HS7C1_DICDI
ID HS7C1_DICDI Reviewed; 640 AA.
AC P36415; Q55C64;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Heat shock cognate 70 kDa protein 1;
DE Short=HSC70-1;
GN Name=hspB; Synonyms=hsc70; ORFNames=DDB_G0269144;
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], INTERACTION WITH ACPA AND ACPB, AND FUNCTION.
RC STRAIN=AX3;
RX PubMed=8404847; DOI=10.1002/j.1460-2075.1993.tb06054.x;
RA Haus U., Trommler P., Fisher P.R., Hartmann H., Lottspeich F., Noegel A.A.,
RA Schleicher M.;
RT "The heat shock cognate protein from Dictyostelium affects actin
RT polymerization through interaction with the actin-binding protein
RT cap32/34.";
RL EMBO J. 12:3763-3771(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 34-46; 102-106 AND
RP 298-309.
RC STRAIN=AX3;
RX PubMed=8226849; DOI=10.1016/s0021-9258(19)49458-1;
RA Eddy R.J., Sauterer R.A., Condeelis J.S.;
RT "Aginactin, an agonist-regulated F-actin capping activity is associated
RT with an Hsc70 in Dictyostelium.";
RL J. Biol. Chem. 268:23267-23274(1993).
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 FUNCTION.
RX PubMed=8982279; DOI=10.1016/s0167-4889(96)00108-5;
RA Eddy R.J., Han J., Sauterer R.A., Condeelis J.S.;
RT "A major agonist-regulated capping activity in Dictyostelium is due to the
RT capping protein, cap32/34.";
RL Biochim. Biophys. Acta 1314:247-259(1996).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16782229; DOI=10.1016/j.ejcb.2006.05.008;
RA Koch K.V., Reinders Y., Ho T.-H., Sickmann A., Graef R.;
RT "Identification and isolation of Dictyostelium microtubule-associated
RT protein interactors by tandem affinity purification.";
RL Eur. J. Cell Biol. 85:1079-1090(2006).
RN [6]
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 [7]
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: Affects actin polymerization through interaction with the
CC actin-binding protein CAP32/34 (acpA/acpB). Acts as a chaperone by
CC stimulating the refolding of denaturated acpA and acpB, but neither
CC stimulates nor inhibits the capping activity of native CAP32/34.
CC {ECO:0000269|PubMed:8404847, ECO:0000269|PubMed:8982279}.
CC -!- SUBUNIT: Interacts with the heterodimeric F-actin-capping protein
CC CAP32/34 (acpA/acpB). Binds via its C-terminal tail and interaction is
CC ATP-dependent. {ECO:0000269|PubMed:8404847}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Found in F-actin-rich regions of
CC the cell cortex and cell protrusions.
CC -!- DEVELOPMENTAL STAGE: Heat shock cognate proteins are expressed
CC constitutively during normal development. Up-regulated in aspidocytes,
CC a resistant cell type induced from amoebae by a range of toxins
CC including heavy metals and antibiotics. {ECO:0000269|PubMed:17259634}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; X75263; CAA53039.1; -; mRNA.
DR EMBL; L22736; AAA33219.1; -; mRNA.
DR EMBL; AAFI02000005; EAL71922.1; -; Genomic_DNA.
DR PIR; A48872; A48872.
DR PIR; S37394; S37394.
DR RefSeq; XP_646617.1; XM_641525.1.
DR AlphaFoldDB; P36415; -.
DR SMR; P36415; -.
DR STRING; 44689.DDB0191168; -.
DR SWISS-2DPAGE; P36415; -.
DR PaxDb; P36415; -.
DR PRIDE; P36415; -.
DR EnsemblProtists; EAL71922; EAL71922; DDB_G0269144.
DR GeneID; 8617589; -.
DR KEGG; ddi:DDB_G0269144; -.
DR dictyBase; DDB_G0269144; hspB.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_0_0_1; -.
DR InParanoid; P36415; -.
DR OMA; KANPIMM; -.
DR PhylomeDB; P36415; -.
DR Reactome; R-DDI-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-DDI-3371571; HSF1-dependent transactivation.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-DDI-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-DDI-8876725; Protein methylation.
DR PRO; PR:P36415; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR GO; GO:0051015; F:actin filament binding; IDA: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 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..640
FT /note="Heat shock cognate 70 kDa protein 1"
FT /id="PRO_0000078300"
FT REGION 609..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 1..29
FT /note="MSSIGIDLGTTYSCVGVWQNDRVEIIAND -> IHHHINGNATWVVESGPVS
FT EVLSFN (in Ref. 2; AAA33219)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="N -> T (in Ref. 2; AAA33219)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="V -> A (in Ref. 2; AAA33219)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="A -> R (in Ref. 1; CAA53039)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="S -> A (in Ref. 2; AAA33219)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="V -> A (in Ref. 2; AAA33219)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="I -> L (in Ref. 2; AAA33219)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="F -> P (in Ref. 2; AAA33219)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 640 AA; 70415 MW; 4812A47E93AFFBFF CRC64;
MSSIGIDLGT TYSCVGVWQN DRVEIIANDQ GNRTTPSYVA FTDTERLIGD AAKNQVAMNP
TNTVFDAKRL IGRKFSDKEV QSDMKHWPFK VIPKDGDKPH IQVEFKGETK VFSPEEISSM
VLLKMKETAE AYLGKTINNA VITVPAYFND SQRQATKDAG TISKLNVQRI INEPTAAAIA
YGLEKKGSGE KNILIFDLGG GTFDVSLLTI EDGVFEVKAT AGDTHLGGED FDNRLVSHFV
DEFKRKHKKD IMGNQRAVRR LRTACERAKR TLSSSAQASI EIDSLFEGID FYTSITRARF
EELCADLFRG CLDPVEKVLK DSKLDKKSIH EIVLVGGSTR IPKVQQLLQE FFNGKELNKS
INPDEAVAYG AAVQAAILSN EGGAKVADLL LLDVAPLSMG LETAGGVMTT LIPRNTTIPC
KKTQTFSTYS DNQPGVLIQV YEGERAMTKD NNLLGKFELS GIPPAPRGVP QVEVTFDVDA
NGILNVSAED KSTGNKQKIT ITNDKGRLSK EEIEKMVADA EKFKQQDEQQ KDRVESKNKL
ENYAFTVKNS IKDEKVAAKI SDSDKSTIES ETESVLKWLE SNQTAEKDEY EDKMKALEAV
VNPIMSKLYQ EGGMPQGGGM PGGMSNDSPK SSNNKVDELD
