ID   HS7C3_DICDI             Reviewed;         630 AA.
AC   Q54BE0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Heat shock cognate 70 kDa protein 3;
DE            Short=HSC70-3;
GN   ORFNames=DDB_G0293674;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
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: May function in protein folding and assembly, and disassembly
CC       of protein complexes. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 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; AAFI02000218; EAL60649.1; -; Genomic_DNA.
DR   RefSeq; XP_629089.1; XM_629087.1.
DR   AlphaFoldDB; Q54BE0; -.
DR   SMR; Q54BE0; -.
DR   STRING; 44689.DDB0192086; -.
DR   PaxDb; Q54BE0; -.
DR   EnsemblProtists; EAL60649; EAL60649; DDB_G0293674.
DR   GeneID; 8629382; -.
DR   KEGG; ddi:DDB_G0293674; -.
DR   dictyBase; DDB_G0293674; hspH2.
DR   eggNOG; KOG0101; Eukaryota.
DR   HOGENOM; CLU_005965_3_0_1; -.
DR   InParanoid; Q54BE0; -.
DR   OMA; VNEAESY; -.
DR   PhylomeDB; Q54BE0; -.
DR   Reactome; R-DDI-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR   PRO; PR:Q54BE0; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005811; C:lipid droplet; HDA:dictyBase.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR   GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR   GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..630
FT                   /note="Heat shock cognate 70 kDa protein 3"
FT                   /id="PRO_0000327972"
FT   REGION          611..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   630 AA;  69947 MW;  90DDDF2A88E20F05 CRC64;
     MTSIGIDLGT TYSCVGVWLN DRVEIIANDQ GNRTTPSYVA FNDTERLIGD AAKNQVAMNP
     INTVFDAKRL IGRKFSDSVV QSDMKHWPFK VITNKNDDKP LIQVDFKGET KTFSPEEISS
     MVLSKMKETA ESYLGKPVNN AVITVPAYFN DGQRQATKDA GTISKLNVQR IINEPSAAAI
     AYGLDKKGSK SGEIKVLIFD LGGGTFDVSL LSIDDGVFEV LATAGDTHLG GEDFDNRLVN
     HFVDEFKRKH KKDIMGNQRA LRRLRTACER AKRTLSSSSQ ASVEIDSLYD GIDFYTSITR
     ARFEELCSDL FNNCIEPVEK VLKDCKLDKK SIDEIVLVGG STRIPKVQQL IQNLFNGKEL
     NKSINPDEAV AYGAAVQAAI LSGDKSSRIS ELIFIDVAPL SLGIETVGGV MTNIVPRNTI
     IPCKKTQTFS THTDNQSGVL IQVYEGERTM TKDNNLLGKF ELTGIPPAPR GTPQIEVSFD
     VDSNGILNVT AEDKTTKKVE KITITNDKGR LSLKDITKMV EDAEKFKEQD QQQKERIESK
     NNLENYIFSV KNSINDQKII SKLSKSDKNI IESETESTLK WLESNQSAEK DEFNQKISDL
     ESIVNPILSK FYQGNNNPKP TTTTFNQDLD