ID   F1SK58_PIG              Unreviewed;       427 AA.
AC   F1SK58;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2022, sequence version 3.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=Heat shock protein family A (Hsp70) member 13 {ECO:0000313|Ensembl:ENSSSCP00000012792.4};
GN   Name=HSPA13 {ECO:0000313|Ensembl:ENSSSCP00000012792.4,
GN   ECO:0000313|VGNC:VGNC:108663};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000012792.4, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000012792.4, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000012792.4,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000012792.4}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381}.
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DR   AlphaFoldDB; F1SK58; -.
DR   STRING; 9823.ENSSSCP00000012792; -.
DR   PaxDb; 9823-ENSSSCP00000012792; -.
DR   PeptideAtlas; F1SK58; -.
DR   Ensembl; ENSSSCT00000013138.5; ENSSSCP00000012792.4; ENSSSCG00000012007.5.
DR   VGNC; VGNC:108663; HSPA13.
DR   eggNOG; KOG0101; Eukaryota.
DR   GeneTree; ENSGT00890000139503; -.
DR   HOGENOM; CLU_005965_0_3_1; -.
DR   InParanoid; F1SK58; -.
DR   TreeFam; TF105047; -.
DR   Reactome; R-SSC-3371453; Regulation of HSF1-mediated heat shock response.
DR   Proteomes; UP000008227; Chromosome 13.
DR   Bgee; ENSSSCG00000012007; Expressed in pituitary gland and 43 other cell types or tissues.
DR   Genevisible; F1SK58; SS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0044183; F:protein folding chaperone; 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   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; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375:SF169; HEAT SHOCK 70 KDA PROTEIN 13; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   Pfam; PF00012; HSP70; 2.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:F1SK58};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT   REGION          269..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..294
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   427 AA;  47615 MW;  1E33B3B75946F718 CRC64;
     MAGEMTILGK VKVIPDENGH ISIPSMVSFT DDDVYVGYES LELADSNPQN TIYDAKRFIG
     KIFTPEELEA EIGRYPFKVL NKNGMVEFSV TSNETITVTP EYVGSRLLLK LKEMAEEYLG
     MPVANAVISV PAEFDLKQRN STIEAANLAG LKILRVINEP TAAAMAYGLH KADVFHVLVI
     DLGGGTLDVS LLNKQGGMFL TRAMSGNNKL GGQDFNQRLL QYLYKQIYQT YGFIPSRKEE
     IHRLRQAVEM VKLNLTLHQT AHMSVLLTVE EKDRREPQST DAELPKDRLS SADRPHMNRV
     FGATLSEKKN GESQVLFETE ISRKLFDTLN EDLFQKILVP IQQVLKEGHL EKTEIDEVVL
     VGGSTRIPRI RQVIQEFFGK DPNTSVDPDL AVVTGVAIQA GIDGGSWPLQ VSALEIPNKH
     LQKTNFN
//