HSP74_RAT
ID HSP74_RAT Reviewed; 840 AA.
AC O88600;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Heat shock 70 kDa protein 4;
DE AltName: Full=Ischemia responsive 94 kDa protein;
GN Name=Hspa4; Synonyms=Irp94;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RX PubMed=10098860; DOI=10.1046/j.1471-4159.1999.721544.x;
RA Yagita Y., Kitagawa K., Taguchi A., Ohtsuki T., Kuwabara K., Mabuchi T.,
RA Matsumoto M., Yanagihara T., Hori M.;
RT "Molecular cloning of a novel member of the HSP110 family of genes,
RT ischemia-responsive protein 94 kDa (irp94), expressed in rat brain after
RT transient forebrain ischemia.";
RL J. Neurochem. 72:1544-1551(1999).
RN [2]
RP PROTEIN SEQUENCE OF 391-405; 574-591 AND 619-629, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Chen W.-Q., Afjehi-Sadat L.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND THR-538, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- SUBUNIT: Interacts with TJP1/ZO-1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in testis.
CC {ECO:0000269|PubMed:10098860}.
CC -!- INDUCTION: Up-regulated in neuronal cells upon ischemia.
CC {ECO:0000269|PubMed:10098860}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; AF077354; AAC27937.1; -; mRNA.
DR RefSeq; NP_705893.1; NM_153629.1.
DR AlphaFoldDB; O88600; -.
DR SMR; O88600; -.
DR BioGRID; 251801; 18.
DR IntAct; O88600; 3.
DR MINT; O88600; -.
DR STRING; 10116.ENSRNOP00000023628; -.
DR iPTMnet; O88600; -.
DR PhosphoSitePlus; O88600; -.
DR World-2DPAGE; 0004:O88600; -.
DR jPOST; O88600; -.
DR PaxDb; O88600; -.
DR PRIDE; O88600; -.
DR GeneID; 266759; -.
DR KEGG; rno:266759; -.
DR UCSC; RGD:628878; rat.
DR CTD; 3308; -.
DR RGD; 628878; Hspa4.
DR eggNOG; KOG0103; Eukaryota.
DR InParanoid; O88600; -.
DR OrthoDB; 406172at2759; -.
DR PhylomeDB; O88600; -.
DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR ChiTaRS; Hspa4; rat.
DR PRO; PR:O88600; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR GO; GO:0005811; C:lipid droplet; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
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; IPI:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:RGD.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISO:RGD.
DR GO; GO:0001822; P:kidney development; IEP:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEP:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
DR GO; GO:0043392; P:negative regulation of DNA binding; IMP:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEP:RGD.
DR GO; GO:0032092; P:positive regulation of protein binding; IDA:RGD.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; ISO:RGD.
DR GO; GO:0009408; P:response to heat; IDA:RGD.
DR CDD; cd11737; HSPA4_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 2.
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 InterPro; IPR042052; HSPA4_NBD.
DR Pfam; PF00012; HSP70; 2.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 2.
DR SUPFAM; SSF53067; SSF53067; 2.
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..840
FT /note="Heat shock 70 kDa protein 4"
FT /id="PRO_0000255934"
FT REGION 500..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61316"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 89
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P34932"
FT MOD_RES 336
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P34932"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34932"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61316"
FT MOD_RES 430
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P34932"
FT MOD_RES 538
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34932"
FT MOD_RES 660
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q61316"
FT MOD_RES 756
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34932"
FT MOD_RES 773
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P34932"
FT CONFLICT 627..628
FT /note="EM -> DF (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 840 AA; 94057 MW; 77BC00171669BF71 CRC64;
MSVVGIDLGF QSCYVAVARA GGIETIANEY SDRCTPACVS FGPKNRSVGA AAKSQVISNA
KNTVQGFKRF HGRAFSDPFV EAEKSNLAYD IVQLPTGLTG IKVTYMEEER NFTTEQVTAM
LLSKLKETAE SVLKKPVVDC VVSVPSFYTD AERRSVMDAT QIAGLNCLRL MNETTAVALA
YGIYKQDLPA LEEKPRNVVF VDMGHSAYQV SVCAFNRGKL KVLATAFDTT LGGRKFDEVL
VNHFCEEFGK KYKLDIKSKV RALLRLSQEC EKLKKLMSAN ASDLPLSIEC FMNDIDVSGT
MNRGKFLEMC DDLLARVEPP LRSILDQSKL KKEDIYAVEI VGGATRIPAV KEKISKFFGK
ELSTTLNADE AVTRGCALQC AILSPAFKVR EFSITDVVPY PISLRWNSPA EEGSSDCEVF
PKNHAAPFSK VLTFYRKEPF TLEAYYSSPQ DLPYPDPAIA QFSVQKVTPQ SDGSSSKVKV
KVRVNVHGIF SVSSAALVEV HKSEESEEPM ETDQNAKEEE KMQVDQEEPH TEEQQPQTPA
ENKAESEEME TSQAGSKDKK MDQPPQAKKA KVKTSTVDLP IESQLLWQLD REMLGLYTEN
EGKMIMQDKL EKERNDAKNA VEEYVYEMRD KLSGEYEKFV SEDDRNNFTL KLEDTENWLY
EDGEDQPKQV YVDKLAELRT LGQPIKTRFQ ESEERPKLFE ELGKQIQQYM KVISSFKNKE
DQYEHLDAAD MTKVEKSTNE AMEWMNSKLN LQNKQSLTAD PVVKTKEIEA KIKELTNICS
PIISKPKPKV EPPKEEPKHA EQNGPVDGQG DNPGTQAAEH GADTAVPSDG DKKLPEMDID
