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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}.
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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
 
 
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