ID   L5JR15_PTEAL            Unreviewed;       470 AA.
AC   L5JR15;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Heat shock 70 kDa protein 13 {ECO:0000256|ARBA:ARBA00018765};
DE   AltName: Full=Stress-70 protein chaperone microsome-associated 60 kDa protein {ECO:0000256|ARBA:ARBA00031426};
GN   ORFNames=PAL_GLEAN10016368 {ECO:0000313|EMBL:ELK00568.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK00568.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- FUNCTION: Has peptide-independent ATPase activity.
CC       {ECO:0000256|ARBA:ARBA00002077}.
CC   -!- SUBUNIT: Binds UBQLN2. {ECO:0000256|ARBA:ARBA00011671}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000256|ARBA:ARBA00004240}. Microsome
CC       {ECO:0000256|ARBA:ARBA00004144}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381}.
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DR   EMBL; KB031157; ELK00568.1; -; Genomic_DNA.
DR   RefSeq; XP_006926290.1; XM_006926228.2.
DR   AlphaFoldDB; L5JR15; -.
DR   STRING; 9402.L5JR15; -.
DR   GeneID; 102898565; -.
DR   KEGG; pale:102898565; -.
DR   CTD; 6782; -.
DR   eggNOG; KOG0101; Eukaryota.
DR   InParanoid; L5JR15; -.
DR   OrthoDB; 143at2759; -.
DR   Proteomes; UP000010552; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; 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; cd10237; HSPA13-like_NBD; 1.
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   InterPro; IPR042048; HSPA13.
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; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022848};
KW   Microsome {ECO:0000256|ARBA:ARBA00022848};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Stress response {ECO:0000313|EMBL:ELK00568.1}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..470
FT                   /note="Heat shock 70 kDa protein 13"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005688079"
FT   REGION          314..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   470 AA;  51970 MW;  E7061320CC329030 CRC64;
     MAGEMTILGS AVLTLLLAGY LAQQYLPLPT PKVIGIDLGT TYCSVGVFFP GTGKVKVIPD
     ENGHISIPSM VSFTDHDVYV GYESLELADS NPQNTIYDAK RFIGKIFTPE ELEAEIGRYP
     FKVLNKNGMV EFSVTSNETI TVSPEYVGSR LLLKLKEMAE EYLGMPVVNA VISVPAEFDL
     KQRNSTIEAA NLAGLKILRV INEPTAAAMA YGLHKVDVFH VLVIDLGGGT LDVSLLNKQG
     GMFLTRAMSG NNKLGGQDFN QRLLQYVYKQ IYQTYGFVPS KKEEIHRLRQ AVEMVKLNLT
     LHQSAHMSVL LTVEEEDKKE PQSSDTELPK DRLSPADGYH VNSKFGTGLS EKKRESQVLF
     ETEISRKLFD TLNEDLFQKI LVPIQQVLKD GHLEKTEIDE VVLVGGSTRI PRIRQVIQEF
     FGKDPNTSVD PDLAVVTGVA IQAGIDGGSW PLQVSALEIP NKHLQKTNFN
//