HSP7D_DROME
ID HSP7D_DROME Reviewed; 651 AA.
AC P11147; Q3KN45; Q8SXQ4; Q9VFB0;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 3.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Heat shock 70 kDa protein cognate 4;
DE AltName: Full=Heat shock 70 kDa protein 88E;
GN Name=Hsc70-4; Synonyms=Hsc4; ORFNames=CG4264;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Embryo;
RX PubMed=8514184; DOI=10.1016/0378-1119(93)90558-k;
RA Rubin D.M., Mehta A., Zhu J., Shoham S., Chen X.J., Wells Q., Palter K.B.;
RT "Genomic structure and sequence analysis of Drosophila melanogaster HSC70
RT genes.";
RL Gene 128:155-163(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2111451; DOI=10.1128/mcb.10.6.3232-3238.1990;
RA Perkins L.A., Doctor J.S., Zhang K., Stinson L., Perrimon N., Craig E.A.;
RT "Molecular and developmental characterization of the heat shock cognate 4
RT gene of Drosophila melanogaster.";
RL Mol. Cell. Biol. 10:3232-3238(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-104.
RX PubMed=6311649; DOI=10.1016/0012-1606(83)90291-9;
RA Craig E.A., Ingolia T.D., Manseau L.J.;
RT "Expression of Drosophila heat-shock cognate genes during heat shock and
RT development.";
RL Dev. Biol. 99:418-426(1983).
RN [8]
RP PROTEIN SEQUENCE OF 580-592.
RC STRAIN=Vallecas; TISSUE=Wing imaginal disk;
RX PubMed=8500545; DOI=10.1006/excr.1993.1141;
RA Santaren J.F., van Damme J., Puype M., Vandekerckhove J.,
RA Garcia-Bellido A.;
RT "Identification of Drosophila wing imaginal disc proteins by two-
RT dimensional gel analysis and microsequencing.";
RL Exp. Cell Res. 206:220-226(1993).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-35, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
CC -!- INTERACTION:
CC P11147; O96757: stumps; NbExp=3; IntAct=EBI-75181, EBI-74922;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Nucleus.
CC Note=Localized to a meshwork of cytoplasmic fibers around the nucleus.
CC Translocates to the nucleus after thermal stress.
CC -!- DEVELOPMENTAL STAGE: Heat shock cognate proteins are expressed
CC constitutively during normal development.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; L01500; AAB59186.1; -; Genomic_DNA.
DR EMBL; M36114; AAA28627.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF55150.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13637.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13638.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13639.1; -; Genomic_DNA.
DR EMBL; AE014297; AAO41567.1; -; Genomic_DNA.
DR EMBL; AE014297; AAO41568.1; -; Genomic_DNA.
DR EMBL; AY084193; AAL89931.1; -; mRNA.
DR EMBL; BT023894; ABA81828.1; -; mRNA.
DR EMBL; J02569; AAA28631.1; ALT_SEQ; Genomic_DNA.
DR PIR; A36333; A36333.
DR RefSeq; NP_001262586.1; NM_001275657.1.
DR RefSeq; NP_524356.1; NM_079632.6.
DR RefSeq; NP_731987.1; NM_169625.2.
DR RefSeq; NP_731988.1; NM_169626.2.
DR RefSeq; NP_731989.1; NM_169627.2.
DR RefSeq; NP_788679.1; NM_176502.2.
DR RefSeq; NP_788680.1; NM_176503.2.
DR AlphaFoldDB; P11147; -.
DR SMR; P11147; -.
DR BioGRID; 66904; 87.
DR DIP; DIP-19158N; -.
DR IntAct; P11147; 12.
DR MINT; P11147; -.
DR STRING; 7227.FBpp0082516; -.
DR GlyGen; P11147; 1 site.
DR iPTMnet; P11147; -.
DR PaxDb; P11147; -.
DR PRIDE; P11147; -.
DR DNASU; 41840; -.
DR EnsemblMetazoa; FBtr0083055; FBpp0082514; FBgn0266599.
DR EnsemblMetazoa; FBtr0083056; FBpp0082515; FBgn0266599.
DR EnsemblMetazoa; FBtr0083057; FBpp0082516; FBgn0266599.
DR EnsemblMetazoa; FBtr0083058; FBpp0082517; FBgn0266599.
DR EnsemblMetazoa; FBtr0083059; FBpp0082518; FBgn0266599.
DR EnsemblMetazoa; FBtr0083060; FBpp0082519; FBgn0266599.
DR EnsemblMetazoa; FBtr0337053; FBpp0307982; FBgn0266599.
DR GeneID; 41840; -.
DR KEGG; dme:Dmel_CG4264; -.
DR CTD; 41840; -.
DR FlyBase; FBgn0266599; Hsc70-4.
DR VEuPathDB; VectorBase:FBgn0266599; -.
DR eggNOG; KOG0101; Eukaryota.
DR GeneTree; ENSGT00940000154813; -.
DR HOGENOM; CLU_005965_3_0_1; -.
DR InParanoid; P11147; -.
DR OMA; VVVQFKG; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; P11147; -.
DR Reactome; R-DME-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-DME-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-DME-3371571; HSF1-dependent transactivation.
DR Reactome; R-DME-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-DME-888590; GABA synthesis, release, reuptake and degradation.
DR SignaLink; P11147; -.
DR BioGRID-ORCS; 41840; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Hsc70-4; fly.
DR GenomeRNAi; 41840; -.
DR PRO; PR:P11147; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0266599; Expressed in wing disc and 23 other tissues.
DR ExpressionAtlas; P11147; baseline and differential.
DR Genevisible; P11147; DM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005726; C:perichromatin fibrils; IDA:FlyBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
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:0051087; F:chaperone binding; IDA:FlyBase.
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:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0007413; P:axonal fasciculation; IMP:FlyBase.
DR GO; GO:0035967; P:cellular response to topologically incorrect protein; IMP:FlyBase.
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:0061077; P:chaperone-mediated protein folding; IDA:FlyBase.
DR GO; GO:0061738; P:late endosomal microautophagy; IMP:FlyBase.
DR GO; GO:0097753; P:membrane bending; IDA:FlyBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:FlyBase.
DR GO; GO:0007399; P:nervous system development; IMP:FlyBase.
DR GO; GO:0007269; P:neurotransmitter secretion; IMP:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IMP:FlyBase.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0070922; P:RISC complex assembly; IGI:FlyBase.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:FlyBase.
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; Cytoplasm; Direct protein sequencing; Glycoprotein;
KW Nucleotide-binding; Nucleus; Reference proteome; Stress response.
FT CHAIN 1..651
FT /note="Heat shock 70 kDa protein cognate 4"
FT /id="PRO_0000078340"
FT REGION 621..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CONFLICT 167
FT /note="L -> P (in Ref. 2; AAA28627)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="L -> P (in Ref. 2; AAA28627)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="K -> Q (in Ref. 5; AAL89931)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="N -> S (in Ref. 5; AAL89931)"
FT /evidence="ECO:0000305"
FT CONFLICT 625
FT /note="P -> G (in Ref. 2; AAA28627)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 651 AA; 71131 MW; 30F6BD7E07407B63 CRC64;
MSKAPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
MNPTQTIFDA KRLIGRKFDD AAVQSDMKHW PFEVVSADGK PKIEVTYKDE KKTFFPEEIS
SMVLTKMKET AEAYLGKTVT NAVITVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA
IAYGLDKKAV GERNVLIFDL GGGTFDVSIL SIDDGIFEVK STAGDTHLGG EDFDNRLVTH
FVQEFKRKHK KDLTTNKRAL RRLRTACERA KRTLSSSTQA SIEIDSLFEG TDFYTSITRA
RFEELNADLF RSTMDPVEKA LRDAKLDKSV IHDIVLVGGS TRIPKVQRLL QDLFNGKELN
KSINPDEAVA YGAAVQAAIL HGDKSQEVQD LLLLDVTPLS LGIETAGGVM SVLIKRNTTI
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LSGIPPAPRG VPQIEVTFDI
DANGILNVTA LERSTNKENK ITITNDKGRL SKEDIERMVN EAEKYRNEDE KQKETIAAKN
GLESYCFNMK ATLDEDNLKT KISDSDRTTI LDKCNETIKW LDANQLADKE EYEHRQKELE
GVCNPIITKL YQGAGFPPGG MPGGPGGMPG AAGAAGAAGA GGAGPTIEEV D
