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 02-OCT-2024, entry version 171. 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; 191. DR DIP; DIP-47280N; -. DR IntAct; Q7Z7A1; 194. 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 jPOST; Q7Z7A1; -. DR MassIVE; Q7Z7A1; -. DR PaxDb; 9606-ENSP00000362962; -. DR PeptideAtlas; 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; 42 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 AGR; HGNC:1858; -. DR CTD; 11064; -. DR DisGeNET; 11064; -. DR GeneCards; CNTRL; -. DR HGNC; HGNC:1858; CNTRL. DR HPA; ENSG00000119397; Tissue enhanced (lymphoid tissue, 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; XYIENLE; -. DR OrthoDB; 5397397at2759; -. 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; 15 hits in 1166 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 169 other cell types or tissues. DR ExpressionAtlas; Q7Z7A1; baseline and differential. 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:HPA. 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:0035904; P:aorta development; IEA:Ensembl. 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:0003281; P:ventricular septum development; IEA:Ensembl. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2. DR InterPro; IPR050576; Cilia_flagella_integrity. DR InterPro; IPR001611; Leu-rich_rpt. DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp. DR InterPro; IPR032675; LRR_dom_sf. DR PANTHER; PTHR45973:SF5; CENTRIOLIN; 1. DR PANTHER; PTHR45973; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT SDS22-RELATED; 1. DR Pfam; PF14580; LRR_9; 1. DR SMART; SM00365; LRR_SD22; 3. DR SMART; SM00369; LRR_TYP; 3. DR SUPFAM; SSF52058; L domain-like; 1. 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 Proteomics identification; 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 //