ID   HSP74_MOUSE             Reviewed;         841 AA.
AC   Q61316;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 149.
DE   RecName: Full=Heat shock 70 kDa protein 4;
DE   AltName: Full=Heat shock 70-related protein APG-2;
GN   Name=Hspa4; Synonyms=Apg2, Hsp110;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=DDY/STD; TISSUE=Testis;
RX   PubMed=9161406; DOI=10.1016/s0378-1119(96)00807-4;
RA   Kaneko Y., Kimura T., Kishishita M., Noda Y., Fujita J.;
RT   "Cloning of apg-2 encoding a novel member of heat shock protein 110
RT   family.";
RL   Gene 189:19-24(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 74-124; 155-169; 186-196; 220-234; 330-346; 361-374;
RP   391-405; 699-705 AND 719-734, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-336 AND TYR-661, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Mast cell;
RX   PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-336, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-415 AND THR-540, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- SUBUNIT: Interacts with TJP1/ZO-1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; D85904; BAA12914.1; -; mRNA.
DR   AlphaFoldDB; Q61316; -.
DR   SMR; Q61316; -.
DR   DIP; DIP-46965N; -.
DR   IntAct; Q61316; 8.
DR   MINT; Q61316; -.
DR   STRING; 10090.ENSMUSP00000020630; -.
DR   GlyGen; Q61316; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q61316; -.
DR   PhosphoSitePlus; Q61316; -.
DR   SwissPalm; Q61316; -.
DR   REPRODUCTION-2DPAGE; Q61316; -.
DR   CPTAC; non-CPTAC-3824; -.
DR   EPD; Q61316; -.
DR   jPOST; Q61316; -.
DR   MaxQB; Q61316; -.
DR   PaxDb; 10090-ENSMUSP00000020630; -.
DR   PeptideAtlas; Q61316; -.
DR   ProteomicsDB; 273195; -.
DR   Pumba; Q61316; -.
DR   AGR; MGI:1342292; -.
DR   MGI; MGI:1342292; Hspa4.
DR   eggNOG; KOG0103; Eukaryota.
DR   InParanoid; Q61316; -.
DR   Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR   ChiTaRS; Hspa4; mouse.
DR   PRO; PR:Q61316; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q61316; Protein.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR   GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
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:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISO:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:0051402; P:neuron apoptotic process; ISO:MGI.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; ISO:MGI.
DR   GO; GO:1903978; P:regulation of microglial cell activation; ISO:MGI.
DR   CDD; cd11737; HSPA4_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 2.
DR   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
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   InterPro; IPR042052; HSPA4_NBD.
DR   PANTHER; PTHR45639:SF6; HEAT SHOCK 70 KDA PROTEIN 4; 1.
DR   PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR   Pfam; PF00012; HSP70; 2.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 2.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing;
KW   Methylation; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Stress response.
FT   CHAIN           1..841
FT                   /note="Heat shock 70 kDa protein 4"
FT                   /id="PRO_0000078263"
FT   REGION          500..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          783..841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..532
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..569
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        789..803
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        826..841
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         53
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         76
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         89
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P34932"
FT   MOD_RES         336
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:17947660,
FT                   ECO:0007744|PubMed:18034455"
FT   MOD_RES         393
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P34932"
FT   MOD_RES         415
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         430
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P34932"
FT   MOD_RES         540
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         548
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P34932"
FT   MOD_RES         661
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:17947660"
FT   MOD_RES         680
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P34932"
FT   MOD_RES         757
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P34932"
FT   MOD_RES         774
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P34932"
SQ   SEQUENCE   841 AA;  94133 MW;  E7FF19F555C115ED CRC64;
     MSVVGIDLGF QSCYVAVARA GGIETIANEY SDRCTPACVS FGPKNRSIGA AAKSQVISNA
     KNTVQGFKRF HGRAFSDPFV EAEKSNLAYD IVQLPTGLTG IKVTYMEEER NFTTEQVTAM
     LLSKLKETAE SVLKKPVVDC VVSVPSFYTD AERRSVMDAT QIAGLNCLRL MNETTAVALA
     YGIYKQDLPA LEEKPRNVVF VDMGHSAYQV SVCAFNKGKL KVLATAFDTT LGGRKFDEVL
     VNHFCEEFGK KYKLDIKSKI RALLRLSQEC EKLKKLMSAN ASDLPLSIEC FMNDIDVSGT
     MNRGKFLEMC DDLLARVEPP LRSVLEQSKL KKEDIYAVEI VGGATRIPAV KEKISKFFGK
     ELSTTLNADE AVTRGCALQC AILSPAFKVR EFSITDVVPY PISLRWNSPA EEGLSDCEVF
     PKNHAAPFSK VLTFYRKEPF TLEAYYSSPQ DLPYPDPAIA QFSVQKVTPQ SDGSSSKVKV
     KVRVNVHGIF SVSSAALVEV HKSEESEEPM ETDQNAKEEE KMQVDQEEPH TEEQQQQPQT
     PAENKAESEE METSQAGSKD KKTDQPPQAK KAKVKTSTVD LPIEHTLWQL DREMLALYTE
     NEGKMIMQDK LEKERNDAKN AVEEYVYEMR DKLSGEYEKF VSEDDRNTFT LKLEDTENWL
     YEDGEDQPKQ VYVDKLAELK SLGQPIKTRF QESEERPKLF EELGKQIQQY MKVISSFKNK
     EDQYEHLDAA DVTKVEKSTN EAMEWMNSKL NLQNKQSLTV DPVVKTKEIE AKIKELTSIC
     SPIISKPKPK VEPPKEEPKH AEQNGPVDGQ GDNPGSQAAE HGADTAVPSD GDKKLPEMDI
     D
//