ID   HSP13_BOVIN             Reviewed;         471 AA.
AC   Q2TBX4;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Heat shock 70 kDa protein 13;
DE   AltName: Full=Stress-70 protein chaperone microsome-associated 60 kDa protein;
DE   Flags: Precursor;
GN   Name=HSPA13; Synonyms=STCH;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has peptide-independent ATPase activity. {ECO:0000250}.
CC   -!- SUBUNIT: Binds UBQLN2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Microsome {ECO:0000250}. Endoplasmic reticulum
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; BC109505; AAI09506.1; -; mRNA.
DR   RefSeq; NP_001033594.1; NM_001038505.2.
DR   AlphaFoldDB; Q2TBX4; -.
DR   SMR; Q2TBX4; -.
DR   STRING; 9913.ENSBTAP00000017155; -.
DR   PaxDb; Q2TBX4; -.
DR   PRIDE; Q2TBX4; -.
DR   Ensembl; ENSBTAT00000017155; ENSBTAP00000017155; ENSBTAG00000012908.
DR   GeneID; 505907; -.
DR   KEGG; bta:505907; -.
DR   CTD; 6782; -.
DR   VEuPathDB; HostDB:ENSBTAG00000012908; -.
DR   VGNC; VGNC:53581; HSPA13.
DR   eggNOG; KOG0101; Eukaryota.
DR   GeneTree; ENSGT00890000139503; -.
DR   HOGENOM; CLU_005965_0_3_1; -.
DR   InParanoid; Q2TBX4; -.
DR   OMA; LRKTNFN; -.
DR   OrthoDB; 288077at2759; -.
DR   TreeFam; TF105047; -.
DR   Reactome; R-BTA-3371453; Regulation of HSF1-mediated heat shock response.
DR   PRO; PR:Q2TBX4; -.
DR   Proteomes; UP000009136; Chromosome 1.
DR   Bgee; ENSBTAG00000012908; Expressed in spermatocyte and 111 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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   CDD; cd10237; HSPA13-like_NBD; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   InterPro; IPR042048; HSPA13.
DR   PANTHER; PTHR19375; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 2.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Endoplasmic reticulum; Microsome; Nucleotide-binding;
KW   Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..471
FT                   /note="Heat shock 70 kDa protein 13"
FT                   /id="PRO_0000289949"
FT   REGION          315..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..337
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   471 AA;  51920 MW;  5ED1779A14CAF5B3 CRC64;
     MAGEMTILGS AVLTLLLAGY LAQQYLPLPT PKVIGIDLGT TYCSVGVFFP GTGKVKVIPD
     ENGHISIPSM VSFTDDDVYV GYESLELADS NPQNTIYDAK RFIGKVFTPE ELEAEIGRYP
     FKVLNKNGMV EFSVTSNETI TVSPEYVGSR LLLKLKEMAE EYLGMPVANA VISVPAEFDL
     KQRNSTIQAA NLAGLKILRV INEPTAAAMA YGLHKAEVFH VLVIDLGGGT LDVSLLNKQG
     GMFLTRAMSG NNKLGGQDFN QRLLQYLYKQ IYQTYGFLPS RKEEIHRLRQ AVEMVKLNLT
     LHETAQMSVL LTVEENDRKG PPTSDSELPK DKFSQANDPH VDSMFGANLS EKKNGEGQVL
     FETEISRKLF DTLNEDLFQK ILVPIQQVLK EGHLEKTEID EVVLVGGSTR IPRIRQVIQE
     FFGKDPNTSV DPDLAVVTGV AIQAGIDGGS WPLQVSALEI PNKHLQKTNF N