ID   HS74L_MESAU             Reviewed;         211 AA.
AC   P86265;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Heat shock 70 kDa protein 4L {ECO:0000250|UniProtKB:O95757};
DE   AltName: Full=Heat shock 70-related protein APG-1 {ECO:0000250|UniProtKB:O95757};
DE   AltName: Full=Osmotic stress protein 94 {ECO:0000250|UniProtKB:O95757};
DE   Flags: Fragments;
GN   Name=HSPA4L {ECO:0000250|UniProtKB:O95757};
GN   Synonyms=APG1 {ECO:0000250|UniProtKB:O95757},
GN   OSP94 {ECO:0000250|UniProtKB:O95757};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20400973; DOI=10.1038/aja.2010.19;
RA   Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT   "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT   (GP96) are unique to hamster caput epididymal spermatozoa.";
RL   Asian J. Androl. 12:344-355(2010).
CC   -!- FUNCTION: Possesses chaperone activity in vitro where it inhibits
CC       aggregation of citrate synthase. {ECO:0000250|UniProtKB:O95757}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O95757}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95757}. Nucleus
CC       {ECO:0000250|UniProtKB:O95757}. Note=May translocate to the nucleus
CC       after heat shock. {ECO:0000250|UniProtKB:O95757}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000255}.
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DR   AlphaFoldDB; P86265; -.
DR   eggNOG; KOG0103; Eukaryota.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; 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   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   Pfam; PF00012; HSP70; 2.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Stress response.
FT   CHAIN           <1..>211
FT                   /note="Heat shock 70 kDa protein 4L"
FT                   /id="PRO_0000394416"
FT   MOD_RES         161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95757"
FT   NON_CONS        43..44
FT                   /evidence="ECO:0000305"
FT   NON_CONS        59..60
FT                   /evidence="ECO:0000305"
FT   NON_CONS        79..80
FT                   /evidence="ECO:0000305"
FT   NON_CONS        94..95
FT                   /evidence="ECO:0000305"
FT   NON_CONS        152..153
FT                   /evidence="ECO:0000305"
FT   NON_CONS        160..161
FT                   /evidence="ECO:0000305"
FT   NON_CONS        172..173
FT                   /evidence="ECO:0000305"
FT   NON_CONS        185..186
FT                   /evidence="ECO:0000305"
FT   NON_CONS        194..195
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         211
SQ   SEQUENCE   211 AA;  23670 MW;  E61393D6FD82A4FC CRC64;
     SVVGIDLGFL NCYIAVARSG GIETIANEYS DRCTPACISL GSRSQIVTNV RNTIHGFKKI
     RLPYELQKMP NGSTGVKVRL KVLATTFDPY LGGRVEPPLK SVMDQANLQR EDINSIEIVG
     GATRIPAVKE QVTRFFLKDI STTLNADEAV ARNHPAPFSK SIDLPIQSSL YRNAVEEYVY
     DFRDKFITPE DMNKYGQPIQ MKYVEHEERP K