ID   TCPE2_AVESA             Reviewed;         535 AA.
AC   P54411;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=T-complex protein 1 subunit epsilon;
DE            Short=TCP-1-epsilon;
DE   AltName: Full=CCT-epsilon;
DE   AltName: Full=TCP-K36;
OS   Avena sativa (Oat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Poodae; Poeae; Aveninae; Avena.
OX   NCBI_TaxID=4498;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Pewi; TISSUE=Coleoptile, and Mesocotyl;
RX   PubMed=7903257; DOI=10.1016/0014-5793(93)80827-h;
RA   Ehmann B., Krenz M., Mummert E., Schaefer E.;
RT   "Two Tcp-1-related but highly divergent gene families exist in oat encoding
RT   proteins of assumed chaperone function.";
RL   FEBS Lett. 336:313-316(1993).
CC   -!- FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP
CC       hydrolysis. Known to play a role, in vitro, in the folding of actin and
CC       tubulin.
CC   -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that forms
CC       two stacked rings, 12 to 16 nm in diameter.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; X75778; CAA53397.1; -; mRNA.
DR   PIR; S40462; S40462.
DR   AlphaFoldDB; P54411; -.
DR   SMR; P54411; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR   CDD; cd03339; TCP1_epsilon; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
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/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.
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   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding.
FT   CHAIN           1..535
FT                   /note="T-complex protein 1 subunit epsilon"
FT                   /id="PRO_0000128352"
SQ   SEQUENCE   535 AA;  59034 MW;  02761226F5F17B81 CRC64;
     MALDFDEYWR PFIILREQEK KSRLQGLDAQ KANIAAGKSV ARILRTSLGP KGMDKMLQSP
     DGDVTITNDG ATILELMDVD NQIAKLMVEL SRSQDYDIGD GTTGVVVMAG SLLEQAEKLL
     ERGIHPIRVA EGYEMASRIA VDHLESISTK YEFSATDIEP LVQTCMTTLS SKIVSRCKRA
     LAEIAVKAVL AVADLERKDV NLDLIKVEGK VGGKLEDTEL VQGIIVDKDM SHPQMPKRIE
     DAHIAILTCP FEPPKPKTKH KVDIDTVEKF QTLRGQEQKY FDEMVQKCKD VGATLVICQW
     GFDDEANHLL MQRELPAVRW VGGVELELIA IATGGRIVPR FQELSTEKLG KAGLVREKSF
     GTTKDRMLYI EKCANSKAVT IFIRGGNKMM IEETKRSIHD ALCVARNLII NNSIVYGGGS
     AEISCSIAVE AAADRHPGVE QYAIRAFADA LDAIPLALAE NSGLPPIDTL TVVKSQHVKE
     NNSRCGIDCN DVGTNDMKEQ NVFETLIGKQ QQILLATQVV KMILKIDDVI TPSEY