ID   F10A1_PONAB             Reviewed;         369 AA.
AC   Q5RF31;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Hsc70-interacting protein;
DE            Short=Hip;
DE   AltName: Full=Protein FAM10A1;
DE   AltName: Full=Protein ST13 homolog;
GN   Name=ST13; Synonyms=FAM10A1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One HIP oligomer binds the ATPase domains of at least two
CC       HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40.
CC       Stabilizes the ADP state of HSC70 that has a high affinity for
CC       substrate protein. Through its own chaperone activity, it may
CC       contribute to the interaction of HSC70 with various target proteins (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotetramer. Interacts with HSC70 as well as DNAJ homologs
CC       and HSP90 (By similarity). Interacts (via the C-terminus 303- 319 AA)
CC       with GRK5 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FAM10 family. {ECO:0000305}.
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DR   EMBL; CR857330; CAH89626.1; -; mRNA.
DR   EMBL; CR926105; CAI29731.1; -; mRNA.
DR   RefSeq; NP_001127121.1; NM_001133649.1.
DR   AlphaFoldDB; Q5RF31; -.
DR   SMR; Q5RF31; -.
DR   STRING; 9601.ENSPPYP00000013232; -.
DR   GeneID; 100174167; -.
DR   KEGG; pon:100174167; -.
DR   CTD; 6767; -.
DR   eggNOG; KOG1308; Eukaryota.
DR   InParanoid; Q5RF31; -.
DR   OrthoDB; 1282821at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   CDD; cd14438; Hip_N; 1.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR034649; Hip_N.
DR   InterPro; IPR041243; STI1.
DR   InterPro; IPR006636; STI1_HS-bd.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF18253; HipN; 1.
DR   Pfam; PF17830; STI1; 1.
DR   SMART; SM00727; STI1; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Chaperone; Cytoplasm; Phosphoprotein; Reference proteome;
KW   Repeat; TPR repeat.
FT   CHAIN           1..369
FT                   /note="Hsc70-interacting protein"
FT                   /id="PRO_0000190813"
FT   REPEAT          114..147
FT                   /note="TPR 1"
FT   REPEAT          149..181
FT                   /note="TPR 2"
FT   REPEAT          183..215
FT                   /note="TPR 3"
FT   DOMAIN          319..358
FT                   /note="STI1"
FT   REGION          38..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          256..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..71
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..273
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         346
FT                   /note="Phosphoserine; by GRK5"
FT                   /evidence="ECO:0000250|UniProtKB:P50502"
FT   MOD_RES         353
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99L47"
FT   MOD_RES         360
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99L47"
SQ   SEQUENCE   369 AA;  41270 MW;  F346565BF4099255 CRC64;
     MDPRKVNELR AFVKMCKQDP SVLHTEEMRF LREWVESMGG KVPPATQKAK SEENTKEEKP
     DSKKVEEDLK ADEPSSEESD LEIDKEGVIE PDTDAPQEMG DENAEITEEM MDQANDKKVA
     AIEALNDGEL QKAIDLFTDA IKLNPRLAIL YAKRASVFVK LQKPNAAIRD CDRAIEINPD
     SAQPYKWRGK AHRLLGHWEE AAHDLALACK LDYDEDASAM LKEVQPKAQK IAEHRRKYER
     KREEREIKER IERVKKAREE HERAQREEEA RRQSGAQYGS FPGGFPGGMP GNLPGGMPGM
     GGGMPGMAGM PGLNEILSDP EVLAAMQDPE VMVAFQDVAQ NPANMSKYQS NPKVMNLISK
     LSAKFGGQA