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HS7C2_DICDI
ID   HS7C2_DICDI             Reviewed;         632 AA.
AC   Q557E0; O15766; Q869V7;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Heat shock cognate 70 kDa protein 2;
DE            Short=HSC70-2;
GN   Name=hspE-1; ORFNames=DDB_G0273249;
GN   and
GN   Name=hspE-2; ORFNames=DDB_G0273623;
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=AX3;
RA   Boves H., Mintert U., Dittrich W., Faix J., Gerisch G.;
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(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).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16512674; DOI=10.1021/pr050350q;
RA   Reinders Y., Schulz I., Graef R., Sickmann A.;
RT   "Identification of novel centrosomal proteins in Dictyostelium discoideum
RT   by comparative proteomic approaches.";
RL   J. Proteome Res. 5:589-598(2006).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=AX2;
RX   PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA   Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA   Soldati T.;
RT   "Proteomics fingerprinting of phagosome maturation and evidence for the
RT   role of a Galpha during uptake.";
RL   Mol. Cell. Proteomics 5:2228-2243(2006).
RN   [6]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=17259634; DOI=10.1099/mic.0.2006/000562-0;
RA   Serafimidis I., Bloomfield G., Skelton J., Ivens A., Kay R.R.;
RT   "A new environmentally resistant cell type from Dictyostelium.";
RL   Microbiology 153:619-630(2007).
CC   -!- FUNCTION: May function in protein folding and assembly, and disassembly
CC       of protein complexes. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome.
CC   -!- DEVELOPMENTAL STAGE: Up-regulated in aspidocytes, a resistant cell type
CC       induced from amoebae by a range of toxins including heavy metals and
CC       antibiotics. {ECO:0000269|PubMed:17259634}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC   -!- CAUTION: The gene for this protein is duplicated in strains AX3 and
CC       AX4. These strains contain a duplication of a segment of 750 kb of
CC       chromosome 2 compared to the corresponding sequence in strain AX2.
CC       {ECO:0000305}.
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DR   EMBL; AF025951; AAB81865.1; -; mRNA.
DR   EMBL; AAFI02000011; EAL70502.1; -; Genomic_DNA.
DR   EMBL; AAFI02000009; EAL70842.1; -; Genomic_DNA.
DR   PIR; T45471; T45471.
DR   RefSeq; XP_644428.1; XM_639336.1.
DR   RefSeq; XP_644822.1; XM_639730.1.
DR   AlphaFoldDB; Q557E0; -.
DR   SMR; Q557E0; -.
DR   IntAct; Q557E0; 1.
DR   STRING; 44689.DDB0185047; -.
DR   PaxDb; Q557E0; -.
DR   EnsemblProtists; EAL70502; EAL70502; DDB_G0273623.
DR   EnsemblProtists; EAL70842; EAL70842; DDB_G0273249.
DR   GeneID; 8618924; -.
DR   GeneID; 8619053; -.
DR   KEGG; ddi:DDB_G0273249; -.
DR   KEGG; ddi:DDB_G0273623; -.
DR   dictyBase; DDB_G0273249; hspE-1.
DR   dictyBase; DDB_G0273623; hspE-2.
DR   eggNOG; KOG0101; Eukaryota.
DR   HOGENOM; CLU_005965_3_0_1; -.
DR   InParanoid; Q557E0; -.
DR   OMA; VVVQFKG; -.
DR   PhylomeDB; Q557E0; -.
DR   Reactome; R-DDI-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR   PRO; PR:Q557E0; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005811; C:lipid droplet; HDA:dictyBase.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0045335; C:phagocytic vesicle; 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   GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
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   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW   Reference proteome; Stress response.
FT   CHAIN           1..632
FT                   /note="Heat shock cognate 70 kDa protein 2"
FT                   /id="PRO_0000327971"
FT   REGION          609..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        219
FT                   /note="K -> N (in Ref. 1; AAB81865)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        259
FT                   /note="L -> H (in Ref. 1; AAB81865)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   632 AA;  69790 MW;  6975BD250451CDCB CRC64;
     MSSSIGIDLG TTYSCVGVWQ NDRVEIIAND QGNRTTPSYV AFNETERLIG DAAKNQVAMN
     PTNTIFDAKR LIGRKFSDPV IQSDMKHWPF KVIAKEGDKP HLQVEFKGEV KTFSPEEVSS
     MVLLKMKETA EAYLGKTINN AVITVPAYFN DSQRQATKDA GAIAKLNVQR IINEPTAAAI
     AYGLEKKSQG ERNILIFDLG GGTFDVSLLT IEDGVFEVKA TAGDTHLGGE DFDNRLVNHF
     VDEFKRKHKK DLMTNQRALR RLRTACERAK RTLSSSAQAS IEIDSLFEGI DFYTSITRAR
     FEELCADLFR GCLDPVDKVL KDSKLDKKTI HEIVLVGGST RIPKVQQLLQ DHFNGKELNK
     SINPDEAVAY GAAVQAAILS NEGGAKVADI LLLDVAPLSM GLETAGGVMT TLIPRNTTIP
     CKKNQTFSTY SDNQTGVLVQ VYEGERAMTR DNNLLGKFEL TNIPPAPRGV PQIEVTFDID
     ANGILNVSAE DKSTGNKHKI TITNDKGRLT AEQIEKMVKD AEMFKAQDEA QREVVESKNK
     LENYAYTVRS TIKDDKIAAK LSKEDRKTVE EKSDEAINWL HANDSATKEE YEKAMKDLEA
     VCSPIISKVY GQQGGENPGN FSGAKTTEED LD
 
 
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