ID   HPBP1_MACFA             Reviewed;         364 AA.
AC   Q4R588;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Hsp70-binding protein 1;
DE            Short=HspBP1;
DE   AltName: Full=Heat shock protein-binding protein 1;
DE   AltName: Full=Hsp70-interacting protein 1;
GN   Name=HSPBP1; ORFNames=QccE-13919;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Inhibits HSPA1A chaperone activity by changing the
CC       conformation of the ATP-binding domain of HSPA1A and interfering with
CC       ATP binding. Interferes with ubiquitination mediated by STUB1 and
CC       inhibits chaperone-assisted degradation of target proteins (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the ATP-binding domain of HSPA1A. Detected in a
CC       ternary complex containing STUB1, HSPA1A and HSPBP1 (By similarity).
CC       Interacts with PGLYRP1; this interaction blocks the cytotoxic activity
CC       of the PGLYRP1-HSPA1A complex (By similarity). {ECO:0000250}.
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DR   EMBL; AB169656; BAE01737.1; -; mRNA.
DR   AlphaFoldDB; Q4R588; -.
DR   SMR; Q4R588; -.
DR   STRING; 9541.XP_005590443.1; -.
DR   eggNOG; KOG2160; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR013918; Nucleotide_exch_fac_Fes1.
DR   Pfam; PF08609; Fes1; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..364
FT                   /note="Hsp70-binding protein 1"
FT                   /id="PRO_0000084036"
FT   REPEAT          137..179
FT                   /note="ARM 1"
FT   REPEAT          182..222
FT                   /note="ARM 2"
FT   REPEAT          225..264
FT                   /note="ARM 3"
FT   REPEAT          267..306
FT                   /note="ARM 4"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         356
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL4"
FT   MOD_RES         361
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL4"
SQ   SEQUENCE   364 AA;  39686 MW;  657FB32B64CDF1C0 CRC64;
     MSDEGSRGSR LPLALPPASQ GCSSGGGGGG GGGGSSSAGG SGNPRPPRNL QGLLQMAITA
     GSEEPDPPPE PMSEERRQWL QEAMSAAFRG QREEVEQMKS CLRVLSQPMP PTAGEAEQAA
     DQQEREGALE LLADLCENMD NAADFCQLSG MHLLVGRYLE AGAAGLRWRA AQLIGTCSQN
     VAAIQEQVLG LGALRKLLRL LDRDACDTVR VKALFAISCL VREQEAGLLQ FLRLDGFSVL
     MRAMQQQVQK LKVKSAFLLQ NLLVGHPEHR GTLCSMGMVQ QLVALVRTEH SPFHEHVLGA
     LCSLVTDFPQ GVRECREPEL GLEELLRHRC QLLQQHEEYQ EELEFCEKLL QTCFSSPTDD
     SMDR