CNTRL_HUMAN
ID CNTRL_HUMAN Reviewed; 2325 AA.
AC Q7Z7A1; A2A2Y1; B2RP67; Q3MN79; Q5FWF8; Q5JVD0; Q6MZR3; Q6PKC1; Q8TEP3;
AC Q9Y489;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Centriolin;
DE AltName: Full=Centrosomal protein 1;
DE AltName: Full=Centrosomal protein of 110 kDa;
DE Short=Cep110;
GN Name=CNTRL; Synonyms=CEP1, CEP110;
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 3), TISSUE SPECIFICITY, CHROMOSOMAL
RP TRANSLOCATION WITH FGFR1, AND SUBCELLULAR LOCATION.
RX PubMed=10688839;
RA Guasch G., Mack G.J., Popovici C., Dastugue N., Birnbaum D., Rattner J.B.,
RA Pebusque M.-J.;
RT "FGFR1 is fused to the centrosome-associated protein CEP110 in the 8p12
RT stem cell myeloproliferative disorder with t(8;9)(p12;q33).";
RL Blood 95:1788-1796(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-56, SUBCELLULAR
RP LOCATION, AND FUNCTION.
RX PubMed=12732615; DOI=10.1083/jcb.200301105;
RA Gromley A., Jurczyk A., Sillibourne J., Halilovic E., Mogensen M.,
RA Groisman I., Blomberg M., Doxsey S.J.;
RT "A novel human protein of the maternal centriole is required for the final
RT stages of cytokinesis and entry into S phase.";
RL J. Cell Biol. 161:535-545(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Liver;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1513 (ISOFORM 2).
RC TISSUE=Lymph, and Placenta;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 434-1677 (ISOFORM 1).
RX PubMed=16112646; DOI=10.1016/j.bbrc.2005.08.024;
RA Guinn B.-A., Bland E.A., Lodi U., Liggins A.P., Tobal K., Petters S.,
RA Wells J.W., Banham A.H., Mufti G.J.;
RT "Humoral detection of leukaemia-associated antigens in presentation acute
RT myeloid leukaemia.";
RL Biochem. Biophys. Res. Commun. 335:1293-1304(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 527-2325 (ISOFORM 5).
RC TISSUE=Spleen;
RX PubMed=12693554; DOI=10.1093/dnares/10.1.49;
RA Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
RA Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen. II. The
RT complete sequences of 81 cDNA clones.";
RL DNA Res. 10:49-57(2003).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=11956314; DOI=10.1242/jcs.115.9.1825;
RA Ou Y.Y., Mack G.J., Zhang M., Rattner J.B.;
RT "CEP110 and ninein are located in a specific domain of the centrosome
RT associated with centrosome maturation.";
RL J. Cell Sci. 115:1825-1835(2002).
RN [9]
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 [10]
RP FUNCTION, INTERACTION WITH EXOC6 AND SNAPIN, AND SUBCELLULAR LOCATION.
RX PubMed=16213214; DOI=10.1016/j.cell.2005.07.027;
RA Gromley A., Yeaman C., Rosa J., Redick S., Chen C.-T., Mirabelle S.,
RA Guha M., Sillibourne J., Doxsey S.J.;
RT "Centriolin anchoring of exocyst and SNARE complexes at the midbody is
RT required for secretory-vesicle-mediated abscission.";
RL Cell 123:75-87(2005).
RN [11]
RP INTERACTION WITH HOOK2.
RX PubMed=17140400; DOI=10.1111/j.1600-0854.2006.00511.x;
RA Szebenyi G., Hall B., Yu R., Hashim A.I., Kraemer H.;
RT "Hook2 localizes to the centrosome, binds directly to centriolin/CEP110 and
RT contributes to centrosomal function.";
RL Traffic 8:32-46(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831 AND SER-1475, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: Involved in cell cycle progression and cytokinesis. During
CC the late steps of cytokinesis, anchors exocyst and SNARE complexes at
CC the midbody, thereby allowing secretory vesicle-mediated abscission.
CC {ECO:0000269|PubMed:12732615, ECO:0000269|PubMed:16213214}.
CC -!- SUBUNIT: Interacts with HOOK2. Interacts with EXOC6 and SNAPIN.
CC Associates with the exocyst complex. {ECO:0000269|PubMed:16213214,
CC ECO:0000269|PubMed:17140400}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:10688839,
CC ECO:0000269|PubMed:11956314, ECO:0000269|PubMed:12732615,
CC ECO:0000269|PubMed:14654843}. Midbody, Midbody ring
CC {ECO:0000269|PubMed:12732615, ECO:0000269|PubMed:16213214}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q7Z7A1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z7A1-2; Sequence=VSP_032048;
CC Name=3;
CC IsoId=Q7Z7A1-3; Sequence=VSP_032047;
CC Name=4;
CC IsoId=Q7Z7A1-4; Sequence=VSP_032046, VSP_032050;
CC Name=5;
CC IsoId=Q7Z7A1-5; Sequence=VSP_032049;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in testis and
CC trachea. {ECO:0000269|PubMed:10688839}.
CC -!- DISEASE: Note=A chromosomal aberration involving CEP110 may be a cause
CC of stem cell myeloproliferative disorder (MPD). Translocation
CC t(8;9)(p12;q33) with FGFR1. MPD is characterized by myeloid
CC hyperplasia, eosinophilia and T-cell or B-cell lymphoblastic lymphoma.
CC In general it progresses to acute myeloid leukemia. The fusion protein
CC CEP110-FGFR1 is found in the cytoplasm, exhibits constitutive kinase
CC activity and may be responsible for the transforming activity.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH02932.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH02932.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH89415.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; 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; AF083322; AAC32373.1; -; mRNA.
DR EMBL; AF513978; AAP43846.1; -; mRNA.
DR EMBL; BX640927; CAE45965.1; -; mRNA.
DR EMBL; AL137068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002932; AAH02932.1; ALT_SEQ; mRNA.
DR EMBL; BC089415; AAH89415.1; ALT_SEQ; mRNA.
DR EMBL; BC137286; AAI37287.1; -; mRNA.
DR EMBL; AY651261; AAX35689.1; -; mRNA.
DR EMBL; AK074079; BAB84905.1; -; mRNA.
DR CCDS; CCDS35118.1; -. [Q7Z7A1-1]
DR CCDS; CCDS83409.1; -. [Q7Z7A1-2]
DR RefSeq; NP_001317691.1; NM_001330762.1. [Q7Z7A1-2]
DR RefSeq; NP_008949.4; NM_007018.4. [Q7Z7A1-1]
DR RefSeq; XP_005251736.1; XM_005251679.3.
DR AlphaFoldDB; Q7Z7A1; -.
DR SMR; Q7Z7A1; -.
DR BioGRID; 116248; 178.
DR DIP; DIP-47280N; -.
DR IntAct; Q7Z7A1; 187.
DR MINT; Q7Z7A1; -.
DR STRING; 9606.ENSP00000362962; -.
DR CarbonylDB; Q7Z7A1; -.
DR GlyGen; Q7Z7A1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7Z7A1; -.
DR PhosphoSitePlus; Q7Z7A1; -.
DR BioMuta; CNTRL; -.
DR DMDM; 172045911; -.
DR EPD; Q7Z7A1; -.
DR jPOST; Q7Z7A1; -.
DR MassIVE; Q7Z7A1; -.
DR MaxQB; Q7Z7A1; -.
DR PaxDb; Q7Z7A1; -.
DR PeptideAtlas; Q7Z7A1; -.
DR PRIDE; Q7Z7A1; -.
DR ProteomicsDB; 69493; -. [Q7Z7A1-1]
DR ProteomicsDB; 69494; -. [Q7Z7A1-2]
DR ProteomicsDB; 69495; -. [Q7Z7A1-3]
DR ProteomicsDB; 69496; -. [Q7Z7A1-4]
DR ProteomicsDB; 69497; -. [Q7Z7A1-5]
DR Antibodypedia; 30137; 35 antibodies from 13 providers.
DR DNASU; 11064; -.
DR Ensembl; ENST00000373850.6; ENSP00000362956.1; ENSG00000119397.19. [Q7Z7A1-2]
DR Ensembl; ENST00000373855.7; ENSP00000362962.1; ENSG00000119397.19. [Q7Z7A1-1]
DR GeneID; 11064; -.
DR KEGG; hsa:11064; -.
DR MANE-Select; ENST00000373855.7; ENSP00000362962.1; NM_007018.6; NP_008949.4.
DR UCSC; uc004bkx.1; human. [Q7Z7A1-1]
DR CTD; 11064; -.
DR DisGeNET; 11064; -.
DR GeneCards; CNTRL; -.
DR HGNC; HGNC:1858; CNTRL.
DR HPA; ENSG00000119397; Tissue enhanced (bone marrow, testis).
DR MIM; 605496; gene.
DR neXtProt; NX_Q7Z7A1; -.
DR OpenTargets; ENSG00000119397; -.
DR PharmGKB; PA26414; -.
DR VEuPathDB; HostDB:ENSG00000119397; -.
DR eggNOG; KOG0531; Eukaryota.
DR GeneTree; ENSGT00940000155434; -.
DR HOGENOM; CLU_231608_0_0_1; -.
DR InParanoid; Q7Z7A1; -.
DR OMA; QMQHEYL; -.
DR OrthoDB; 79816at2759; -.
DR PhylomeDB; Q7Z7A1; -.
DR TreeFam; TF101135; -.
DR PathwayCommons; Q7Z7A1; -.
DR Reactome; R-HSA-1839117; Signaling by cytosolic FGFR1 fusion mutants. [Q7Z7A1-3]
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-5655302; Signaling by FGFR1 in disease. [Q7Z7A1-3]
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR SignaLink; Q7Z7A1; -.
DR SIGNOR; Q7Z7A1; -.
DR BioGRID-ORCS; 11064; 14 hits in 1083 CRISPR screens.
DR ChiTaRS; CNTRL; human.
DR GeneWiki; CNTRL; -.
DR GenomeRNAi; 11064; -.
DR Pharos; Q7Z7A1; Tbio.
DR PRO; PR:Q7Z7A1; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q7Z7A1; protein.
DR Bgee; ENSG00000119397; Expressed in calcaneal tendon and 167 other tissues.
DR ExpressionAtlas; Q7Z7A1; baseline and differential.
DR Genevisible; Q7Z7A1; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0120103; C:centriolar subdistal appendage; IDA:GO_Central.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
DR GO; GO:0090619; C:meiotic spindle pole; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0097431; C:mitotic spindle pole; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0035904; P:aorta development; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IEA:InterPro.
DR GO; GO:0003281; P:ventricular septum development; IEA:Ensembl.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR028640; CEP110.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR34491:SF2; PTHR34491:SF2; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR PROSITE; PS51450; LRR; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Chromosomal rearrangement;
KW Coiled coil; Cytoplasm; Cytoskeleton; Leucine-rich repeat; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..2325
FT /note="Centriolin"
FT /id="PRO_0000323675"
FT REPEAT 126..147
FT /note="LRR 1"
FT REPEAT 148..169
FT /note="LRR 2"
FT REPEAT 170..191
FT /note="LRR 3"
FT REPEAT 194..215
FT /note="LRR 4"
FT DOMAIN 228..266
FT /note="LRRCT"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1948..2118
FT /note="Required for centrosome localization"
FT REGION 1985..2325
FT /note="Sufficient for interaction with HOOK2"
FT /evidence="ECO:0000269|PubMed:17140400"
FT REGION 2288..2325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 267..343
FT /evidence="ECO:0000255"
FT COILED 435..799
FT /evidence="ECO:0000255"
FT COILED 851..1101
FT /evidence="ECO:0000255"
FT COILED 1317..2255
FT /evidence="ECO:0000255"
FT COMPBIAS 8..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 2139..2140
FT /note="Breakpoint for translocation to form CEP110-FGFR1"
FT MOD_RES 831
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..1818
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_032046"
FT VAR_SEQ 1..1331
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10688839"
FT /id="VSP_032047"
FT VAR_SEQ 1..552
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032048"
FT VAR_SEQ 1291..1296
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:12693554"
FT /id="VSP_032049"
FT VAR_SEQ 1962..1986
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_032050"
FT VARIANT 56
FT /note="V -> I (in dbSNP:rs10818503)"
FT /evidence="ECO:0000269|PubMed:12732615"
FT /id="VAR_039559"
FT VARIANT 216
FT /note="P -> L (in dbSNP:rs10818504)"
FT /id="VAR_039560"
FT VARIANT 889
FT /note="A -> T (in dbSNP:rs17292952)"
FT /id="VAR_039561"
FT VARIANT 1146
FT /note="M -> V (in dbSNP:rs35342437)"
FT /id="VAR_061622"
FT CONFLICT 1389
FT /note="Q -> R (in Ref. 1; AAC32373)"
FT /evidence="ECO:0000305"
FT CONFLICT 1699
FT /note="K -> Q (in Ref. 1; AAC32373)"
FT /evidence="ECO:0000305"
FT CONFLICT 1828
FT /note="E -> D (in Ref. 1; AAC32373)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2325 AA; 268886 MW; 93DD4CA08B5BD4AF CRC64;
MKKGSQQKIF SKAKIPSSSH SPIPSSMSNM RSRSLSPLIG SETLPFHSGG QWCEQVEIAD
ENNMLLDYQD HKGADSHAGV RYITEALIKK LTKQDNLALI KSLNLSLSKD GGKKFKYIEN
LEKCVKLEVL NLSYNLIGKI EKLDKLLKLR ELNLSYNKIS KIEGIENMCN LQKLNLAGNE
IEHIPVWLGK KLKSLRVLNL KGNKISSLQD ISKLKPLQDL ISLILVENPV VTLPHYLQFT
IFHLRSLESL EGQPVTTQDR QEAFERFSLE EVERLERDLE KKMIETEELK SKQTRFLEEI
KNQDKLNKSL KEEAMLQKQS CEELKSDLNT KNELLKQKTI ELTRACQKQY ELEQELAFYK
IDAKFEPLNY YPSEYAEIDK APDESPYIGK SRYKRNMFAT ESYIIDSAQA VQIKKMEPDE
QLRNDHMNLR GHTPLDTQLE DKEKKISAAQ TRLSELHDEI EKAEQQILRA TEEFKQLEEA
IQLKKISEAG KDLLYKQLSG RLQLVNKLRQ EALDLELQME KQKQEIAGKQ KEIKDLQIAI
DSLDSKDPKH SHMKAQKSGK EQQLDIMNKQ YQQLESRLDE ILSRIAKETE EIKDLEEQLT
EGQIAANEAL KKDLEGVISG LQEYLGTIKG QATQAQNECR KLRDEKETLL QRLTEVEQER
DQLEIVAMDA ENMRKELAEL ESALQEQHEV NASLQQTQGD LSAYEAELEA RLNLRDAEAN
QLKEELEKVT RLTQLEQSAL QAELEKERQA LKNALGKAQF SEEKEQENSE LHAKLKHLQD
DNNLLKQQLK DFQNHLNHVV DGLVRPEEVA ARVDELRRKL KLGTGEMNIH SPSDVLGKSL
ADLQKQFSEI LARSKWERDE AQVRERKLQE EMALQQEKLA TGQEEFRQAC ERALEARMNF
DKRQHEARIQ QMENEIHYLQ ENLKSMEEIQ GLTDLQLQEA DEEKERILAQ LRELEKKKKL
EDAKSQEQVF GLDKELKKLK KAVATSDKLA TAELTIAKDQ LKSLHGTVMK INQERAEELQ
EAERFSRKAA QAARDLTRAE AEIELLQNLL RQKGEQFRLE MEKTGVGTGA NSQVLEIEKL
NETMERQRTE IARLQNVLDL TGSDNKGGFE NVLEEIAELR REVSYQNDYI SSMADPFKRR
GYWYFMPPPP SSKVSSHSSQ ATKDSGVGLK YSASTPVRKP RPGQQDGKEG SQPPPASGYW
VYSPIRSGLH KLFPSRDADS GGDSQEESEL DDQEEPPFVP PPGYMMYTVL PDGSPVPQGM
ALYAPPPPLP NNSRPLTPGT VVYGPPPAGA PMVYGPPPPN FSIPFIPMGV LHCNVPEHHN
LENEVSRLED IMQHLKSKKR EERWMRASKR QSEKEMEELH HNIDDLLQEK KSLECEVEEL
HRTVQKRQQQ KDFIDGNVES LMTELEIEKS LKHHEDIVDE IECIEKTLLK RRSELREADR
LLAEAESELS CTKEKTKNAV EKFTDAKRSL LQTESDAEEL ERRAQETAVN LVKADQQLRS
LQADAKDLEQ HKIKQEEILK EINKIVAAKD SDFQCLSKKK EKLTEELQKL QKDIEMAERN
EDHHLQVLKE SEVLLQAKRA ELEKLKSQVT SQQQEMAVLD RQLGHKKEEL HLLQGSMVQA
KADLQEALRL GETEVTEKCN HIREVKSLLE ELSFQKGELN VQISERKTQL TLIKQEIEKE
EENLQVVLRQ MSKHKTELKN ILDMLQLENH ELQGLKLQHD QRVSELEKTQ VAVLEEKLEL
ENLQQISQQQ KGEIEWQKQL LERDKREIER MTAESRALQS CVECLSKEKE DLQEKCDIWE
KKLAQTKRVL AAAEENSKME QSNLEKLELN VRKLQQELDQ LNRDKLSLHN DISAMQQQLQ
EKREAVNSLQ EELANVQDHL NLAKQDLLHT TKHQDVLLSE QTRLQKDISE WANRFEDCQK
EEETKQQQLQ VLQNEIEENK LKLVQQEMMF QRLQKERESE ESKLETSKVT LKEQQHQLEK
ELTDQKSKLD QVLSKVLAAE ERVRTLQEEE RWCESLEKTL SQTKRQLSER EQQLVEKSGE
LLALQKEADS MRADFSLLRN QFLTERKKAE KQVASLKEAL KIQRSQLEKN LLEQKQENSC
IQKEMATIEL VAQDNHERAR RLMKELNQMQ YEYTELKKQM ANQKDLERRQ MEISDAMRTL
KSEVKDEIRT SLKNLNQFLP ELPADLEAIL ERNENLEGEL ESLKENLPFT MNEGPFEEKL
NFSQVHIMDE HWRGEALREK LRHREDRLKA QLRHCMSKQA EVLIKGKRQT EGTLHSLRRQ
VDALGELVTS TSADSASSPS LSQLESSLTE DSQLGQNQEK NASAR
