Full text data of CCT5
CCT5
(CCTE, KIAA0098)
[Confidence: high (present in two of the MS resources)]
T-complex protein 1 subunit epsilon; TCP-1-epsilon (CCT-epsilon)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
T-complex protein 1 subunit epsilon; TCP-1-epsilon (CCT-epsilon)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00010720
IPI00010720 T-complex protein 1, epsilon subunit Bone marrow, Molecular chaperone; assist the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00010720 T-complex protein 1, epsilon subunit Bone marrow, Molecular chaperone; assist the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P48643
ID TCPE_HUMAN Reviewed; 541 AA.
AC P48643; A8JZY8;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1996, sequence version 1.
DT 22-JAN-2014, entry version 139.
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;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III.
RT The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-24; 28-35; 50-59; 90-96; 133-170; 184-201;
RP 203-214; 248-261; 264-275; 283-293; 324-340; 345-368; 382-388;
RP 393-399; 401-410; 484-496; 514-525 AND 530-541, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL Submitted (MAR-2008) to UniProtKB.
RN [6]
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
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 203-210; 248-261; 324-340; 353-368 AND 515-525,
RP AND 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 [8]
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 [9]
RP INDUCTION, AND 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
RT reveal differential cellular gene expression in response to
RT enterovirus 71 infection.";
RL Cell. Microbiol. 8:565-580(2006).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN BBS/CCT 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
RT chaperonins and mediate BBSome assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010).
RN [12]
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.,
RA Buerckstuemmer T., 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
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-
RT containing T-complex peptide-1 (Cct5) gene causes autosomal recessive
RT mutilating sensory neuropathy with spastic paraplegia.";
RL J. Med. Genet. 43:441-443(2006).
CC -!- FUNCTION: Molecular chaperone; assists the folding of proteins
CC upon ATP hydrolysis. As part of the BBS/CCT complex may play a
CC role in the assembly of BBSome, a complex involved in ciliogenesis
CC regulating transports vesicles to the cilia. Known to play a role,
CC in vitro, in the folding of actin and tubulin.
CC -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that
CC forms two stacked rings, 12 to 16 nm in diameter. Interacts with
CC PACRG. Component of the BBS/CCT complex composed at least of MKKS,
CC BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome.
CC -!- INDUCTION: Down-regulated in response to enterovirus 71 (EV71)
CC infection (at protein level).
CC -!- DISEASE: Hereditary sensory neuropathy, autosomal recessive, with
CC spastic paraplegia (HSNSP) [MIM:256840]: A disease characterized
CC by spastic paraplegia and progressive distal sensory neuropathy
CC leading to mutilating ulcerations of the upper and lower limbs.
CC Note=The disease is caused by mutations affecting the gene
CC represented in this entry.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA07894.2; Type=Erroneous initiation;
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DR EMBL; D43950; BAA07894.2; ALT_INIT; mRNA.
DR EMBL; AK289353; BAF82042.1; -; mRNA.
DR EMBL; CH471102; EAX08072.1; -; Genomic_DNA.
DR EMBL; BC006543; AAH06543.1; -; mRNA.
DR EMBL; BC035499; AAH35499.1; -; mRNA.
DR RefSeq; NP_036205.1; NM_012073.3.
DR UniGene; Hs.1600; -.
DR ProteinModelPortal; P48643; -.
DR SMR; P48643; 18-537.
DR DIP; DIP-31181N; -.
DR IntAct; P48643; 46.
DR MINT; MINT-1154718; -.
DR STRING; 9606.ENSP00000280326; -.
DR PhosphoSite; P48643; -.
DR DMDM; 1351211; -.
DR OGP; P48643; -.
DR REPRODUCTION-2DPAGE; IPI00010720; -.
DR SWISS-2DPAGE; P48643; -.
DR PaxDb; P48643; -.
DR PeptideAtlas; P48643; -.
DR PRIDE; P48643; -.
DR DNASU; 22948; -.
DR Ensembl; ENST00000280326; ENSP00000280326; ENSG00000150753.
DR GeneID; 22948; -.
DR KEGG; hsa:22948; -.
DR UCSC; uc003jeq.3; human.
DR CTD; 22948; -.
DR GeneCards; GC05P010236; -.
DR H-InvDB; HIX0120997; -.
DR HGNC; HGNC:1618; CCT5.
DR HPA; CAB006271; -.
DR HPA; HPA002238; -.
DR HPA; HPA005958; -.
DR MIM; 256840; phenotype.
DR MIM; 610150; gene.
DR neXtProt; NX_P48643; -.
DR Orphanet; 139578; Hereditary sensory and autonomic neuropathy with spastic paraplegia.
DR PharmGKB; PA26182; -.
DR eggNOG; COG0459; -.
DR HOGENOM; HOG000226735; -.
DR HOVERGEN; HBG106507; -.
DR InParanoid; P48643; -.
DR KO; K09497; -.
DR OMA; MRAFASA; -.
DR OrthoDB; EOG722J8B; -.
DR PhylomeDB; P48643; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; CCT5; human.
DR GeneWiki; CCT5_(gene); -.
DR GenomeRNAi; 22948; -.
DR NextBio; 43711; -.
DR PRO; PR:P48643; -.
DR ArrayExpress; P48643; -.
DR Bgee; P48643; -.
DR CleanEx; HS_CCT5; -.
DR Genevestigator; P48643; -.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0002199; C:zona pellucida receptor complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR Gene3D; 1.10.560.10; -; 2.
DR Gene3D; 3.30.260.10; -; 2.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012718; Chap_CCT_epsi.
DR InterPro; IPR017998; Chaperone_TCP-1.
DR InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR InterPro; IPR002423; Cpn60/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom.
DR InterPro; IPR027413; GROEL-like_equatorial.
DR InterPro; IPR027410; TCP-1-like_intermed.
DR PANTHER; PTHR11353; PTHR11353; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF48592; SSF48592; 2.
DR SUPFAM; SSF52029; SSF52029; 1.
DR TIGRFAMs; TIGR02343; chap_CCT_epsi; 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 Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Disease mutation; Neuropathy;
KW Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 541 T-complex protein 1 subunit epsilon.
FT /FTId=PRO_0000128346.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 26 26 Phosphoserine.
FT VARIANT 146 146 E -> V (in dbSNP:rs11557652).
FT /FTId=VAR_052267.
FT VARIANT 147 147 H -> R (in HSNSP).
FT /FTId=VAR_030658.
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
//
ID TCPE_HUMAN Reviewed; 541 AA.
AC P48643; A8JZY8;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1996, sequence version 1.
DT 22-JAN-2014, entry version 139.
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;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III.
RT The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-24; 28-35; 50-59; 90-96; 133-170; 184-201;
RP 203-214; 248-261; 264-275; 283-293; 324-340; 345-368; 382-388;
RP 393-399; 401-410; 484-496; 514-525 AND 530-541, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL Submitted (MAR-2008) to UniProtKB.
RN [6]
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
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 203-210; 248-261; 324-340; 353-368 AND 515-525,
RP AND 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 [8]
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 [9]
RP INDUCTION, AND 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
RT reveal differential cellular gene expression in response to
RT enterovirus 71 infection.";
RL Cell. Microbiol. 8:565-580(2006).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN BBS/CCT 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
RT chaperonins and mediate BBSome assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010).
RN [12]
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.,
RA Buerckstuemmer T., 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
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-
RT containing T-complex peptide-1 (Cct5) gene causes autosomal recessive
RT mutilating sensory neuropathy with spastic paraplegia.";
RL J. Med. Genet. 43:441-443(2006).
CC -!- FUNCTION: Molecular chaperone; assists the folding of proteins
CC upon ATP hydrolysis. As part of the BBS/CCT complex may play a
CC role in the assembly of BBSome, a complex involved in ciliogenesis
CC regulating transports vesicles to the cilia. Known to play a role,
CC in vitro, in the folding of actin and tubulin.
CC -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that
CC forms two stacked rings, 12 to 16 nm in diameter. Interacts with
CC PACRG. Component of the BBS/CCT complex composed at least of MKKS,
CC BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome.
CC -!- INDUCTION: Down-regulated in response to enterovirus 71 (EV71)
CC infection (at protein level).
CC -!- DISEASE: Hereditary sensory neuropathy, autosomal recessive, with
CC spastic paraplegia (HSNSP) [MIM:256840]: A disease characterized
CC by spastic paraplegia and progressive distal sensory neuropathy
CC leading to mutilating ulcerations of the upper and lower limbs.
CC Note=The disease is caused by mutations affecting the gene
CC represented in this entry.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA07894.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; D43950; BAA07894.2; ALT_INIT; mRNA.
DR EMBL; AK289353; BAF82042.1; -; mRNA.
DR EMBL; CH471102; EAX08072.1; -; Genomic_DNA.
DR EMBL; BC006543; AAH06543.1; -; mRNA.
DR EMBL; BC035499; AAH35499.1; -; mRNA.
DR RefSeq; NP_036205.1; NM_012073.3.
DR UniGene; Hs.1600; -.
DR ProteinModelPortal; P48643; -.
DR SMR; P48643; 18-537.
DR DIP; DIP-31181N; -.
DR IntAct; P48643; 46.
DR MINT; MINT-1154718; -.
DR STRING; 9606.ENSP00000280326; -.
DR PhosphoSite; P48643; -.
DR DMDM; 1351211; -.
DR OGP; P48643; -.
DR REPRODUCTION-2DPAGE; IPI00010720; -.
DR SWISS-2DPAGE; P48643; -.
DR PaxDb; P48643; -.
DR PeptideAtlas; P48643; -.
DR PRIDE; P48643; -.
DR DNASU; 22948; -.
DR Ensembl; ENST00000280326; ENSP00000280326; ENSG00000150753.
DR GeneID; 22948; -.
DR KEGG; hsa:22948; -.
DR UCSC; uc003jeq.3; human.
DR CTD; 22948; -.
DR GeneCards; GC05P010236; -.
DR H-InvDB; HIX0120997; -.
DR HGNC; HGNC:1618; CCT5.
DR HPA; CAB006271; -.
DR HPA; HPA002238; -.
DR HPA; HPA005958; -.
DR MIM; 256840; phenotype.
DR MIM; 610150; gene.
DR neXtProt; NX_P48643; -.
DR Orphanet; 139578; Hereditary sensory and autonomic neuropathy with spastic paraplegia.
DR PharmGKB; PA26182; -.
DR eggNOG; COG0459; -.
DR HOGENOM; HOG000226735; -.
DR HOVERGEN; HBG106507; -.
DR InParanoid; P48643; -.
DR KO; K09497; -.
DR OMA; MRAFASA; -.
DR OrthoDB; EOG722J8B; -.
DR PhylomeDB; P48643; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; CCT5; human.
DR GeneWiki; CCT5_(gene); -.
DR GenomeRNAi; 22948; -.
DR NextBio; 43711; -.
DR PRO; PR:P48643; -.
DR ArrayExpress; P48643; -.
DR Bgee; P48643; -.
DR CleanEx; HS_CCT5; -.
DR Genevestigator; P48643; -.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0002199; C:zona pellucida receptor complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR Gene3D; 1.10.560.10; -; 2.
DR Gene3D; 3.30.260.10; -; 2.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012718; Chap_CCT_epsi.
DR InterPro; IPR017998; Chaperone_TCP-1.
DR InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR InterPro; IPR002423; Cpn60/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom.
DR InterPro; IPR027413; GROEL-like_equatorial.
DR InterPro; IPR027410; TCP-1-like_intermed.
DR PANTHER; PTHR11353; PTHR11353; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF48592; SSF48592; 2.
DR SUPFAM; SSF52029; SSF52029; 1.
DR TIGRFAMs; TIGR02343; chap_CCT_epsi; 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 Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Disease mutation; Neuropathy;
KW Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 541 T-complex protein 1 subunit epsilon.
FT /FTId=PRO_0000128346.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 26 26 Phosphoserine.
FT VARIANT 146 146 E -> V (in dbSNP:rs11557652).
FT /FTId=VAR_052267.
FT VARIANT 147 147 H -> R (in HSNSP).
FT /FTId=VAR_030658.
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
//
MIM
256840
*RECORD*
*FIELD* NO
256840
*FIELD* TI
#256840 NEUROPATHY, HEREDITARY SENSORY, WITH SPASTIC PARAPLEGIA, AUTOSOMAL
RECESSIVE
read more*FIELD* TX
A number sign (#) is used with this entry because autosomal recessive
sensory neuropathy with spastic paraplegia is caused by mutations in the
CCT5 gene (610150).
CLINICAL FEATURES
Cavanagh et al. (1979) described a seemingly unique form of sensory
neuropathy with mutilating ulcerations of the hands and feet similar to
that described in entry 162400 except for the additional feature of
spastic paraplegia. Three of the patients, 2 of whom were thought to be
half sibs (different paternity), developed paraplegia in the first 2
years of life; this was associated at an early stage with the clinical
features of a peripheral neuropathy. In contrast, the other 2 patients,
a brother and sister, demonstrated paraplegia and neuropathy much later,
although it was difficult to date the onset precisely.
Thomas et al. (1994) described progressive sensory neuropathy in
association with spastic paraplegia and a mutilating acropathy of the
lower limbs in 5 patients, including 2 pairs of sibs who were the
offspring of normal consanguineous parents. Nerve biopsy in 3 of the
patients showed an axonopathy with loss of myelinated nerve fibers of
all diameters as well as loss of unmyelinated axons.
Bouhouche et al. (2006) reported a consanguineous Moroccan family in
which 4 sibs had a severe mutilating sensory neuropathy with spastic
paraplegia. Age at onset ranged from 1 to 5 years. The clinical features
included lower limb spasticity, hyperreflexia with clonus, positive
Babinski sign, and subtle distal amyotrophy with normal motor function.
Affected members had distal sensory loss for all modalities in the upper
and lower limbs, particularly in the feet. Two patients had
'deformities' of the hands and feet, and most had deep perforating
ulcers of the extremities. The oldest patient, aged 34, had scars of
healed ulcers in the hands and a history of osteomyelitis of the feet
leading to amputation of both legs up to his thighs. Although the
progression of spasticity was slow, the sensory neuropathy was rapidly
progressive and severe. Electrophysiologic studies showed normal or
mildly decreased motor nerve conduction velocities consistent with a
sensory axonal neuropathy. MRI of 2 patients showed severe atrophy of
the spinal cord, and laboratory investigations of 2 patients showed
decreased serum apolipoprotein B (APOB; 107730), total cholesterol, and
triglycerides.
MAPPING
By genomewide analysis of a consanguineous Moroccan family with sensory
neuropathy and spastic paraplegia, Bouhouche et al. (2006) identified a
candidate disease locus within a 25-cM region on chromosome
5p15.31-p14.1 between markers D5S2054 and D5S648 (maximum lod score of
3.92).
MOLECULAR GENETICS
In 4 affected members of a Moroccan family reported by Bouhouche et al.
(2006), Bouhouche et al. (2006) identified a homozygous mutation in the
CCT5 gene (610150.0001).
*FIELD* RF
1. Bouhouche, A.; Benomar, A.; Bouslam, N.; Chkili, T.; Yahyaoui,
M.: Mutation in the epsilon subunit of the cytosolic chaperonin-containing
t-complex peptide-1 (Cct5) gene causes autosomal recessive mutilating
sensory neuropathy with spastic paraplegia. J. Med. Genet. 43: 441-443,
2006.
2. Bouhouche, A.; Benomar, A.; Bouslam, N.; Ouazzani, R.; Chkili,
T.; Yahyaoui, M.: Autosomal recessive mutilating sensory neuropathy
with spastic paraplegia maps to chromosome 5p15.31-14.1. Europ. J.
Hum. Genet. 14: 249-252, 2006.
3. Cavanagh, N. P. C.; Eames, R. A.; Galvin, R. J.; Brett, E. M.;
Kelly, R. E.: Hereditary sensory neuropathy with spastic paraplegia. Brain 102:
79-94, 1979.
4. Thomas, P. K.; Misra, V. P.; King, R. H. M.; Muddle, J. R.; Wroe,
S.; Bhatia, K. P.; Anderson, M.; Cabello, A.; Vilchez, J.; Wadia,
N. H.: Autosomal recessive hereditary sensory neuropathy with spastic
paraplegia. Brain 117: 651-659, 1994.
*FIELD* CS
INHERITANCE:
Autosomal recessive
SKELETAL:
[Limbs];
Distal ulceration and osteomyelitis leading to autoamputation;
[Hands];
Hand deformities;
Distal ulceration and osteomyelitis leading to autoamputation;
[Feet];
Foot deformities;
Distal ulceration and osteomyelitis leading to autoamputation
NEUROLOGIC:
[Peripheral nervous system];
Distal limb muscle atrophy due to peripheral neuropathy, mild;
Lower limb spasticity;
Spastic gait;
Spastic paraplegia;
Pyramidal signs;
Hyperreflexia;
Clonus;
Babinski sign;
Distal sensory loss of all modalities;
Normal or mildly decreased motor nerve conduction velocity (NCV);
Axonal neuropathy;
MRI shows atrophy of the spinal cord
LABORATORY ABNORMALITIES:
Decreased plasma apolipoprotein B (APOB, 107730);
Decreased plasma triglycerides;
Decreased plasma total cholesterol
MISCELLANEOUS:
Onset in early childhood (infancy to 5 years);
Spasticity is slowly progressive;
Sensory loss is rapidly progressive and severe
MOLECULAR BASIS:
Caused by mutation in the chaperonin-containing t-complex peptide-1
subunit 5 gene (CCT5, 610150.0001)
*FIELD* CN
Cassandra L. Kniffin - updated: 6/12/2006
Cassandra L. Kniffin - revised: 2/10/2006
*FIELD* CD
John F. Jackson: 6/15/1995
*FIELD* ED
joanna: 10/26/2006
ckniffin: 6/12/2006
ckniffin: 2/10/2006
*FIELD* CN
Cassandra L. Kniffin - updated: 6/12/2006
Cassandra L. Kniffin - updated: 2/10/2006
*FIELD* CD
Victor A. McKusick: 9/23/1987
*FIELD* ED
wwang: 06/16/2006
ckniffin: 6/12/2006
wwang: 2/24/2006
ckniffin: 2/10/2006
mark: 3/28/1995
mimadm: 3/11/1994
supermim: 3/17/1992
supermim: 3/20/1990
ddp: 10/27/1989
marie: 3/25/1988
*RECORD*
*FIELD* NO
256840
*FIELD* TI
#256840 NEUROPATHY, HEREDITARY SENSORY, WITH SPASTIC PARAPLEGIA, AUTOSOMAL
RECESSIVE
read more*FIELD* TX
A number sign (#) is used with this entry because autosomal recessive
sensory neuropathy with spastic paraplegia is caused by mutations in the
CCT5 gene (610150).
CLINICAL FEATURES
Cavanagh et al. (1979) described a seemingly unique form of sensory
neuropathy with mutilating ulcerations of the hands and feet similar to
that described in entry 162400 except for the additional feature of
spastic paraplegia. Three of the patients, 2 of whom were thought to be
half sibs (different paternity), developed paraplegia in the first 2
years of life; this was associated at an early stage with the clinical
features of a peripheral neuropathy. In contrast, the other 2 patients,
a brother and sister, demonstrated paraplegia and neuropathy much later,
although it was difficult to date the onset precisely.
Thomas et al. (1994) described progressive sensory neuropathy in
association with spastic paraplegia and a mutilating acropathy of the
lower limbs in 5 patients, including 2 pairs of sibs who were the
offspring of normal consanguineous parents. Nerve biopsy in 3 of the
patients showed an axonopathy with loss of myelinated nerve fibers of
all diameters as well as loss of unmyelinated axons.
Bouhouche et al. (2006) reported a consanguineous Moroccan family in
which 4 sibs had a severe mutilating sensory neuropathy with spastic
paraplegia. Age at onset ranged from 1 to 5 years. The clinical features
included lower limb spasticity, hyperreflexia with clonus, positive
Babinski sign, and subtle distal amyotrophy with normal motor function.
Affected members had distal sensory loss for all modalities in the upper
and lower limbs, particularly in the feet. Two patients had
'deformities' of the hands and feet, and most had deep perforating
ulcers of the extremities. The oldest patient, aged 34, had scars of
healed ulcers in the hands and a history of osteomyelitis of the feet
leading to amputation of both legs up to his thighs. Although the
progression of spasticity was slow, the sensory neuropathy was rapidly
progressive and severe. Electrophysiologic studies showed normal or
mildly decreased motor nerve conduction velocities consistent with a
sensory axonal neuropathy. MRI of 2 patients showed severe atrophy of
the spinal cord, and laboratory investigations of 2 patients showed
decreased serum apolipoprotein B (APOB; 107730), total cholesterol, and
triglycerides.
MAPPING
By genomewide analysis of a consanguineous Moroccan family with sensory
neuropathy and spastic paraplegia, Bouhouche et al. (2006) identified a
candidate disease locus within a 25-cM region on chromosome
5p15.31-p14.1 between markers D5S2054 and D5S648 (maximum lod score of
3.92).
MOLECULAR GENETICS
In 4 affected members of a Moroccan family reported by Bouhouche et al.
(2006), Bouhouche et al. (2006) identified a homozygous mutation in the
CCT5 gene (610150.0001).
*FIELD* RF
1. Bouhouche, A.; Benomar, A.; Bouslam, N.; Chkili, T.; Yahyaoui,
M.: Mutation in the epsilon subunit of the cytosolic chaperonin-containing
t-complex peptide-1 (Cct5) gene causes autosomal recessive mutilating
sensory neuropathy with spastic paraplegia. J. Med. Genet. 43: 441-443,
2006.
2. Bouhouche, A.; Benomar, A.; Bouslam, N.; Ouazzani, R.; Chkili,
T.; Yahyaoui, M.: Autosomal recessive mutilating sensory neuropathy
with spastic paraplegia maps to chromosome 5p15.31-14.1. Europ. J.
Hum. Genet. 14: 249-252, 2006.
3. Cavanagh, N. P. C.; Eames, R. A.; Galvin, R. J.; Brett, E. M.;
Kelly, R. E.: Hereditary sensory neuropathy with spastic paraplegia. Brain 102:
79-94, 1979.
4. Thomas, P. K.; Misra, V. P.; King, R. H. M.; Muddle, J. R.; Wroe,
S.; Bhatia, K. P.; Anderson, M.; Cabello, A.; Vilchez, J.; Wadia,
N. H.: Autosomal recessive hereditary sensory neuropathy with spastic
paraplegia. Brain 117: 651-659, 1994.
*FIELD* CS
INHERITANCE:
Autosomal recessive
SKELETAL:
[Limbs];
Distal ulceration and osteomyelitis leading to autoamputation;
[Hands];
Hand deformities;
Distal ulceration and osteomyelitis leading to autoamputation;
[Feet];
Foot deformities;
Distal ulceration and osteomyelitis leading to autoamputation
NEUROLOGIC:
[Peripheral nervous system];
Distal limb muscle atrophy due to peripheral neuropathy, mild;
Lower limb spasticity;
Spastic gait;
Spastic paraplegia;
Pyramidal signs;
Hyperreflexia;
Clonus;
Babinski sign;
Distal sensory loss of all modalities;
Normal or mildly decreased motor nerve conduction velocity (NCV);
Axonal neuropathy;
MRI shows atrophy of the spinal cord
LABORATORY ABNORMALITIES:
Decreased plasma apolipoprotein B (APOB, 107730);
Decreased plasma triglycerides;
Decreased plasma total cholesterol
MISCELLANEOUS:
Onset in early childhood (infancy to 5 years);
Spasticity is slowly progressive;
Sensory loss is rapidly progressive and severe
MOLECULAR BASIS:
Caused by mutation in the chaperonin-containing t-complex peptide-1
subunit 5 gene (CCT5, 610150.0001)
*FIELD* CN
Cassandra L. Kniffin - updated: 6/12/2006
Cassandra L. Kniffin - revised: 2/10/2006
*FIELD* CD
John F. Jackson: 6/15/1995
*FIELD* ED
joanna: 10/26/2006
ckniffin: 6/12/2006
ckniffin: 2/10/2006
*FIELD* CN
Cassandra L. Kniffin - updated: 6/12/2006
Cassandra L. Kniffin - updated: 2/10/2006
*FIELD* CD
Victor A. McKusick: 9/23/1987
*FIELD* ED
wwang: 06/16/2006
ckniffin: 6/12/2006
wwang: 2/24/2006
ckniffin: 2/10/2006
mark: 3/28/1995
mimadm: 3/11/1994
supermim: 3/17/1992
supermim: 3/20/1990
ddp: 10/27/1989
marie: 3/25/1988
MIM
610150
*RECORD*
*FIELD* NO
610150
*FIELD* TI
*610150 CHAPERONIN CONTAINING T-COMPLEX POLYPEPTIDE 1, SUBUNIT 5; CCT5
;;CHAPERONIN CONTAINING TCP1, SUBUNIT 5;;
read moreCCT-EPSILON; CCTE;;
KIAA0098
*FIELD* TX
DESCRIPTION
CCT5 is a subunit of the 950-kD chaperonin containing TCP1 (186980)
complex (CCT), which is involved in proper folding of cytoskeletal
proteins. The 8 CCT subunits are arranged into 2 stacked multimeric
rings, with a central cavity on each side of the molecule (Liou and
Willison, 1997).
CLONING
Kubota et al. (1994) cloned several subunits of mouse CCT, including
Cct5.
By sequencing clones obtained from a size-fractionated human myeloid
leukemia cell line cDNA library, Nagase et al. (1995) cloned CCT5, which
they designated KIAA0098. The deduced 546-amino acid protein shares
95.8% amino acid identity with mouse Cct5. Northern blot analysis
detected highest expression in colon, with intermediate or low
expression in all other tissues and cell lines examined.
GENE FUNCTION
Liou and Willison (1997) purified intact CCT and CCT microcomplexes from
mouse testis and human HEK293 cells. Western blot analysis of sucrose
gradient fractions detected CCT-epsilon only as a component of complexes
with molecular masses above 120 kD; it was not detected as a monomer.
CCT-epsilon appeared to associate with CCT-alpha (TCP1) and CCT-zeta
(CCT6A; 104613).
Llorca et al. (2001) identified the domains of actin (see 102610) and
tubulin (see 191130) that bound various CCT subunits, including CCT5.
GENE STRUCTURE
The CCT5 gene contains 11 exons (Bouhouche et al., 2006).
MAPPING
By PCR of human-rodent hybrid cell lines, Nagase et al. (1995)
determined that the CCT5 gene maps to chromosome 5 or 6. The
International Radiation Hybrid Mapping Consortium mapped the CCT5 gene
to chromosome 5 (TMAP RH25325).
MOLECULAR GENETICS
In 4 affected members of a Moroccan family with autosomal recessive
mutilating sensory neuropathy with spastic paraplegia (256840) linked to
5p15-p14, Bouhouche et al. (2006) identified a homozygous mutation in
the CCT5 gene (610150.0001).
*FIELD* AV
.0001
NEUROPATHY, HEREDITARY SENSORY, WITH SPASTIC PARAPLEGIA, AUTOSOMAL
RECESSIVE
CCT5, HIS147ARG
In 4 affected members of a Moroccan family with autosomal recessive
mutilating sensory neuropathy with spastic paraplegia (256840),
Bouhouche et al. (2006) identified a homozygous 492A-G transition in
exon 4 of the CCT5 gene, resulting in a his147-to-arg (H147R)
substitution in the equatorial domain-1 region of the protein. The
mutation was not identified in 384 ethnically matched control
chromosomes.
*FIELD* RF
1. Bouhouche, A.; Benomar, A.; Bouslam, N.; Chkili, T.; Yahyaoui,
M.: Mutation in the epsilon subunit of the cytosolic chaperonin-containing
t-complex peptide-1 (Cct5) gene causes autosomal recessive mutilating
sensory neuropathy with spastic paraplegia. J. Med. Genet. 43: 441-443,
2006.
2. Kubota, H.; Hynes, G.; Carne, A.; Ashworth, A.; Willison, K.:
Identification of six Tcp-1-related genes encoding divergent subunits
of the TCP-1-containing chaperonin. Curr. Biol. 4: 89-99, 1994.
3. Liou, A. K. F.; Willison, K. R.: Elucidation of the subunit orientation
in CCT (chaperonin containing TCP1) from the subunit composition of
CCT micro-complexes. EMBO J. 16: 4311-4316, 1997.
4. Llorca, O.; Martin-Benito, J.; Gomez-Puertas, P.; Ritco-Vonsovici,
M.; Willison, K. R.; Carrascosa, J. L.; Valpuesta, J. M.: Analysis
of the interaction between the eukaryotic chaperonin CCT and its substrates
actin and tubulin. J. Struct. Biol. 135: 205-218, 2001.
5. Nagase, T; Miyajima, N; Tanaka, A.; Sazuka, T.; Seki, N.; Sato,
S.; Tabata, S.; Ishikawa, K.; Kawarabayashi, Y.; Kotani, H.; Nomura,
N.: Prediction of the coding sequences of unidentified human genes.
III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced
by analysis of cDNA clones from human cell line KG-1. DNA Res. 2:
37-43, 1995.
*FIELD* CN
Cassandra L. Kniffin - updated: 6/12/2006
*FIELD* CD
Patricia A. Hartz: 5/30/2006
*FIELD* ED
terry: 06/04/2009
wwang: 6/16/2006
ckniffin: 6/12/2006
mgross: 6/2/2006
mgross: 5/30/2006
*RECORD*
*FIELD* NO
610150
*FIELD* TI
*610150 CHAPERONIN CONTAINING T-COMPLEX POLYPEPTIDE 1, SUBUNIT 5; CCT5
;;CHAPERONIN CONTAINING TCP1, SUBUNIT 5;;
read moreCCT-EPSILON; CCTE;;
KIAA0098
*FIELD* TX
DESCRIPTION
CCT5 is a subunit of the 950-kD chaperonin containing TCP1 (186980)
complex (CCT), which is involved in proper folding of cytoskeletal
proteins. The 8 CCT subunits are arranged into 2 stacked multimeric
rings, with a central cavity on each side of the molecule (Liou and
Willison, 1997).
CLONING
Kubota et al. (1994) cloned several subunits of mouse CCT, including
Cct5.
By sequencing clones obtained from a size-fractionated human myeloid
leukemia cell line cDNA library, Nagase et al. (1995) cloned CCT5, which
they designated KIAA0098. The deduced 546-amino acid protein shares
95.8% amino acid identity with mouse Cct5. Northern blot analysis
detected highest expression in colon, with intermediate or low
expression in all other tissues and cell lines examined.
GENE FUNCTION
Liou and Willison (1997) purified intact CCT and CCT microcomplexes from
mouse testis and human HEK293 cells. Western blot analysis of sucrose
gradient fractions detected CCT-epsilon only as a component of complexes
with molecular masses above 120 kD; it was not detected as a monomer.
CCT-epsilon appeared to associate with CCT-alpha (TCP1) and CCT-zeta
(CCT6A; 104613).
Llorca et al. (2001) identified the domains of actin (see 102610) and
tubulin (see 191130) that bound various CCT subunits, including CCT5.
GENE STRUCTURE
The CCT5 gene contains 11 exons (Bouhouche et al., 2006).
MAPPING
By PCR of human-rodent hybrid cell lines, Nagase et al. (1995)
determined that the CCT5 gene maps to chromosome 5 or 6. The
International Radiation Hybrid Mapping Consortium mapped the CCT5 gene
to chromosome 5 (TMAP RH25325).
MOLECULAR GENETICS
In 4 affected members of a Moroccan family with autosomal recessive
mutilating sensory neuropathy with spastic paraplegia (256840) linked to
5p15-p14, Bouhouche et al. (2006) identified a homozygous mutation in
the CCT5 gene (610150.0001).
*FIELD* AV
.0001
NEUROPATHY, HEREDITARY SENSORY, WITH SPASTIC PARAPLEGIA, AUTOSOMAL
RECESSIVE
CCT5, HIS147ARG
In 4 affected members of a Moroccan family with autosomal recessive
mutilating sensory neuropathy with spastic paraplegia (256840),
Bouhouche et al. (2006) identified a homozygous 492A-G transition in
exon 4 of the CCT5 gene, resulting in a his147-to-arg (H147R)
substitution in the equatorial domain-1 region of the protein. The
mutation was not identified in 384 ethnically matched control
chromosomes.
*FIELD* RF
1. Bouhouche, A.; Benomar, A.; Bouslam, N.; Chkili, T.; Yahyaoui,
M.: Mutation in the epsilon subunit of the cytosolic chaperonin-containing
t-complex peptide-1 (Cct5) gene causes autosomal recessive mutilating
sensory neuropathy with spastic paraplegia. J. Med. Genet. 43: 441-443,
2006.
2. Kubota, H.; Hynes, G.; Carne, A.; Ashworth, A.; Willison, K.:
Identification of six Tcp-1-related genes encoding divergent subunits
of the TCP-1-containing chaperonin. Curr. Biol. 4: 89-99, 1994.
3. Liou, A. K. F.; Willison, K. R.: Elucidation of the subunit orientation
in CCT (chaperonin containing TCP1) from the subunit composition of
CCT micro-complexes. EMBO J. 16: 4311-4316, 1997.
4. Llorca, O.; Martin-Benito, J.; Gomez-Puertas, P.; Ritco-Vonsovici,
M.; Willison, K. R.; Carrascosa, J. L.; Valpuesta, J. M.: Analysis
of the interaction between the eukaryotic chaperonin CCT and its substrates
actin and tubulin. J. Struct. Biol. 135: 205-218, 2001.
5. Nagase, T; Miyajima, N; Tanaka, A.; Sazuka, T.; Seki, N.; Sato,
S.; Tabata, S.; Ishikawa, K.; Kawarabayashi, Y.; Kotani, H.; Nomura,
N.: Prediction of the coding sequences of unidentified human genes.
III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced
by analysis of cDNA clones from human cell line KG-1. DNA Res. 2:
37-43, 1995.
*FIELD* CN
Cassandra L. Kniffin - updated: 6/12/2006
*FIELD* CD
Patricia A. Hartz: 5/30/2006
*FIELD* ED
terry: 06/04/2009
wwang: 6/16/2006
ckniffin: 6/12/2006
mgross: 6/2/2006
mgross: 5/30/2006