:0000312|EMBL:BAE21661.1};
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] {ECO:0000305, ECO:0000312|EMBL:BAA22386.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 82-241, AND TISSUE SPECIFICITY.
RC STRAIN=ICR {ECO:0000312|EMBL:BAA22386.1};
RC TISSUE=Hippocampus {ECO:0000269|PubMed:9275178};
RX PubMed=9275178; DOI=10.1073/pnas.94.18.9654;
RA Nakagawa T., Tanaka Y., Matsuoka E., Kondo S., Okada Y., Noda Y., Kanai Y.,
RA Hirokawa N.;
RT "Identification and classification of 16 new kinesin superfamily (KIF)
RT proteins in mouse genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9654-9659(1997).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12361599; DOI=10.1016/s1534-5807(02)00255-1;
RA Putkey F.R., Cramer T., Morphew M.K., Silk A.D., Johnson R.S.,
RA McIntosh J.R., Cleveland D.W.;
RT "Unstable kinetochore-microtubule capture and chromosomal instability
RT following deletion of CENP-E.";
RL Dev. Cell 3:351-365(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
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).
CC -!- FUNCTION: Microtubule plus-end-directed kinetochore motor which plays
CC an important role in chromosome congression, microtubule-kinetochore
CC conjugation and spindle assembly checkpoint activation. Drives
CC chromosome congression (alignment of chromosomes at the spindle equator
CC resulting in the formation of the metaphase plate) by mediating the
CC lateral sliding of polar chromosomes along spindle microtubules towards
CC the spindle equator and by aiding the establishment and maintenance of
CC connections between kinetochores and spindle microtubules. The
CC transport of pole-proximal chromosomes towards the spindle equator is
CC favored by microtubule tracks that are detyrosinated. Acts as a
CC processive bi-directional tracker of dynamic microtubule tips; after
CC chromosomes have congressed, continues to play an active role at
CC kinetochores, enhancing their links with dynamic microtubule ends.
CC Suppresses chromosome congression in NDC80-depleted cells and
CC contributes positively to congression only when microtubules are
CC stabilized (By similarity). Plays an important role in the formation of
CC stable attachments between kinetochores and spindle microtubules
CC (PubMed:12925705). The stabilization of kinetochore-microtubule
CC attachment also requires CENPE-dependent localization of other proteins
CC to the kinetochore including BUB1B, MAD1 and MAD2. Plays a role in
CC spindle assembly checkpoint activation (SAC) via its interaction with
CC BUB1B resulting in the activation of its kinase activity, which is
CC important for activating SAC (PubMed:12361599). Necessary for the
CC mitotic checkpoint signal at individual kinetochores to prevent
CC aneuploidy due to single chromosome loss (PubMed:12925705).
CC {ECO:0000250|UniProtKB:Q02224, ECO:0000269|PubMed:12361599,
CC ECO:0000269|PubMed:12925705}.
CC -!- SUBUNIT: Monomer. Interacts with CENPF, SEPT7 KIF18A and PRC1 (By
CC similarity). Interacts with BUB1B (PubMed:12925705). Interacts with
CC SKAP; this interaction greatly favors SKAP binding to microtubules.
CC Interacts with TRAPPC12 and CTCF (By similarity).
CC {ECO:0000250|UniProtKB:Q02224, ECO:0000269|PubMed:12925705}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:12361599, ECO:0000269|PubMed:12925705}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:12361599,
CC ECO:0000269|PubMed:12925705}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:Q02224}. Note=Associates with kinetochores
CC during congression (as early as prometaphase), relocates to the spindle
CC midzone at anaphase, and is quantitatively discarded at the end of the
CC cell division (PubMed:12361599, PubMed:12925705). Recruited to the
CC kinetochore in a SEPT7, CENPQ and TRAPPC12-dependent manner. Recruited
CC to the pericentromeric/centromeric regions of the chromosome in a CTCF-
CC dependent manner (By similarity). {ECO:0000250|UniProtKB:Q02224,
CC ECO:0000269|PubMed:12361599, ECO:0000269|PubMed:12925705}.
CC -!- TISSUE SPECIFICITY: Expressed in hippocampus. Also detected in liver
CC and fibroblasts (at protein level). {ECO:0000269|PubMed:12361599,
CC ECO:0000269|PubMed:9275178}.
CC -!- DOMAIN: The protein is composed of a N-terminal kinesin-motor domain
CC involved in the chromosome movements, a long coil-coiled region
CC involved in the homodimerization and an inhibitory C-tail involved in
CC autoinhibition of the N-terminal catalytic part. {ECO:0000250}.
CC -!- PTM: The C-terminal inhibitory domain is phosphorylated.
CC Phosphorylation relieves autoinhibition of the kinetochore motor (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Sumoylated with SUMO2 and SUMO3. The sumoylation mediates the
CC association to the kinetochore. {ECO:0000250|UniProtKB:Q02224}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH52843.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAI06097.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAC33868.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY493378; AAR85498.1; -; mRNA.
DR EMBL; BC049989; AAH49989.1; -; mRNA.
DR EMBL; BC052843; AAH52843.1; ALT_SEQ; mRNA.
DR EMBL; BC059032; AAH59032.1; -; mRNA.
DR EMBL; BC106096; AAI06097.1; ALT_SEQ; mRNA.
DR EMBL; AK049676; BAC33868.1; ALT_FRAME; mRNA.
DR EMBL; AK133445; BAE21661.1; -; mRNA.
DR EMBL; AB001426; BAA22386.1; -; mRNA.
DR RefSeq; NP_776123.3; NM_173762.4.
DR AlphaFoldDB; Q6RT24; -.
DR SMR; Q6RT24; -.
DR BioGRID; 230907; 124.
DR IntAct; Q6RT24; 4.
DR STRING; 10090.ENSMUSP00000057938; -.
DR iPTMnet; Q6RT24; -.
DR PhosphoSitePlus; Q6RT24; -.
DR EPD; Q6RT24; -.
DR jPOST; Q6RT24; -.
DR MaxQB; Q6RT24; -.
DR PaxDb; Q6RT24; -.
DR PRIDE; Q6RT24; -.
DR ProteomicsDB; 281536; -.
DR DNASU; 229841; -.
DR GeneID; 229841; -.
DR KEGG; mmu:229841; -.
DR CTD; 1062; -.
DR MGI; MGI:1098230; Cenpe.
DR eggNOG; KOG0242; Eukaryota.
DR InParanoid; Q6RT24; -.
DR OrthoDB; 21522at2759; -.
DR PhylomeDB; Q6RT24; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 229841; 20 hits in 75 CRISPR screens.
DR ChiTaRS; Cenpe; mouse.
DR PRO; PR:Q6RT24; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6RT24; protein.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0000775; C:chromosome, centromeric region; ISO:MGI.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0005828; C:kinetochore microtubule; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:1990023; C:mitotic spindle midzone; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000940; C:outer kinetochore; IDA:MGI.
DR GO; GO:0051233; C:spindle midzone; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043515; F:kinetochore binding; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0003777; F:microtubule motor activity; ISO:MGI.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IMP:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; ISO:MGI.
DR GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB.
DR GO; GO:0051382; P:kinetochore assembly; ISO:MGI.
DR GO; GO:0099607; P:lateral attachment of mitotic spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0051310; P:metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0099606; P:microtubule plus-end directed mitotic chromosome migration; ISO:MGI.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; ISO:MGI.
DR GO; GO:0007079; P:mitotic chromosome movement towards spindle pole; ISO:MGI.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; ISO:MGI.
DR GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; IMP:UniProtKB.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; IMP:UniProtKB.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IMP:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0050793; P:regulation of developmental process; IMP:UniProtKB.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; ISO:MGI.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; IMP:MGI.
DR GO; GO:0007057; P:spindle assembly involved in female meiosis I; IMP:MGI.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein; Kinetochore;
KW Lipoprotein; Methylation; Mitosis; Motor protein; Nucleotide-binding;
KW Phosphoprotein; Prenylation; Reference proteome; Ubl conjugation.
FT CHAIN 1..2471
FT /note="Centromere-associated protein E"
FT /id="PRO_0000365106"
FT PROPEP 2472..2474
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396743"
FT DOMAIN 6..329
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1962..2252
FT /note="Kinetochore binding domain"
FT /evidence="ECO:0000250|UniProtKB:Q02224"
FT REGION 2196..2217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2286..2471
FT /note="Globular autoinhibitory domain"
FT /evidence="ECO:0000250"
FT REGION 2371..2441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 334..2366
FT /evidence="ECO:0000255"
FT COMPBIAS 2393..2411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02224"
FT MOD_RES 2414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02224"
FT MOD_RES 2426
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02224"
FT MOD_RES 2471
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 2471
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q02224"
FT CONFLICT 231..241
FT /note="LNLVDLAGSER -> IKLIDTVDLEG (in Ref. 4; BAA22386)"
FT /evidence="ECO:0000305"
FT CONFLICT 1760
FT /note="T -> A (in Ref. 3; BAC33868)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2474 AA; 286525 MW; BAF52DD6068A2903 CRC64;
MAEEASVAVC VRVRPLNSRE EELGEATHIY WKTDKNAIYQ SDGGKSFQFD RVFDSNETTK
NVYEEIAVPI ISSAIQGYNG TIFAYGQTAS GKTHTMMGSE DCLGVIPRAI HDIFQRIKKF
PEREFLLRVS YMEIYNETIT DLLCNAQKMK PLIIREDTNR TVYVSDLTEE VVYTAEMALK
WLATGEKNRH YGITKMNQRS SRSHTIFRMI LESREKAEPS NCDGSVKVSH LNLVDLAGSE
RAAQTGAEGV RLKEGCFINR NLFILGQVIK KLSDGQVGGF INYRDSKLTR ILQNSLGGNA
KTRIICTITP ASLDETLTTL QFASTAKYMK NTPYVNEVSN DEALLKRYRR EIADLRKQLE
EVNTKTRAQE MEKDQLAQLL DEKDLLQKVQ DEKINNLKRM LVTSSSIALQ QELEIKRKRR
VTWCYGKMKD SNYEKEFKVP TSITTRKRKT SVTSLRENSL MKFGESAASS EFEMLNNTLE
SLAEVEWSSA TTLLSEENVE SELNSLNAQY NDLVLDYEQL RRENEDLKLK LKEKNELEEF
ELLEQKEERD QEMQLMHEVS NLKNLIKHAE EYNQDLENDL SSKVKLLKEK EEQIKNLQEY
IDAQKSEKMK IDLSYTSDAT EDLKQAMRTL SDLDTVALDA KKESAFLRSE NLELKEKINE
LSDSRKQMES DIQMYQRQLE AKKKMQTDLD KELQLAFQEI SKLSALVDGK GLLSNLELEK
RITDLQKELN KEAEEKQTLQ EEVNLLSELK SLPSEVETLR RELYEKSEEL HIITTEREKL
FSEMAHKDSR IQGLLEEIGN TRDDLATSQL SRRGSDGEWQ ALESLHAELE HRHAGVLEER
ERLKQEIGAL SKEAESLAFS LDSVKAELSH KTQELEQKTV EGQERLNKME ALREELESRD
SSLQSVEKEK VLLTEKLQQA LKEVKALTQE KKNLKQLQES LQTERDQLRS DIQDTVNMNI
DTQEQLLNAL ESLKQHQETI NMLKMKAAEE LSDNLHVKDR GGARDEAQQK MDGIDEQNES
AHTLLGGGKD NEVTEEQRKI DSLMQENSGL QQTLESVRAE KEQLKMDLKE NIEMSIENQE
ELRILRDELK RQQEVAAQEK DHATEKTQEL SRTQERLAKT EEKLEEKNQK LQETQQQLLS
TQEAMSKLQA KVIDMESLQN EFRNQGLALE RVETEKLELA QRLHESYEEV KSITKERNDL
KELQESFEIE KKQLKEYARE IEAEGLQAKE ELNIAHANLK EYQEIITELR GSISENEAQG
ASTQDTAKSA PELQGEVPEL LEQELLPVVK EARHSAEKVN GLEPVGAHSR TVHSMTMEGI
EIGNLRLTKK LEESQMEISC LTREREDLRR TQETLQVECT QLKEDARRTL ANHLETEEEL
NLARCCLKEQ ENKIDTLITS LSQRETELSS VRGQLALTTA ELERKVQELC EKQEELTRKE
TSEAQGKMSE LEQLRELLLA QASALQNAES DRLRLNTQLE ESQEEMKTLR EEREELRRMQ
EALHVESEQQ KESMKEISSK LQELQNKEYE CLAMKTINET QGSRCEMDHL NQQLEAQKST
LEKVEMENVN LTQRLHETLE EMRSVAKERD ELWSMEERLT VERDQLKKSL EETVTKGMEK
EEELRVAHVH LEEHQETINK LRKMVSDYTD EISHTQGDLK HTNAVVEAQN QDLREKEHQL
SQVKADLRET VDQMEQLKKK LEAQSSTLES REIEKLELTQ QLNENLKKIT LVTKENDSLK
IMDEALREER DQLRKSLQQT EARDLENQEK LRIAHMNLKE HQETIDRLME TMSEKTEEIS
NMKMELENVN MKLQEKVQEL KTSERQRVKL KADASEAKKE LKEQGLTLSK IEMENLNLAQ
KIHENLEEMK SVRKERDDLK KLEEILRMER DQLKDNLREA MLKAHQNHEE TMKCGKGLLC
AGEYCTGRLR EKCFRIEKLL KRYSEMANDY ECLNKVSLDL ERETKTQKEL SVTVRTKLSL
PHTQTKEMEK LLTANQRCSL EFHRALKRLK YVLSSIARIK EEQHESINKR EMAFIQEVEK
QNELQIQIQS LSQTYRIPAR DLQIKLSQEM DLHIEEMLKD FSENDFLTIK TEVQQVLNNR
KEITEFLGKW LNTLFDTENL KSTIQKENKS IGLVNNFYHS RITAMINEST EFEERSATRS
KDLDQYLKSL KETTEQLSEV YQTLTASQSV VHLHPTVQPS TRDSERPQAA SGAEQLTSKN
KIALGAVPYK EEIEDLKMQL VKSDLEKKAT AKEFDKKILS LKATVEHQEE MIRLLRENLR
GHQQAQDTSM ISEQDSQLLS KPLTCGGGSG IVQSTKALIL KSEYKRMGSE ISKLKQQNEQ
LRKQNNQLLS DNSQLSNEVK TWEERTLKRD SYRETTCENS PKSPKVTRTD SKRRQNTTSQ
CRAQNLQDPV PKDSPKSWFF DNRSKSLPAP HPIRYFDNSS LGLCPEPDDV ENVEPKTDLC
QASLEKDVSQ CKTQ
