CEP97_HUMAN
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};
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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
