CP135_HUMAN
ID CP135_HUMAN Reviewed; 1140 AA.
AC Q66GS9; B2RMY0; O75130; Q58F25; Q9H8H7;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Centrosomal protein of 135 kDa {ECO:0000305};
DE Short=Cep135;
DE AltName: Full=Centrosomal protein 4;
GN Name=CEP135 {ECO:0000312|HGNC:HGNC:29086}; Synonyms=CEP4, KIAA0635;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 277-1140 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17681131; DOI=10.1016/j.devcel.2007.07.002;
RA Kleylein-Sohn J., Westendorf J., Le Clech M., Habedanck R., Stierhof Y.-D.,
RA Nigg E.A.;
RT "Plk4-induced centriole biogenesis in human cells.";
RL Dev. Cell 13:190-202(2007).
RN [7]
RP FUNCTION, AND INTERACTION WITH CEP250.
RX PubMed=18851962; DOI=10.1016/j.yexcr.2008.09.016;
RA Kim K., Lee S., Chang J., Rhee K.;
RT "A novel function of CEP135 as a platform protein of C-NAP1 for its
RT centriolar localization.";
RL Exp. Cell Res. 314:3692-3700(2008).
RN [8]
RP INVOLVEMENT IN MCPH8.
RX PubMed=22521416; DOI=10.1016/j.ajhg.2012.03.016;
RA Hussain M.S., Baig S.M., Neumann S., Nurnberg G., Farooq M., Ahmad I.,
RA Alef T., Hennies H.C., Technau M., Altmuller J., Frommolt P., Thiele H.,
RA Noegel A.A., Nurnberg P.;
RT "A truncating mutation of CEP135 causes primary microcephaly and disturbed
RT centrosomal function.";
RL Am. J. Hum. Genet. 90:871-878(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; SER-439; SER-688 AND
RP THR-1121, AND 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).
RN [10]
RP FUNCTION.
RX PubMed=26675238; DOI=10.1242/jcs.179713;
RA Kurtulmus B., Wang W., Ruppert T., Neuner A., Cerikan B., Viol L.,
RA Duenas-Sanchez R., Gruss O.J., Pereira G.;
RT "WDR8 is a centriolar satellite and centriole-associated protein that
RT promotes ciliary vesicle docking during ciliogenesis.";
RL J. Cell Sci. 129:621-636(2016).
RN [11]
RP FUNCTION.
RX PubMed=27185865; DOI=10.1242/jcs.186338;
RA Chang C.W., Hsu W.B., Tsai J.J., Tang C.J., Tang T.K.;
RT "CEP295 interacts with microtubules and is required for centriole
RT elongation.";
RL J. Cell Sci. 129:2501-2513(2016).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=32060285; DOI=10.1038/s41467-020-14767-2;
RA Atorino E.S., Hata S., Funaya C., Neuner A., Schiebel E.;
RT "CEP44 ensures the formation of bona fide centriole wall, a requirement for
RT the centriole-to-centrosome conversion.";
RL Nat. Commun. 11:903-903(2020).
RN [13] {ECO:0007744|PDB:5NG4}
RP X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 82-144, AND DISULFIDE BOND.
RX PubMed=30135143; DOI=10.1042/bsr20181073;
RA Kraatz S.H.W., Bianchi S., Steinmetz M.O.;
RT "Combinatorial use of disulfide bridges and native sulfur-SAD phasing for
RT rapid structure determination of coiled-coils.";
RL Biosci. Rep. 38:0-0(2018).
CC -!- FUNCTION: Centrosomal protein involved in centriole biogenesis. Acts as
CC a scaffolding protein during early centriole biogenesis. Required for
CC the targeting of centriole satellite proteins to centrosomes such as of
CC PCM1, SSX2IP and CEP290 and recruitment of WRAP73 to centrioles. Also
CC required for centriole-centriole cohesion during interphase by acting
CC as a platform protein for CEP250 at the centriole. Required for the
CC recruitment of CEP295 to the proximal end of new-born centrioles at the
CC centriolar microtubule wall during early S phase in a PLK4-dependent
CC manner (PubMed:27185865). {ECO:0000269|PubMed:17681131,
CC ECO:0000269|PubMed:18851962, ECO:0000269|PubMed:26675238,
CC ECO:0000269|PubMed:27185865}.
CC -!- SUBUNIT: Interacts with DCTN2 (By similarity). Interacts with CEP250
CC (PubMed:18851962). {ECO:0000250|UniProtKB:Q6P5D4,
CC ECO:0000269|PubMed:18851962}.
CC -!- INTERACTION:
CC Q66GS9; Q9HC77: CENPJ; NbExp=8; IntAct=EBI-1046993, EBI-946194;
CC Q66GS9; O94986-3: CEP152; NbExp=2; IntAct=EBI-1046993, EBI-15878364;
CC Q66GS9; Q5TB80: CEP162; NbExp=3; IntAct=EBI-1046993, EBI-1059012;
CC Q66GS9; A0A087WUI6: PIBF1; NbExp=3; IntAct=EBI-1046993, EBI-11749468;
CC Q66GS9; Q6UVJ0: SASS6; NbExp=8; IntAct=EBI-1046993, EBI-1570153;
CC Q66GS9; Q8N0Z3: SPICE1; NbExp=4; IntAct=EBI-1046993, EBI-2361917;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:14654843,
CC ECO:0000269|PubMed:17681131, ECO:0000269|PubMed:32060285}. Note=During
CC centriole biogenesis, it is concentrated within the proximal lumen of
CC both parental centrioles and procentrioles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q66GS9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q66GS9-2; Sequence=VSP_012743, VSP_012744;
CC -!- DISEASE: Microcephaly 8, primary, autosomal recessive (MCPH8)
CC [MIM:614673]: A disease defined as a head circumference more than 3
CC standard deviations below the age-related mean. Brain weight is
CC markedly reduced and the cerebral cortex is disproportionately small.
CC Despite this marked reduction in size, the gyral pattern is relatively
CC well preserved, with no major abnormality in cortical architecture.
CC Affected individuals are mentally retarded. Primary microcephaly is
CC further defined by the absence of other syndromic features or
CC significant neurological deficits due to degenerative brain disorder.
CC {ECO:0000269|PubMed:22521416}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CEP135/TSGA10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH12003.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA31610.2; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK023683; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC118280; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012003; AAH12003.1; ALT_SEQ; mRNA.
DR EMBL; BC136535; AAI36536.1; -; mRNA.
DR EMBL; BC136536; AAI36537.1; -; mRNA.
DR EMBL; AB014535; BAA31610.2; ALT_SEQ; mRNA.
DR EMBL; BK005586; DAA05590.1; -; mRNA.
DR CCDS; CCDS33986.1; -. [Q66GS9-1]
DR RefSeq; NP_079285.2; NM_025009.4. [Q66GS9-1]
DR PDB; 5FCN; X-ray; 1.80 A; A/B=82-144.
DR PDB; 5NG4; X-ray; 2.14 A; A/B=82-144.
DR PDBsum; 5FCN; -.
DR PDBsum; 5NG4; -.
DR AlphaFoldDB; Q66GS9; -.
DR SMR; Q66GS9; -.
DR BioGRID; 115018; 265.
DR DIP; DIP-50271N; -.
DR IntAct; Q66GS9; 186.
DR MINT; Q66GS9; -.
DR STRING; 9606.ENSP00000257287; -.
DR MoonDB; Q66GS9; Predicted.
DR iPTMnet; Q66GS9; -.
DR PhosphoSitePlus; Q66GS9; -.
DR BioMuta; CEP135; -.
DR DMDM; 296434460; -.
DR EPD; Q66GS9; -.
DR jPOST; Q66GS9; -.
DR MassIVE; Q66GS9; -.
DR MaxQB; Q66GS9; -.
DR PaxDb; Q66GS9; -.
DR PeptideAtlas; Q66GS9; -.
DR PRIDE; Q66GS9; -.
DR ProteomicsDB; 65948; -. [Q66GS9-1]
DR ProteomicsDB; 65949; -. [Q66GS9-2]
DR Antibodypedia; 23978; 155 antibodies from 23 providers.
DR DNASU; 9662; -.
DR Ensembl; ENST00000257287.5; ENSP00000257287.3; ENSG00000174799.11. [Q66GS9-1]
DR Ensembl; ENST00000422247.6; ENSP00000412799.2; ENSG00000174799.11. [Q66GS9-2]
DR GeneID; 9662; -.
DR KEGG; hsa:9662; -.
DR MANE-Select; ENST00000257287.5; ENSP00000257287.3; NM_025009.5; NP_079285.2.
DR UCSC; uc003hbh.3; human. [Q66GS9-1]
DR CTD; 9662; -.
DR DisGeNET; 9662; -.
DR GeneCards; CEP135; -.
DR HGNC; HGNC:29086; CEP135.
DR HPA; ENSG00000174799; Low tissue specificity.
DR MalaCards; CEP135; -.
DR MIM; 611423; gene.
DR MIM; 614673; phenotype.
DR neXtProt; NX_Q66GS9; -.
DR OpenTargets; ENSG00000174799; -.
DR Orphanet; 2512; Autosomal recessive primary microcephaly.
DR PharmGKB; PA128394551; -.
DR VEuPathDB; HostDB:ENSG00000174799; -.
DR eggNOG; ENOG502QT27; Eukaryota.
DR GeneTree; ENSGT00940000159453; -.
DR HOGENOM; CLU_1152849_0_0_1; -.
DR InParanoid; Q66GS9; -.
DR OMA; QGRENTM; -.
DR OrthoDB; 1249457at2759; -.
DR PhylomeDB; Q66GS9; -.
DR TreeFam; TF326518; -.
DR PathwayCommons; Q66GS9; -.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR SignaLink; Q66GS9; -.
DR BioGRID-ORCS; 9662; 104 hits in 1090 CRISPR screens.
DR ChiTaRS; CEP135; human.
DR GeneWiki; CEP135; -.
DR GenomeRNAi; 9662; -.
DR Pharos; Q66GS9; Tbio.
DR PRO; PR:Q66GS9; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q66GS9; protein.
DR Bgee; ENSG00000174799; Expressed in amniotic fluid and 162 other tissues.
DR Genevisible; Q66GS9; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0007099; P:centriole replication; IMP:UniProtKB.
DR GO; GO:0010457; P:centriole-centriole cohesion; IMP:UniProtKB.
DR GO; GO:1904951; P:positive regulation of establishment of protein localization; IMP:UniProtKB.
DR GO; GO:1902857; P:positive regulation of non-motile cilium assembly; IMP:UniProtKB.
DR InterPro; IPR026732; Cep135.
DR PANTHER; PTHR23159:SF18; PTHR23159:SF18; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disulfide bond; Intellectual disability; Phosphoprotein;
KW Primary microcephaly; Reference proteome.
FT CHAIN 1..1140
FT /note="Centrosomal protein of 135 kDa"
FT /id="PRO_0000089491"
FT REGION 1114..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 71..152
FT /evidence="ECO:0000255"
FT COILED 195..420
FT /evidence="ECO:0000255"
FT COILED 447..1039
FT /evidence="ECO:0000255"
FT COILED 1069..1116
FT /evidence="ECO:0000255"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1121
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P5D4"
FT DISULFID 110
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:30135143,
FT ECO:0007744|PDB:5NG4"
FT VAR_SEQ 234..249
FT /note="IELREREIERLSVALD -> VGFLFTCIVGIEIGML (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012743"
FT VAR_SEQ 250..1140
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012744"
FT VARIANT 769
FT /note="I -> L (in dbSNP:rs3214045)"
FT /id="VAR_057785"
FT CONFLICT 336
FT /note="V -> L (in Ref. 4; BAA31610)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="Q -> R (in Ref. 3; AAH12003)"
FT /evidence="ECO:0000305"
FT HELIX 82..131
FT /evidence="ECO:0007829|PDB:5FCN"
SQ SEQUENCE 1140 AA; 133490 MW; AD56754BEBB3AA5B CRC64;
MTTAVERKYI NIRKRLDQLG YRQTLTVECL PLVEKLFSDL VHTTESLRQS KLSAVKAEKE
SANFDFVLEP YKLENARLSR ENNELYLELM KLREHSDQHV KELKTSLKKC ARETADLKFL
NNQYAHKLKL LEKESKAKNE RIQQLQEKNL HAVVQTPGGK KRSIAFRRQR MQIDEPVPPS
EVSSYPVPQP DDPYIADLLQ VADNRIQELQ QEVHQLQEKL AMMESGVRDY SKQIELRERE
IERLSVALDG GRSPDVLSLE SRNKTNEKLI AHLNIQVDFL QQANKDLEKR IRELMETKET
VTSEVVNLSN KNEKLCQELT EIDQLAQQLE RHKEEVLETA DKELGEAKKE IKRKLSEMQD
LEETMAKLQL ELNLCQKEKE RLSDELLVKS DLETVVHQLE QEKQRLSKKV ESFAVTERQL
TLEVERMRLE HGIKRRDRSP SRLDTFLKGI EEERDYYKKE LERLQHIIQR RSCSTSYSAR
EKSSIFRTPE KGDYNSEIHQ ITRERDELQR MLERFEKYME DIQSNVKLLT AERDKLSVLY
NEAQEELSAL RKESTQTTAP HNIVSLMEKE KELALSDLRR IMAEKEALRE KLEHIEEVSL
FGKSELEKTI EHLTCVNHQL ESEKYELKSK VLIMKETIES LENKLKVQAQ KFSHVAGDSS
HQKTEVNSLR IVNEQLQRSV DDYQHRLSIK RGELESAQAQ IKILEEKIDE LNLKMTSQDE
EAHVMKKTIG VIDKEKDFLQ ETVDEKTEKI ANLQENLANK EKAVAQMKIM ISECESSVNQ
LKETLVNRDR EINSLRRQLD AAHKELDEVG RSREIAFKEN RRLQDDLATM ARENQEISLE
LEAAVQEKEE MKSRVHKYIT EVSRWESLMA AKEKENQDLL DRFQMLHNRA EDWEVKAHQA
EGESSSVRLE LLSIDTERRH LRERVELLEK EIQEHINAHH AYESQISSMA KAMSRLEEEL
RHQEDEKATV LNDLSSLREL CIKLDSGKDI MTQQLNSKNL EFERVVVELE NVKSESDLLK
KQLSNERHTV KNLESLLATN RDKEFHSHLT SHEKDTEIQL LKEKLTLSES KLTSQSRENT
MLRAKVAQLQ TDYDALKRQI STERYERERA IQEMRRHGLA TPPLSSTLRS PSHSPEHRNV
