TCPQM_HUMAN
ID TCPQM_HUMAN Reviewed; 557 AA.
AC Q96SF2; A4QPH3; Q9UJS3;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=T-complex protein 1 subunit theta-like 2;
GN Name=CCT8L2; Synonyms=CESK1;
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 [GENOMIC DNA], AND VARIANT ARG-320.
RX PubMed=10585773; DOI=10.1006/geno.1999.5975;
RA Riazi M.A., Brinkman-Mills P., Johnson A., Naylor S.L., Minoshima S.,
RA Shimizu N., Baldini A., McDermid H.E.;
RT "Identification of a putative regulatory subunit of a calcium-activated
RT potassium channel in the dup(3q) syndrome region and a related sequence on
RT 22q11.2.";
RL Genomics 62:90-94(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-320.
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-320.
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-320.
RC TISSUE=Brain;
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 IDENTIFICATION.
RX PubMed=20193073; DOI=10.1186/1471-2148-10-64;
RA Mukherjee K., Conway de Macario E., Macario A.J., Brocchieri L.;
RT "Chaperonin genes on the rise: new divergent classes and intense
RT duplication in human and other vertebrate genomes.";
RL BMC Evol. Biol. 10:64-64(2010).
CC -!- FUNCTION: Possible molecular chaperone; assists the folding of proteins
CC upon ATP hydrolysis. {ECO:0000250|UniProtKB:P40227}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P40227}.
CC -!- MISCELLANEOUS: Presence of two highly similar CCT8L genes (CCT8L1P and
CC CCT8L2) in the genomes of human and chimp and of a single copy in other
CC mammal genomes, including rhesus monkey, suggests that the duplication
CC of this gene occurred in the ape lineage (Hominoidea) after its
CC divergence from the old-world monkeys (Cercopithecidae).
CC {ECO:0000303|PubMed:20193073}.
CC -!- MISCELLANEOUS: Expression of CCT8L2 is confirmed by many ESTs mostly
CC identified from the testis. {ECO:0000305|PubMed:20193073}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI39843.2; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
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DR EMBL; AP000365; BAA84680.1; -; Genomic_DNA.
DR EMBL; AP003553; BAB43952.1; -; Genomic_DNA.
DR EMBL; CR456508; CAG30394.1; -; mRNA.
DR EMBL; AP000547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471193; EAW57714.1; -; Genomic_DNA.
DR EMBL; BC033797; AAH33797.1; -; mRNA.
DR EMBL; BC100811; AAI00812.1; -; mRNA.
DR EMBL; BC100812; AAI00813.1; -; mRNA.
DR EMBL; BC100813; AAI00814.1; -; mRNA.
DR EMBL; BC139842; AAI39843.2; ALT_SEQ; mRNA.
DR CCDS; CCDS13738.1; -.
DR RefSeq; NP_055221.1; NM_014406.4.
DR AlphaFoldDB; Q96SF2; -.
DR SMR; Q96SF2; -.
DR BioGRID; 127265; 190.
DR IntAct; Q96SF2; 1.
DR MINT; Q96SF2; -.
DR STRING; 9606.ENSP00000353048; -.
DR GlyGen; Q96SF2; 1 site, 1 O-linked glycan (1 site).
DR PhosphoSitePlus; Q96SF2; -.
DR BioMuta; CCT8L2; -.
DR DMDM; 313104021; -.
DR MassIVE; Q96SF2; -.
DR PaxDb; Q96SF2; -.
DR PeptideAtlas; Q96SF2; -.
DR PRIDE; Q96SF2; -.
DR ProteomicsDB; 78109; -.
DR Antibodypedia; 22616; 422 antibodies from 18 providers.
DR DNASU; 150160; -.
DR Ensembl; ENST00000359963.4; ENSP00000353048.3; ENSG00000198445.4.
DR GeneID; 150160; -.
DR KEGG; hsa:150160; -.
DR MANE-Select; ENST00000359963.4; ENSP00000353048.3; NM_014406.5; NP_055221.1.
DR UCSC; uc002zlp.2; human.
DR CTD; 150160; -.
DR GeneCards; CCT8L2; -.
DR HGNC; HGNC:15553; CCT8L2.
DR HPA; ENSG00000198445; Tissue enriched (testis).
DR neXtProt; NX_Q96SF2; -.
DR OpenTargets; ENSG00000198445; -.
DR PharmGKB; PA162382100; -.
DR VEuPathDB; HostDB:ENSG00000198445; -.
DR eggNOG; KOG0362; Eukaryota.
DR GeneTree; ENSGT00940000163221; -.
DR HOGENOM; CLU_008891_4_2_1; -.
DR InParanoid; Q96SF2; -.
DR OMA; YSVMNTH; -.
DR OrthoDB; 617040at2759; -.
DR PhylomeDB; Q96SF2; -.
DR TreeFam; TF105699; -.
DR PathwayCommons; Q96SF2; -.
DR SignaLink; Q96SF2; -.
DR BioGRID-ORCS; 150160; 20 hits in 1065 CRISPR screens.
DR GenomeRNAi; 150160; -.
DR Pharos; Q96SF2; Tdark.
DR PRO; PR:Q96SF2; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q96SF2; protein.
DR Bgee; ENSG00000198445; Expressed in right testis and 16 other tissues.
DR Genevisible; Q96SF2; HS.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IBA:GO_Central.
DR GO; GO:0005253; F:anion channel activity; TAS:ProtInc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0015269; F:calcium-activated potassium channel activity; TAS:ProtInc.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR017998; Chaperone_TCP-1.
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 PANTHER; PTHR11353; PTHR11353; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT CHAIN 1..557
FT /note="T-complex protein 1 subunit theta-like 2"
FT /id="PRO_0000347339"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 320
FT /note="W -> R (in dbSNP:rs2236639)"
FT /evidence="ECO:0000269|PubMed:10585773,
FT ECO:0000269|PubMed:15461802, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.4"
FT /id="VAR_046042"
SQ SEQUENCE 557 AA; 59388 MW; F7D105C7324D5A30 CRC64;
MDSTVPSALE LPQRLALNPR ESPRSPEEEE PHLLSSLAAV QTLASVIRPC YGPHGRQKFL
VTMKGETVCT GCATAILRAL ELEHPAAWLL REAGQTQAEN SGDGTAFVVL LTEALLEQAE
QLLKAGLPRP QLREAYATAT AEVLATLPSL AIQSLGPLED PSWALHSVMN THTLSPMDHL
TKLVAHACWA IKELDGSFKP ERVGVCALPG GTLEDSCLLP GLAISGKLCG QMATVLSGAR
VALFACPFGP AHPNAPATAR LSSPADLAQF SKGSDQLLEK QVGQLAAAGI NVAVVLGEVD
EETLTLADKY GIVVIQARSW MEIIYLSEVL DTPLLPRLLP PQRPGKCQRV YRQELGDGLA
VVFEWECTGT PALTVVLRGA TTQGLRSAEQ AVYHGIDAYF QLCQDPRLIP GAGATEMALA
KMLSDKGSRL EGPSGPAFLA FAWALKYLPK TLAENAGLAV SDVMAEMSGV HQGGNLLMGV
GTEGIINVAQ EGVWDTLIVK AQGFRAVAEV VLQLVTVDEI VVAKKSPTHQ EIWNPDSKKT
KKHPPPVETK KILGLNN
