ID CEP97_HUMAN Reviewed; 865 AA. AC Q8IW35; B5MDY8; Q8NA71; Q9H5T9; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 03-AUG-2022, entry version 176. DE RecName: Full=Centrosomal protein of 97 kDa; DE Short=Cep97; DE AltName: Full=Leucine-rich repeat and IQ domain-containing protein 2; GN Name=CEP97; Synonyms=LRRIQ2; 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 GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin; 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] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-696 (ISOFORM 2), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 714-865 (ISOFORM 1). RC TISSUE=Lung, and Testis; 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 [4] 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 [5] RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH CALM1 AND RP CCP110, AND SUBCELLULAR LOCATION. RX PubMed=17719545; DOI=10.1016/j.cell.2007.06.027; RA Spektor A., Tsang W.Y., Khoo D., Dynlacht B.D.; RT "Cep97 and CP110 suppress a cilia assembly program."; RL Cell 130:678-690(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-542, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763, AND IDENTIFICATION BY RP 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 [8] RP INTERACTION WITH CEP76. RX PubMed=19460342; DOI=10.1016/j.devcel.2009.03.004; RA Tsang W.Y., Spektor A., Vijayakumar S., Bista B.R., Li J., Sanchez I., RA Duensing S., Dynlacht B.D.; RT "Cep76, a centrosomal protein that specifically restrains centriole RT reduplication."; RL Dev. Cell 16:649-660(2009). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, AND IDENTIFICATION BY RP 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 [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP INTERACTION WITH KIF24. RX PubMed=21620453; DOI=10.1016/j.cell.2011.04.028; RA Kobayashi T., Tsang W.Y., Li J., Lane W., Dynlacht B.D.; RT "Centriolar kinesin Kif24 interacts with CP110 to remodel microtubules and RT regulate ciliogenesis."; RL Cell 145:914-925(2011). RN [13] RP INTERACTION WITH CCP110; HERC2 AND NEURL4. RX PubMed=22261722; DOI=10.1074/mcp.m111.014233; RA Al-Hakim A.K., Bashkurov M., Gingras A.C., Durocher D., Pelletier L.; RT "Interaction proteomics identify NEURL4 and the HECT E3 ligase HERC2 as RT novel modulators of centrosome architecture."; RL Mol. Cell. Proteomics 11:M111.014233.01-M111.014233.14(2012). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308 AND SER-500, 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). RN [15] RP INTERACTION WITH TALPID3. RX PubMed=24421332; DOI=10.1083/jcb.201304153; RA Kobayashi T., Kim S., Lin Y.C., Inoue T., Dynlacht B.D.; RT "The CP110-interacting proteins Talpid3 and Cep290 play overlapping and RT distinct roles in cilia assembly."; RL J. Cell Biol. 204:215-229(2014). RN [16] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MPHOSPH9. RX PubMed=30375385; DOI=10.1038/s41467-018-06990-9; RA Huang N., Zhang D., Li F., Chai P., Wang S., Teng J., Chen J.; RT "M-Phase Phosphoprotein 9 regulates ciliogenesis by modulating CP110-CEP97 RT complex localization at the mother centriole."; RL Nat. Commun. 9:4511-4511(2018). CC -!- FUNCTION: Acts as a key negative regulator of ciliogenesis in CC collaboration with CCP110 by capping the mother centriole thereby CC preventing cilia formation (PubMed:17719545, PubMed:30375385). Required CC for recruitment of CCP110 to the centrosome (PubMed:17719545). CC {ECO:0000269|PubMed:17719545, ECO:0000269|PubMed:30375385}. CC -!- SUBUNIT: Interacts with CALM1, CEP76, CCP110, KIF24, TALPID3. Via its CC interaction with CCP110, may indirectly interact with HERC2 and NEURL4 CC (PubMed:22261722). Interacts with MPHOSPH9 (PubMed:30375385). CC {ECO:0000269|PubMed:17719545, ECO:0000269|PubMed:19460342, CC ECO:0000269|PubMed:21620453, ECO:0000269|PubMed:22261722, CC ECO:0000269|PubMed:24421332, ECO:0000269|PubMed:30375385}. CC -!- INTERACTION: CC Q8IW35; Q562R1: ACTBL2; NbExp=2; IntAct=EBI-1566210, EBI-1773495; CC Q8IW35; O43303: CCP110; NbExp=27; IntAct=EBI-1566210, EBI-1566217; CC Q8IW35; Q5T7B8: KIF24; NbExp=13; IntAct=EBI-1566210, EBI-2556811; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome {ECO:0000269|PubMed:14654843, CC ECO:0000269|PubMed:17719545, ECO:0000269|PubMed:30375385}. Cytoplasm, CC cytoskeleton, microtubule organizing center, centrosome, centriole CC {ECO:0000269|PubMed:30375385}. Note=Recruited at the distal end of the CC mother centriole by MPHOSPH9. {ECO:0000269|PubMed:30375385}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8IW35-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8IW35-2; Sequence=VSP_031155; CC -!- MISCELLANEOUS: [Isoform 2]: Sequence incomplete. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB15531.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC04055.1; Type=Frameshift; 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; AC084198; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC041085; AAH41085.1; -; mRNA. DR EMBL; AK026700; BAB15531.1; ALT_INIT; mRNA. DR EMBL; AK093100; BAC04055.1; ALT_FRAME; mRNA. DR CCDS; CCDS2944.1; -. [Q8IW35-1] DR RefSeq; NP_001290330.1; NM_001303401.1. DR RefSeq; NP_078824.2; NM_024548.3. [Q8IW35-1] DR AlphaFoldDB; Q8IW35; -. DR SMR; Q8IW35; -. DR BioGRID; 122737; 164. DR IntAct; Q8IW35; 57. DR MINT; Q8IW35; -. DR STRING; 9606.ENSP00000342510; -. DR GlyGen; Q8IW35; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8IW35; -. DR MetOSite; Q8IW35; -. DR PhosphoSitePlus; Q8IW35; -. DR BioMuta; CEP97; -. DR DMDM; 74762481; -. DR EPD; Q8IW35; -. DR jPOST; Q8IW35; -. DR MassIVE; Q8IW35; -. DR MaxQB; Q8IW35; -. DR PaxDb; Q8IW35; -. DR PeptideAtlas; Q8IW35; -. DR PRIDE; Q8IW35; -. DR ProteomicsDB; 70798; -. [Q8IW35-1] DR ProteomicsDB; 70799; -. [Q8IW35-2] DR Antibodypedia; 15955; 169 antibodies from 25 providers. DR DNASU; 79598; -. DR Ensembl; ENST00000341893.8; ENSP00000342510.3; ENSG00000182504.11. [Q8IW35-1] DR GeneID; 79598; -. DR KEGG; hsa:79598; -. DR MANE-Select; ENST00000341893.8; ENSP00000342510.3; NM_024548.4; NP_078824.2. DR UCSC; uc003dvk.2; human. [Q8IW35-1] DR CTD; 79598; -. DR DisGeNET; 79598; -. DR GeneCards; CEP97; -. DR HGNC; HGNC:26244; CEP97. DR HPA; ENSG00000182504; Low tissue specificity. DR MIM; 615864; gene. DR neXtProt; NX_Q8IW35; -. DR OpenTargets; ENSG00000182504; -. DR PharmGKB; PA162382176; -. DR VEuPathDB; HostDB:ENSG00000182504; -. DR eggNOG; KOG0531; Eukaryota. DR GeneTree; ENSGT00910000144283; -. DR InParanoid; Q8IW35; -. DR OMA; AYWRGFY; -. DR OrthoDB; 1264004at2759; -. DR PhylomeDB; Q8IW35; -. DR TreeFam; TF320816; -. DR PathwayCommons; Q8IW35; -. DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane. DR Reactome; R-HSA-9013424; RHOV GTPase cycle. DR SignaLink; Q8IW35; -. DR BioGRID-ORCS; 79598; 158 hits in 1088 CRISPR screens. DR ChiTaRS; CEP97; human. DR GeneWiki; CEP97; -. DR GenomeRNAi; 79598; -. DR Pharos; Q8IW35; Tbio. DR PRO; PR:Q8IW35; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q8IW35; protein. DR Bgee; ENSG00000182504; Expressed in corpus callosum and 179 other tissues. DR ExpressionAtlas; Q8IW35; baseline and differential. DR Genevisible; Q8IW35; 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:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW. DR GO; GO:1902018; P:negative regulation of cilium assembly; IMP:UniProtKB. DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:UniProtKB. DR Gene3D; 3.80.10.10; -; 2. DR InterPro; IPR000048; IQ_motif_EF-hand-BS. DR InterPro; IPR001611; Leu-rich_rpt. DR InterPro; IPR032675; LRR_dom_sf. DR PROSITE; PS50096; IQ; 1. DR PROSITE; PS51450; LRR; 7. PE 1: Evidence at protein level; KW Alternative splicing; Calmodulin-binding; Cilium biogenesis/degradation; KW Cytoplasm; Cytoskeleton; Leucine-rich repeat; Phosphoprotein; KW Reference proteome; Repeat. FT CHAIN 1..865 FT /note="Centrosomal protein of 97 kDa" FT /id="PRO_0000263705" FT REPEAT 37..58 FT /note="LRR 1" FT REPEAT 59..80 FT /note="LRR 2" FT REPEAT 81..102 FT /note="LRR 3" FT REPEAT 103..124 FT /note="LRR 4" FT REPEAT 125..146 FT /note="LRR 5" FT REPEAT 147..168 FT /note="LRR 6" FT REPEAT 171..192 FT /note="LRR 7" FT REPEAT 196..205 FT /note="LRR 8" FT DOMAIN 211..249 FT /note="LRRCT" FT DOMAIN 558..587 FT /note="IQ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116" FT REGION 300..750 FT /note="CCP110-binding" FT REGION 506..529 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 587..865 FT /note="Interaction with MPHOSPH9" FT /evidence="ECO:0000269|PubMed:30375385" FT REGION 715..769 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 715..737 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 743..762 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 308 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:23186163" FT MOD_RES 413 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 500 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 530 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9CZ62" FT MOD_RES 542 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17525332" FT MOD_RES 763 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 631 FT /note="Q -> QKWGLAILPRPVSNFWAQAVFPPQPPK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_031155" FT CONFLICT 299..300 FT /note="Missing (in Ref. 3; BAC04055)" FT /evidence="ECO:0000305" FT CONFLICT 399 FT /note="L -> F (in Ref. 3; BAC04055)" FT /evidence="ECO:0000305" FT CONFLICT 758 FT /note="Missing (in Ref. 3; BAB15531)" FT /evidence="ECO:0000305" SQ SEQUENCE 865 AA; 96981 MW; 98B1C230DF586DF7 CRC64; MAVARVDAAL PPGEGSVVNW SGQGLQKLGP NLPCEADIHT LILDKNQIIK LENLEKCKRL IQLSVANNRL VRMMGVAKLT LLRVLNLPHN SIGCVEGLKE LVHLEWLNLA GNNLKAMEQI NSCTALQHLD LSDNNISQIG DLSKLVSLKT LLLHGNIITS LRMAPAYLPR SLAILSLAEN EIRDLNEISF LASLTELEQL SIMNNPCVMA TPSIPGFDYR PYIVSWCLNL RVLDGYVISQ KESLKAEWLY SQGKGRAYRP GQHIQLVQYL ATVCPLTSTL GLQTAEDAKL EKILSKQRFH QRQLMNQSQN EELSPLVPVE TRASLIPEHS SPVQDCQISQ ESEPVIQVNS WVGINSNDDQ LFAVKNNFPA SVHTTRYSRN DLHLEDIQTD EDKLNCSLLS SESTFMPVAS GLSPLSPTVE LRLQGINLGL EDDGVADESV KGLESQVLDK EEEQPLWAAN ENSVQMMRSE INTEVNEKAG LLPCPEPTII SAILKDDNHS LTFFPESTEQ KQSDIKKPEN TQPENKETIS QATSEKLPMI LTQRSVALGQ DKVALQKLND AATKLQACWR GFYARNYNPQ AKDVRYEIRL RRMQEHIVCL TDEIRRLRKE RDEERIKKFV QEEAFRFLWN QVRSLQVWQQ TVDQRLSSWH TDVPPISSTL VPSKHPLFTQ SQESSCDQNA DWFIASDVAP QEKSLPEFPD SGFHSSLTEQ VHSLQHSLDF EKSSTEGSES SIMGNSIDTV RYGKESDLGD VSEEHGEWNK ESSNNEQDNS LLEQYLTSVQ QLEDADERTN FDTETRDSKL HIACFPVQLD TLSDGASVDE SHGISPPLQG EISQTQENSK LNAEVQGQQP ECDSTFQLLH VGVTV //