CH60_DICDI
ID CH60_DICDI Reviewed; 556 AA.
AC Q54J97; Q95025;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=60 kDa heat shock protein, mitochondrial;
DE AltName: Full=60 kDa chaperonin;
DE AltName: Full=Chaperonin 60;
DE Short=CPN60;
DE AltName: Full=Heat shock protein 60;
DE Short=HSP-60;
DE Short=Hsp60;
DE Flags: Precursor;
GN Name=hspA; ORFNames=DDB_G0288181;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AX2;
RA Kotsifas M., DeLozanne A., Fisher P.R.;
RT "The chaperonin 60 gene of Dictyostelium discoideum.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12952082; DOI=10.1023/a:1024444215766;
RA Kotsifas M., Barth C., de Lozanne A., Lay S.T., Fisher P.R.;
RT "Chaperonin 60 and mitochondrial disease in Dictyostelium.";
RL J. Muscle Res. Cell Motil. 23:839-852(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Implicated in mitochondrial protein import and macromolecular
CC assembly. May facilitate the correct folding of imported proteins. May
CC also prevent misfolding and promote the refolding and proper assembly
CC of unfolded polypeptides generated under stress conditions in the
CC mitochondrial matrix (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- INDUCTION: By heat shock. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) 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; U72247; AAB17277.1; -; mRNA.
DR EMBL; AF359268; AAK49534.1; -; Genomic_DNA.
DR EMBL; AAFI02000109; EAL63321.1; -; Genomic_DNA.
DR RefSeq; XP_636839.1; XM_631747.1.
DR AlphaFoldDB; Q54J97; -.
DR SMR; Q54J97; -.
DR STRING; 44689.DDB0219929; -.
DR PaxDb; Q54J97; -.
DR PRIDE; Q54J97; -.
DR EnsemblProtists; EAL63321; EAL63321; DDB_G0288181.
DR GeneID; 8626508; -.
DR KEGG; ddi:DDB_G0288181; -.
DR dictyBase; DDB_G0288181; hspA.
DR eggNOG; KOG0356; Eukaryota.
DR HOGENOM; CLU_016503_3_0_1; -.
DR InParanoid; Q54J97; -.
DR OMA; TDTDKME; -.
DR PhylomeDB; Q54J97; -.
DR PRO; PR:Q54J97; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:dictyBase.
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:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0019954; P:asexual reproduction; IMP:dictyBase.
DR GO; GO:0042742; P:defense response to bacterium; IMP:dictyBase.
DR GO; GO:0007005; P:mitochondrion organization; IMP:dictyBase.
DR GO; GO:0046956; P:positive phototaxis; IMP:dictyBase.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IEP:dictyBase.
DR GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR CDD; cd03344; GroEL; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR HAMAP; MF_00600; CH60; 1.
DR InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR InterPro; IPR001844; Cpn60/GroEL.
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 Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00298; CHAPERONIN60.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR TIGRFAMs; TIGR02348; GroEL; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..556
FT /note="60 kDa heat shock protein, mitochondrial"
FT /id="PRO_0000316526"
FT CONFLICT 139
FT /note="F -> S (in Ref. 1; AAB17277 and 2; AAK49534)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="A -> G (in Ref. 1; AAB17277 and 2; AAK49534)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 556 AA; 59846 MW; D4B0DD4D0EC89845 CRC64;
MFRQIANKST KFGLRNYSTG KDIKFGAECR ALMLRGVEQL AAAVEVTLGP KGRNVILDQP
FGQPKITKDG VTVAKHIEFA DRHINLGAQL VKGVASSQND QSGDGTTTAT ILTRAIFAEG
CKAVAAGMNP MDLWRGINFA VEKVVGELKT ISRPISSTEE ISQVATISAN GDKVIGNLIA
NAMEKIGKEG VITVQDGKTL KDELEIIEGM KFDQGFISRY FINDAKEQKC EFDDPVILVV
DGKISNVQQL VPILELVHSK HKKLVIIADN IEGDALSALI FNKMRGLQVC AVKAPGFGDL
KRVNLQDIAV ISGAQVISEE LGVRLEDVDI TMLGSAKKIT IDSDSTIILD GAGDKAAIQE
RVELIRESLT RTTSDYDKTQ LETRLAKIGG GVAVIRVGGA SEVEVGEKKD RITDALNATK
AAVEEGIVPG GGTALLYSTL ALKKIKMDNF DQTIGVKIVR DALLIPCKTI ANNAGVEGSV
VIGRLLSKRD FEYGYNAQKG VYENMIQAGI IDPTKVVRTA LIDAASVASL MTTTEAMVVE
IKKDTPMPQM PPQMDY
