CH10C_SPIOL
ID CH10C_SPIOL Reviewed; 255 AA.
AC Q02073;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=20 kDa chaperonin, chloroplastic;
DE AltName: Full=Chaperonin 10;
DE Short=Ch-CPN10;
DE Short=Cpn10;
DE AltName: Full=Protein Cpn21;
DE Flags: Precursor;
GN Name=CPN21; Synonyms=CHCPN10;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1356267; DOI=10.1073/pnas.89.18.8696;
RA Bertsch U., Soll J., Seetharam R., Viitanen P.V.;
RT "Identification, characterization, and DNA sequence of a functional
RT 'double' groES-like chaperonin from chloroplasts of higher plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8696-8700(1992).
CC -!- FUNCTION: Seems to function only as a co-chaperone, along with cpn60,
CC and in certain cases is essential for the discharge of biologically
CC active proteins from cpn60.
CC -!- SUBUNIT: Forms stable complexes with CPN60 in the presence of ATP.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the GroES chaperonin family. {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; M87646; AAB59307.1; -; mRNA.
DR PIR; A46176; A46176.
DR AlphaFoldDB; Q02073; -.
DR SMR; Q02073; -.
DR OrthoDB; 1368363at2759; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR GO; GO:1901671; P:positive regulation of superoxide dismutase activity; IEA:InterPro.
DR CDD; cd00320; cpn10; 2.
DR Gene3D; 2.30.33.40; -; 2.
DR HAMAP; MF_00580; CH10; 2.
DR InterPro; IPR020818; Chaperonin_GroES.
DR InterPro; IPR037124; Chaperonin_GroES_sf.
DR InterPro; IPR018369; Chaprnonin_Cpn10_CS.
DR InterPro; IPR017416; Cpn20.
DR InterPro; IPR011032; GroES-like_sf.
DR PANTHER; PTHR10772; PTHR10772; 1.
DR Pfam; PF00166; Cpn10; 2.
DR PIRSF; PIRSF038157; Chaperonin_21_chloroplast; 1.
DR PRINTS; PR00297; CHAPERONIN10.
DR SMART; SM00883; Cpn10; 2.
DR SUPFAM; SSF50129; SSF50129; 2.
DR PROSITE; PS00681; CHAPERONINS_CPN10; 2.
PE 2: Evidence at transcript level;
KW Chaperone; Chloroplast; Plastid; Repeat; Transit peptide.
FT TRANSIT 1..53
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 54..255
FT /note="20 kDa chaperonin, chloroplastic"
FT /id="PRO_0000005046"
FT REGION 54..156
FT /note="Cpn-10 domain 1"
FT REGION 157..255
FT /note="Cpn-10 domain 2"
SQ SEQUENCE 255 AA; 26956 MW; 9676E88785EC4512 CRC64;
MAATHLTSTS SLTINTLPSF EGLRSASGIS KINVSVAYPS FTSRSFRGLV VRAASITTSK
YTSVKPLGDR VLIKTKIVEE KTTSGIFLPT AAQKKPQSGE VVAIGSGKKV GDKKLPVAVK
TGAEVVYSKY TGTEIEVDGS SHLIVKEDDI IGILETDDVK DLKPLNDRLL IKVAEVENKT
SGGLLLAESS KEKPSFGTVV ATGPGVLDEE GNRIPLPVCS GNTVLYSKYA GNDFKGVDGS
DYMVLRVSDV MAVLS