ID   Q3B7U6_RAT              Unreviewed;       561 AA.
AC   Q3B7U6;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 139.
DE   SubName: Full=Chaperonin containing TCP1 subunit 8 like 2 {ECO:0000313|Ensembl:ENSRNOP00000066908.1};
GN   Name=Cct8l2 {ECO:0000313|Ensembl:ENSRNOP00000066908.1,
GN   ECO:0000313|RGD:1561536};
GN   Synonyms=Cct8l1 {ECO:0000313|RGD:1561536}, LOC102553845
GN   {ECO:0000313|RGD:1561536};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000066908.1, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000066908.1, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000066908.1,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000066908.1}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000066908.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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. The TRiC complex mediates the folding of WRAP53/TCAB1,
CC       thereby regulating telomere maintenance. As part of the TRiC complex
CC       may play a role in the assembly of BBSome, a complex involved in
CC       ciliogenesis regulating transports vesicles to the cilia. The TRiC
CC       complex plays a role in the folding of actin and tubulin.
CC       {ECO:0000256|ARBA:ARBA00003895}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family.
CC       {ECO:0000256|ARBA:ARBA00008020, ECO:0000256|RuleBase:RU004187}.
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DR   RefSeq; NP_001032883.1; NM_001037794.1.
DR   AlphaFoldDB; Q3B7U6; -.
DR   SMR; Q3B7U6; -.
DR   STRING; 10116.ENSRNOP00000066908; -.
DR   PhosphoSitePlus; Q3B7U6; -.
DR   PaxDb; 10116-ENSRNOP00000066908; -.
DR   Ensembl; ENSRNOT00000074846.3; ENSRNOP00000066908.1; ENSRNOG00000047114.3.
DR   GeneID; 499967; -.
DR   KEGG; rno:499967; -.
DR   AGR; RGD:1561536; -.
DR   CTD; 150160; -.
DR   RGD; 1561536; Cct8l2.
DR   eggNOG; KOG0362; Eukaryota.
DR   GeneTree; ENSGT00940000163221; -.
DR   HOGENOM; CLU_008891_4_2_1; -.
DR   OMA; YSVMNTH; -.
DR   OrthoDB; 4629119at2759; -.
DR   TreeFam; TF105699; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000047114; Expressed in testis and 2 other cell types or tissues.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IBA:GO_Central.
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:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
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; 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   PANTHER; PTHR11353; CHAPERONIN; 1.
DR   PANTHER; PTHR11353:SF100; T-COMPLEX PROTEIN 1 SUBUNIT THETA-LIKE 1-RELATED; 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.
PE   1: Evidence at protein level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004187};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004187};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004187};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
SQ   SEQUENCE   561 AA;  60630 MW;  6C53333EB1A25F26 CRC64;
     MAVSSSQVTQ TKVQSDLELP QRLKLGLEKN PESQGEEPLC ILRATAAAQT LASIIRSCYG
     PYGLQKFLVS AQGETVCTGH AAAILKALEL EHPAARFVQE LAQTQAENTG DGTAFVVLLT
     EALLEQAQYL LWAGLTPAQL REAFVTATAE VLTALPSLAI CSLGPLEDPS WALYSVMSTH
     TLSNAEYLTK LVAQACWISR EPNGSFKPES IVVCILQGGI LTDSRIIPGI AICGKLCGRK
     TEVLNDARVA LFNCPFGPSN PFAPATLRLS SPEELIRFRK QTEQVEMEIA ELAMMGINVA
     VVLGEVNERS VDQADYCGVM VIQVKSRKEI VYLSDKLGVP LLNRILPPLE PGKCHKVYRM
     EFGESALIMF EWEREIAPFL SVVLRGPTIQ GLRGAEQAVY YGIDAFSQLC QDPRLLPGAG
     ATEMALARML VDKGSRLDGP NGLAFQAFAQ ALSSLPKTLA ENAGLAAQSV LAEMSGYHQA
     GNFVIGVGTD GLVNVAQEGI WDILRTKAQG LQAVTGLVQQ LVTVDQIIVA RKTPRYRLIP
     QSAQNANTSS PLRAKFFGKY E
//