ID TCPE_HUMAN Reviewed; 541 AA. AC P48643; A8JZY8; A8K2X8; B4DYD8; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 27-MAR-2024, entry version 220. DE RecName: Full=T-complex protein 1 subunit epsilon; DE Short=TCP-1-epsilon; DE AltName: Full=CCT-epsilon; GN Name=CCT5; Synonyms=CCTE, KIAA0098 {ECO:0000303|PubMed:7788527}; 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 1). RC TISSUE=Bone marrow; RX PubMed=7788527; DOI=10.1093/dnares/2.1.37; RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. III. The RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of RT cDNA clones from human cell line KG-1."; RL DNA Res. 2:37-43(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Testis, and Umbilical cord blood; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung, and Uterus; 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 PROTEIN SEQUENCE OF 2-24; 28-35; 50-59; 90-96; 133-170; 184-201; 203-214; RP 248-261; 264-275; 283-293; 324-340; 345-368; 382-388; 393-399; 401-410; RP 484-496; 514-525 AND 530-541, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION RP AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lung carcinoma; RA Bienvenut W.V., Vousden K.H., Lukashchuk N.; RL Submitted (MAR-2008) to UniProtKB. RN [7] RP PROTEIN SEQUENCE OF 2-20; 97-126; 133-170; 184-201; 203-214; 266-275; RP 294-340; 345-368; 382-388 AND 401-410, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RA Bienvenut W.V., Waridel P., Quadroni M.; RL Submitted (MAR-2009) to UniProtKB. RN [8] RP PROTEIN SEQUENCE OF 203-210; 248-261; 324-340; 353-368 AND 515-525, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [9] RP INTERACTION WITH PACRG. RX PubMed=14532270; DOI=10.1074/jbc.m309655200; RA Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.; RT "A product of the human gene adjacent to parkin is a component of Lewy RT bodies and suppresses Pael receptor-induced cell death."; RL J. Biol. Chem. 278:51901-51910(2003). RN [10] 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 [11] RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x; RA Leong W.F., Chow V.T.; RT "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal RT differential cellular gene expression in response to enterovirus 71 RT infection."; RL Cell. Microbiol. 8:565-580(2006). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN CHAPERONIN-CONTAINING RP T-COMPLEX. RX PubMed=20080638; DOI=10.1073/pnas.0910268107; RA Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C., RA Sheffield V.C.; RT "BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and RT mediate BBSome assembly."; RL Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010). RN [14] 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346 AND SER-539, 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). RN [19] RP FUNCTION, AND IDENTIFICATION IN THE CHAPERONIN-CONTAINING T-COMPLEX. RX PubMed=25467444; DOI=10.1016/j.cell.2014.10.059; RA Freund A., Zhong F.L., Venteicher A.S., Meng Z., Veenstra T.D., Frydman J., RA Artandi S.E.; RT "Proteostatic control of telomerase function through TRiC-mediated folding RT of TCAB1."; RL Cell 159:1389-1403(2014). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [22] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20; LYS-210; LYS-214; LYS-265; RP LYS-275; LYS-279 AND LYS-392, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [23] RP UBIQUITINATION. RX PubMed=29779948; DOI=10.1016/j.cell.2018.04.028; RA Koren I., Timms R.T., Kula T., Xu Q., Li M.Z., Elledge S.J.; RT "The eukaryotic proteome is shaped by E3 ubiquitin ligases targeting C- RT terminal degrons."; RL Cell 173:1622-1635(2018). RN [24] RP INTERACTION WITH DLEC1. RX PubMed=33144677; DOI=10.1038/s41598-020-75957-y; RA Okitsu Y., Nagano M., Yamagata T., Ito C., Toshimori K., Dohra H., RA Fujii W., Yogo K.; RT "Dlec1 is required for spermatogenesis and male fertility in mice."; RL Sci. Rep. 10:18883-18883(2020). RN [25] RP VARIANT HSNSP ARG-147. RX PubMed=16399879; DOI=10.1136/jmg.2005.039230; RA Bouhouche A., Benomar A., Bouslam N., Chkili T., Yahyaoui M.; RT "Mutation in the epsilon subunit of the cytosolic chaperonin-containing T- RT complex peptide-1 (Cct5) gene causes autosomal recessive mutilating sensory RT neuropathy with spastic paraplegia."; RL J. Med. Genet. 43:441-443(2006). CC -!- FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a CC molecular chaperone complex that assists the folding of proteins upon CC ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding CC of WRAP53/TCAB1, thereby regulating telomere maintenance CC (PubMed:25467444). As part of the TRiC complex may play a role in the CC assembly of BBSome, a complex involved in ciliogenesis regulating CC transports vesicles to the cilia (PubMed:20080638). The TRiC complex CC plays a role in the folding of actin and tubulin (Probable). CC {ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444, CC ECO:0000305}. CC -!- SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a CC heterooligomeric complex of about 850 to 900 kDa that forms two stacked CC rings, 12 to 16 nm in diameter (PubMed:20080638, PubMed:25467444). CC Interacts with PACRG (PubMed:14532270). Interacts with DNAAF4 (By CC similarity). Interacts with DLEC1 (PubMed:33144677). Interacts with CC SPMAP2 (By similarity). {ECO:0000250|UniProtKB:P80316, CC ECO:0000269|PubMed:14532270, ECO:0000269|PubMed:20080638, CC ECO:0000269|PubMed:25467444, ECO:0000269|PubMed:33144677}. CC -!- INTERACTION: CC P48643; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-355710, EBI-2875816; CC P48643; P54253: ATXN1; NbExp=3; IntAct=EBI-355710, EBI-930964; CC P48643; O95817: BAG3; NbExp=3; IntAct=EBI-355710, EBI-747185; CC P48643; Q14457: BECN1; NbExp=3; IntAct=EBI-355710, EBI-949378; CC P48643; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-355710, EBI-350590; CC P48643; Q9H9Q2: COPS7B; NbExp=3; IntAct=EBI-355710, EBI-2510162; CC P48643; Q6NXG1: ESRP1; NbExp=3; IntAct=EBI-355710, EBI-10213520; CC P48643; Q9UKC9: FBXL2; NbExp=3; IntAct=EBI-355710, EBI-724253; CC P48643; Q9NXC2: GFOD1; NbExp=3; IntAct=EBI-355710, EBI-8799578; CC P48643; O75409: H2AP; NbExp=3; IntAct=EBI-355710, EBI-6447217; CC P48643; P52790: HK3; NbExp=3; IntAct=EBI-355710, EBI-2965780; CC P48643; P49639: HOXA1; NbExp=3; IntAct=EBI-355710, EBI-740785; CC P48643; P42858: HTT; NbExp=3; IntAct=EBI-355710, EBI-466029; CC P48643; Q14525: KRT33B; NbExp=3; IntAct=EBI-355710, EBI-1049638; CC P48643; Q68G74: LHX8; NbExp=3; IntAct=EBI-355710, EBI-8474075; CC P48643; A2RU56: LOC401296; NbExp=3; IntAct=EBI-355710, EBI-9088215; CC P48643; Q1L5Z9: LONRF2; NbExp=3; IntAct=EBI-355710, EBI-2510853; CC P48643; O15130-2: NPFF; NbExp=3; IntAct=EBI-355710, EBI-25840002; CC P48643; Q96LB9: PGLYRP3; NbExp=3; IntAct=EBI-355710, EBI-12339509; CC P48643; O75925: PIAS1; NbExp=3; IntAct=EBI-355710, EBI-629434; CC P48643; Q6ZR37: PLEKHG7; NbExp=3; IntAct=EBI-355710, EBI-12891828; CC P48643; Q9H0F5-2: RNF38; NbExp=3; IntAct=EBI-355710, EBI-25866807; CC P48643; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-355710, EBI-9089805; CC P48643; O60902-3: SHOX2; NbExp=3; IntAct=EBI-355710, EBI-9092164; CC P48643; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-355710, EBI-11959123; CC P48643; O75886: STAM2; NbExp=3; IntAct=EBI-355710, EBI-373258; CC P48643; O95630: STAMBP; NbExp=3; IntAct=EBI-355710, EBI-396676; CC P48643; A1L378: STRC; NbExp=3; IntAct=EBI-355710, EBI-22013242; CC P48643; O60220: TIMM8A; NbExp=3; IntAct=EBI-355710, EBI-1049822; CC P48643; P04637: TP53; NbExp=3; IntAct=EBI-355710, EBI-366083; CC P48643; Q9UGJ1-2: TUBGCP4; NbExp=3; IntAct=EBI-355710, EBI-10964469; CC P48643; Q96B02: UBE2W; NbExp=3; IntAct=EBI-355710, EBI-716589; CC P48643; P45880: VDAC2; NbExp=3; IntAct=EBI-355710, EBI-354022; CC P48643; O00308: WWP2; NbExp=6; IntAct=EBI-355710, EBI-743923; CC P48643; Q96N77-2: ZNF641; NbExp=3; IntAct=EBI-355710, EBI-12939666; CC P48643; O60232: ZNRD2; NbExp=4; IntAct=EBI-355710, EBI-741415; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20080638}. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:20080638}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P48643-1; Sequence=Displayed; CC Name=2; CC IsoId=P48643-2; Sequence=VSP_054005, VSP_054006; CC -!- INDUCTION: Down-regulated in response to enterovirus 71 (EV71) CC infection (at protein level). {ECO:0000269|PubMed:16548883}. CC -!- PTM: Ubiquitinated by the DCX(DCAF12) complex specifically recognizes CC the diglutamate (Glu-Glu) at the C-terminus, leading to its CC degradation. {ECO:0000269|PubMed:29779948}. CC -!- DISEASE: Neuropathy, hereditary sensory, with spastic paraplegia, CC autosomal recessive (HSNSP) [MIM:256840]: A disease characterized by CC spastic paraplegia and progressive distal sensory neuropathy leading to CC mutilating ulcerations of the upper and lower limbs. CC {ECO:0000269|PubMed:16399879}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA07894.2; Type=Erroneous initiation; 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; D43950; BAA07894.2; ALT_INIT; mRNA. DR EMBL; AK289353; BAF82042.1; -; mRNA. DR EMBL; AK290393; BAF83082.1; -; mRNA. DR EMBL; AK302383; BAG63700.1; -; mRNA. DR EMBL; AC012640; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471102; EAX08072.1; -; Genomic_DNA. DR EMBL; BC006543; AAH06543.1; -; mRNA. DR EMBL; BC035499; AAH35499.1; -; mRNA. DR CCDS; CCDS3877.1; -. [P48643-1] DR CCDS; CCDS82990.1; -. [P48643-2] DR RefSeq; NP_001293084.1; NM_001306155.1. [P48643-2] DR RefSeq; NP_036205.1; NM_012073.4. [P48643-1] DR PDB; 5UYX; X-ray; 3.50 A; A/B/C/D=1-541. DR PDB; 5UYZ; X-ray; 3.60 A; A/B/C/D=1-541. DR PDB; 6NR8; EM; 7.80 A; E/M=25-541. DR PDB; 6NR9; EM; 8.50 A; E/M=25-541. DR PDB; 6NRA; EM; 7.70 A; E/M=25-541. DR PDB; 6NRB; EM; 8.70 A; E/M=25-541. DR PDB; 6NRC; EM; 8.30 A; E/M=25-541. DR PDB; 6NRD; EM; 8.20 A; E/M=25-541. DR PDB; 6QB8; EM; 3.97 A; E/e=1-541. DR PDB; 7LUM; EM; 4.50 A; D/L=1-541. DR PDB; 7LUP; EM; 6.20 A; D/L=1-541. DR PDB; 7NVL; EM; 2.50 A; E/e=1-541. DR PDB; 7NVM; EM; 3.10 A; E/e=1-541. DR PDB; 7NVN; EM; 3.00 A; E/e=1-541. DR PDB; 7NVO; EM; 3.50 A; E/e=1-541. DR PDB; 7TRG; EM; 3.00 A; D=1-541. DR PDB; 7TTN; EM; 3.30 A; D=1-541. DR PDB; 7TTT; EM; 2.90 A; D=1-541. DR PDB; 7TUB; EM; 3.60 A; D=1-541. DR PDB; 7WU7; EM; 3.85 A; E/M=1-541. DR PDB; 7WZ3; EM; 4.10 A; E/e=3-541. DR PDB; 7X0A; EM; 3.10 A; E/e=3-541. DR PDB; 7X0S; EM; 3.10 A; E/e=3-541. DR PDB; 7X0V; EM; 3.20 A; E/e=3-541. DR PDB; 7X3J; EM; 4.20 A; E/e=3-541. DR PDB; 7X3U; EM; 3.30 A; E/e=3-541. DR PDB; 7X6Q; EM; 4.50 A; E/e=3-541. DR PDB; 7X7Y; EM; 3.80 A; E/e=3-541. DR PDB; 8AJM; EM; 2.83 A; C=1-541. DR PDB; 8AJO; EM; 30.60 A; C=1-541. DR PDB; 8SFE; EM; 3.36 A; E/e=2-541. DR PDB; 8SFF; EM; 3.20 A; E/e=2-541. DR PDB; 8SG8; EM; 3.00 A; E/e=2-541. DR PDB; 8SG9; EM; 2.90 A; E/e=2-541. DR PDB; 8SGC; EM; 2.90 A; E/e=2-541. DR PDB; 8SGL; EM; 2.90 A; E/e=2-541. DR PDB; 8SGQ; EM; 3.70 A; E/e=2-541. DR PDB; 8SH9; EM; 2.70 A; E/e=2-541. DR PDB; 8SHA; EM; 3.00 A; E/e=2-541. DR PDB; 8SHD; EM; 2.90 A; E/e=2-541. DR PDB; 8SHE; EM; 2.80 A; E/e=2-541. DR PDB; 8SHF; EM; 3.00 A; E/e=2-541. DR PDB; 8SHG; EM; 2.80 A; E/e=2-541. DR PDB; 8SHL; EM; 3.00 A; E/e=2-541. DR PDB; 8SHN; EM; 2.80 A; E/e=2-541. DR PDB; 8SHO; EM; 3.00 A; E/e=2-541. DR PDB; 8SHP; EM; 3.00 A; E/e=2-541. DR PDB; 8SHQ; EM; 2.90 A; E/e=2-541. DR PDB; 8SHT; EM; 3.00 A; E/e=2-541. DR PDBsum; 5UYX; -. DR PDBsum; 5UYZ; -. DR PDBsum; 6NR8; -. DR PDBsum; 6NR9; -. DR PDBsum; 6NRA; -. DR PDBsum; 6NRB; -. DR PDBsum; 6NRC; -. DR PDBsum; 6NRD; -. DR PDBsum; 6QB8; -. DR PDBsum; 7LUM; -. DR PDBsum; 7LUP; -. DR PDBsum; 7NVL; -. DR PDBsum; 7NVM; -. DR PDBsum; 7NVN; -. DR PDBsum; 7NVO; -. DR PDBsum; 7TRG; -. DR PDBsum; 7TTN; -. DR PDBsum; 7TTT; -. DR PDBsum; 7TUB; -. DR PDBsum; 7WU7; -. DR PDBsum; 7WZ3; -. DR PDBsum; 7X0A; -. DR PDBsum; 7X0S; -. DR PDBsum; 7X0V; -. DR PDBsum; 7X3J; -. DR PDBsum; 7X3U; -. DR PDBsum; 7X6Q; -. DR PDBsum; 7X7Y; -. DR PDBsum; 8AJM; -. DR PDBsum; 8AJO; -. DR PDBsum; 8SFE; -. DR PDBsum; 8SFF; -. DR PDBsum; 8SG8; -. DR PDBsum; 8SG9; -. DR PDBsum; 8SGC; -. DR PDBsum; 8SGL; -. DR PDBsum; 8SGQ; -. DR PDBsum; 8SH9; -. DR PDBsum; 8SHA; -. DR PDBsum; 8SHD; -. DR PDBsum; 8SHE; -. DR PDBsum; 8SHF; -. DR PDBsum; 8SHG; -. DR PDBsum; 8SHL; -. DR PDBsum; 8SHN; -. DR PDBsum; 8SHO; -. DR PDBsum; 8SHP; -. DR PDBsum; 8SHQ; -. DR PDBsum; 8SHT; -. DR AlphaFoldDB; P48643; -. DR EMDB; EMD-0490; -. DR EMDB; EMD-0491; -. DR EMDB; EMD-0492; -. DR EMDB; EMD-0493; -. DR EMDB; EMD-0494; -. DR EMDB; EMD-0495; -. DR EMDB; EMD-12605; -. DR EMDB; EMD-12606; -. DR EMDB; EMD-12607; -. DR EMDB; EMD-12608; -. DR EMDB; EMD-13754; -. DR EMDB; EMD-15484; -. DR EMDB; EMD-15486; -. DR EMDB; EMD-23522; -. DR EMDB; EMD-23526; -. DR EMDB; EMD-26089; -. DR EMDB; EMD-26120; -. DR EMDB; EMD-26123; -. DR EMDB; EMD-26131; -. DR EMDB; EMD-2947; -. DR EMDB; EMD-2962; -. DR EMDB; EMD-2963; -. DR EMDB; EMD-32823; -. DR EMDB; EMD-32903; -. DR EMDB; EMD-32922; -. DR EMDB; EMD-32923; -. DR EMDB; EMD-32926; -. DR EMDB; EMD-32989; -. DR EMDB; EMD-32993; -. DR EMDB; EMD-33025; -. DR EMDB; EMD-33053; -. DR EMDB; EMD-40439; -. DR EMDB; EMD-40440; -. DR EMDB; EMD-40452; -. DR EMDB; EMD-40453; -. DR EMDB; EMD-40454; -. DR EMDB; EMD-40461; -. DR EMDB; EMD-40464; -. DR EMDB; EMD-40481; -. DR EMDB; EMD-40482; -. DR EMDB; EMD-40484; -. DR EMDB; EMD-40485; -. DR EMDB; EMD-40486; -. DR EMDB; EMD-40487; -. DR EMDB; EMD-40488; -. DR EMDB; EMD-40489; -. DR EMDB; EMD-40490; -. DR EMDB; EMD-40491; -. DR EMDB; EMD-40492; -. DR EMDB; EMD-40494; -. DR EMDB; EMD-4489; -. DR EMDB; EMD-5640; -. DR EMDB; EMD-5641; -. DR SMR; P48643; -. DR BioGRID; 116603; 538. DR ComplexPortal; CPX-6030; Chaperonin-containing T-complex. DR CORUM; P48643; -. DR DIP; DIP-31181N; -. DR IntAct; P48643; 250. DR MINT; P48643; -. DR STRING; 9606.ENSP00000280326; -. DR ChEMBL; CHEMBL4295766; -. DR GlyGen; P48643; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P48643; -. DR MetOSite; P48643; -. DR PhosphoSitePlus; P48643; -. DR SwissPalm; P48643; -. DR BioMuta; CCT5; -. DR DMDM; 1351211; -. DR OGP; P48643; -. DR REPRODUCTION-2DPAGE; IPI00010720; -. DR SWISS-2DPAGE; P48643; -. DR EPD; P48643; -. DR jPOST; P48643; -. DR MassIVE; P48643; -. DR MaxQB; P48643; -. DR PaxDb; 9606-ENSP00000280326; -. DR PeptideAtlas; P48643; -. DR PRIDE; P48643; -. DR ProteomicsDB; 5518; -. DR ProteomicsDB; 55918; -. [P48643-1] DR Pumba; P48643; -. DR ABCD; P48643; 1 sequenced antibody. DR Antibodypedia; 1210; 375 antibodies from 34 providers. DR DNASU; 22948; -. DR Ensembl; ENST00000280326.9; ENSP00000280326.4; ENSG00000150753.12. [P48643-1] DR Ensembl; ENST00000506600.1; ENSP00000423052.1; ENSG00000150753.12. [P48643-2] DR GeneID; 22948; -. DR KEGG; hsa:22948; -. DR MANE-Select; ENST00000280326.9; ENSP00000280326.4; NM_012073.5; NP_036205.1. DR UCSC; uc011cmt.3; human. [P48643-1] DR AGR; HGNC:1618; -. DR CTD; 22948; -. DR DisGeNET; 22948; -. DR GeneCards; CCT5; -. DR HGNC; HGNC:1618; CCT5. DR HPA; ENSG00000150753; Low tissue specificity. DR MalaCards; CCT5; -. DR MIM; 256840; phenotype. DR MIM; 610150; gene. DR neXtProt; NX_P48643; -. DR OpenTargets; ENSG00000150753; -. DR Orphanet; 139578; Mutilating hereditary sensory neuropathy with spastic paraplegia. DR PharmGKB; PA26182; -. DR VEuPathDB; HostDB:ENSG00000150753; -. DR eggNOG; KOG0357; Eukaryota. DR GeneTree; ENSGT00550000074988; -. DR InParanoid; P48643; -. DR OMA; SHPQMPH; -. DR OrthoDB; 212971at2759; -. DR PhylomeDB; P48643; -. DR TreeFam; TF105638; -. DR BRENDA; 3.6.4.B10; 2681. DR PathwayCommons; P48643; -. DR Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC. DR Reactome; R-HSA-389960; Formation of tubulin folding intermediates by CCT/TriC. DR Reactome; R-HSA-390450; Folding of actin by CCT/TriC. DR Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis. DR Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium. DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding. DR SignaLink; P48643; -. DR SIGNOR; P48643; -. DR BioGRID-ORCS; 22948; 788 hits in 1150 CRISPR screens. DR ChiTaRS; CCT5; human. DR GeneWiki; CCT5_(gene); -. DR GenomeRNAi; 22948; -. DR Pharos; P48643; Tbio. DR PRO; PR:P48643; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; P48643; Protein. DR Bgee; ENSG00000150753; Expressed in primordial germ cell in gonad and 211 other cell types or tissues. DR ExpressionAtlas; P48643; baseline and differential. DR Genevisible; P48643; HS. DR GO; GO:0044297; C:cell body; IEA:Ensembl. DR GO; GO:0005813; C:centrosome; IDA:MGI. DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005874; C:microtubule; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro. DR GO; GO:0048487; F:beta-tubulin binding; IPI:UniProtKB. DR GO; GO:0031681; F:G-protein beta-subunit binding; IPI:UniProtKB. DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:CAFA. DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:CAFA. DR GO; GO:0044183; F:protein folding chaperone; IDA:FlyBase. DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central. DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl. DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:ComplexPortal. DR GO; GO:1904851; P:positive regulation of establishment of protein localization to telomere; IMP:BHF-UCL. DR GO; GO:1904871; P:positive regulation of protein localization to Cajal body; HMP:BHF-UCL. DR GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; HMP:BHF-UCL. DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:BHF-UCL. DR GO; GO:0006457; P:protein folding; IDA:FlyBase. DR GO; GO:0050821; P:protein stabilization; IMP:BHF-UCL. DR GO; GO:0009615; P:response to virus; IEP:UniProtKB. DR CDD; cd03339; TCP1_epsilon; 1. DR Gene3D; 3.50.7.10; GroEL; 1. DR Gene3D; 1.10.560.10; GroEL-like equatorial domain; 1. DR Gene3D; 3.30.260.10; TCP-1-like chaperonin intermediate domain; 1. DR InterPro; IPR012718; Chap_CCT_epsi. DR InterPro; IPR017998; Chaperone_TCP-1. DR InterPro; IPR002194; Chaperonin_TCP-1_CS. DR InterPro; IPR002423; Cpn60/GroEL/TCP-1. DR InterPro; IPR027409; GroEL-like_apical_dom_sf. DR InterPro; IPR027413; GROEL-like_equatorial_sf. DR InterPro; IPR027410; TCP-1-like_intermed_sf. DR NCBIfam; TIGR02343; chap_CCT_epsi; 1. DR NCBIfam; NF041082; thermosome_alpha; 1. DR NCBIfam; NF041083; thermosome_beta; 1. DR PANTHER; PTHR11353; CHAPERONIN; 1. DR PANTHER; PTHR11353:SF94; T-COMPLEX PROTEIN 1 SUBUNIT EPSILON; 1. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00304; TCOMPLEXTCP1. DR SUPFAM; SSF52029; GroEL apical domain-like; 1. DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1. DR SUPFAM; SSF54849; GroEL-intermediate domain like; 1. DR PROSITE; PS00750; TCP1_1; 1. DR PROSITE; PS00751; TCP1_2; 1. DR PROSITE; PS00995; TCP1_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Chaperone; KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease variant; KW Isopeptide bond; Neuropathy; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.6, ECO:0000269|Ref.7, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712" FT CHAIN 2..541 FT /note="T-complex protein 1 subunit epsilon" FT /id="PRO_0000128346" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.6, ECO:0000269|Ref.7, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712" FT MOD_RES 26 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 346 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 539 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 20 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 210 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 214 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 265 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 275 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 279 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 392 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..38 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054005" FT VAR_SEQ 56..110 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054006" FT VARIANT 146 FT /note="E -> V (in dbSNP:rs11557652)" FT /id="VAR_052267" FT VARIANT 147 FT /note="H -> R (in HSNSP; dbSNP:rs118203986)" FT /evidence="ECO:0000269|PubMed:16399879" FT /id="VAR_030658" FT CONFLICT 55 FT /note="N -> D (in Ref. 2; BAF83082)" FT /evidence="ECO:0000305" FT CONFLICT 512 FT /note="G -> D (in Ref. 2; BAF83082)" FT /evidence="ECO:0000305" FT STRAND 11..14 FT /evidence="ECO:0007829|PDB:7NVN" FT TURN 20..24 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 26..29 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 31..48 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 49..51 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 58..62 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 63..65 FT /evidence="ECO:0007829|PDB:7NVO" FT STRAND 68..71 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 74..80 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 86..101 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 108..125 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 130..151 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 158..160 FT /evidence="ECO:0007829|PDB:7X0S" FT HELIX 163..173 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 177..181 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 182..195 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 199..202 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 206..208 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 209..217 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 219..221 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 223..231 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 234..236 FT /evidence="ECO:0007829|PDB:7X0A" FT STRAND 241..251 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 255..257 FT /evidence="ECO:0007829|PDB:7X0A" FT STRAND 261..268 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 271..294 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 298..304 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 308..316 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 327..337 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 341..344 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 345..347 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 350..352 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 354..363 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 365..367 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 370..375 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 383..391 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 392..414 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 417..420 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 421..423 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 424..439 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 442..444 FT /evidence="ECO:0007829|PDB:7NVM" FT HELIX 445..455 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 457..465 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 470..483 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 501..504 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 507..509 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 510..528 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 530..535 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 536..538 FT /evidence="ECO:0007829|PDB:7X0S" SQ SEQUENCE 541 AA; 59671 MW; 164168BB80EF022A CRC64; MASMGTLAFD EYGRPFLIIK DQDRKSRLMG LEALKSHIMA AKAVANTMRT SLGPNGLDKM MVDKDGDVTV TNDGATILSM MDVDHQIAKL MVELSKSQDD EIGDGTTGVV VLAGALLEEA EQLLDRGIHP IRIADGYEQA ARVAIEHLDK ISDSVLVDIK DTEPLIQTAK TTLGSKVVNS CHRQMAEIAV NAVLTVADME RRDVDFELIK VEGKVGGRLE DTKLIKGVIV DKDFSHPQMP KKVEDAKIAI LTCPFEPPKP KTKHKLDVTS VEDYKALQKY EKEKFEEMIQ QIKETGANLA ICQWGFDDEA NHLLLQNNLP AVRWVGGPEI ELIAIATGGR IVPRFSELTA EKLGFAGLVQ EISFGTTKDK MLVIEQCKNS RAVTIFIRGG NKMIIEEAKR SLHDALCVIR NLIRDNRVVY GGGAAEISCA LAVSQEADKC PTLEQYAMRA FADALEVIPM ALSENSGMNP IQTMTEVRAR QVKEMNPALG IDCLHKGTND MKQQHVIETL IGKKQQISLA TQMVRMILKI DDIRKPGESE E //