ID   HSP74_CANLF             Reviewed;         840 AA.
AC   Q2TFN9;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Heat shock 70 kDa protein 4;
DE   AltName: Full=Heat shock 70-related protein APG-2;
GN   Name=HSPA4; Synonyms=APG2;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH TJP1.
RX   PubMed=16407410; DOI=10.1091/mbc.e05-06-0507;
RA   Tsapara A., Matter K., Balda M.S.;
RT   "The heat-shock protein Apg-2 binds to the tight junction protein ZO-1 and
RT   regulates transcriptional activity of ZONAB.";
RL   Mol. Biol. Cell 17:1322-1330(2006).
CC   -!- SUBUNIT: Interacts with TJP1/ZO-1. {ECO:0000269|PubMed:16407410}.
CC   -!- INTERACTION:
CC       Q2TFN9; O97758: TJP1; NbExp=3; IntAct=EBI-8002398, EBI-6988333;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; AY911512; AAX89038.1; -; mRNA.
DR   RefSeq; NP_001041481.1; NM_001048016.1.
DR   AlphaFoldDB; Q2TFN9; -.
DR   SMR; Q2TFN9; -.
DR   IntAct; Q2TFN9; 1.
DR   MINT; Q2TFN9; -.
DR   STRING; 9612.ENSCAFP00000001368; -.
DR   PaxDb; Q2TFN9; -.
DR   GeneID; 474680; -.
DR   KEGG; cfa:474680; -.
DR   CTD; 3308; -.
DR   eggNOG; KOG0103; Eukaryota.
DR   InParanoid; Q2TFN9; -.
DR   OrthoDB; 406172at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
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; 1.
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; Methylation; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Stress response.
FT   CHAIN           1..840
FT                   /note="Heat shock 70 kDa protein 4"
FT                   /id="PRO_0000289942"
FT   REGION          506..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          782..840
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..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   MOD_RES         53
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61316"
FT   MOD_RES         76
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P34932"
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:0000250|UniProtKB:P34932"
FT   MOD_RES         546
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P34932"
FT   MOD_RES         647
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         679
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P34932"
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"
SQ   SEQUENCE   840 AA;  94379 MW;  97FDB1918C45B563 CRC64;
     MSVVGIDLGF QSCYVAVARA GGIETIANEY SDRCTPACIS FGPKNRSIGA AAKSQVISNA
     KNTVQGFKRF HGRAFSDPFV EAEKSNLAYD IVQLPTGLTG IKVKYMEEER NFTTEQVTAM
     LLSKLKETAE SVLKKPVVDC VVSVPCFYTD AERRSVMDAT QIAGLNCLRL MNETTAVALA
     YGIYKQDLPA LEEKPRNVVF VDMGHSSYQV SVCAFNRGKL KVLATAFDTT LGGRKFDEVL
     VNHFCEEFGK KYKLDIKSKI RALLRLSQEC EKLKKLMSAN ASDLPLSIEC FMNDVDVSGT
     MNRGKFLEMC DDLLARVEPP LRSVLEQAKL RKEDIYAVEI VGGATRIPAV KEKISKFFGK
     ELSTTLNADE AVTRGCALQC AILSPAFKVR EFSITDVVPY SISLRWNSPA EEGSSDCEVF
     TKNHSAPFSK VLTFYRKEPF TLEAYYSSPQ DLPYPDPAIA QFLVQKVTPQ SDGSSSKVKV
     KVRVNVHGIF SVSSASLVEV LKFEENEEPM ETDQNAKEEE KMQVDQEEPH AEEQQQQTPA
     ENKAESEEME TSQAASKDKK MDQPPQAKKA KVKTSTVDLP IENQLLWQID REMLNLYIEN
     EGKMIMQDKL KKERNDAKNA VEEYVYEMRD KLSGEYEKFV SEDDRNSFTL KLEDTENWLY
     EDGEDQPKQV YVDKLAELKN LGQPIKMRFQ ESEERPKLFE ELGKQIQQYM KVISSFKNKE
     DQYDHLDAAD MLKVEKSTNE AMEWMNNKLN LQNKQSLTVD PVVKAKEIEA KIKELMSVCG
     PIISKPKPKV EPPKEEQKNA EQNGPVDGQG DSPGPQAAEQ GTDTAVPSDS DKKLPEMDID