F10A1_RAT
ID F10A1_RAT Reviewed; 368 AA.
AC P50503;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
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, Hip;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND INTERACTION WITH HSC70
RP AND DNAJ HOMOLOGS.
RC STRAIN=Sprague-Dawley;
RX PubMed=7585962; DOI=10.1016/0092-8674(95)90099-3;
RA Hoehfeld J., Minami Y., Hartl F.-U.;
RT "Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction
RT cycle.";
RL Cell 83:589-598(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 118-141, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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.
CC {ECO:0000269|PubMed:7585962}.
CC -!- SUBUNIT: Homotetramer. Interacts with HSC70 as well as DNAJ homologs
CC and HSP90. Interacts (via the C-terminus 302- 318 AA) with GRK5 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P50503; P06211: Esr1; NbExp=4; IntAct=EBI-917694, EBI-7983651;
CC P50503; P50503: St13; NbExp=2; IntAct=EBI-917694, EBI-917694;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the FAM10 family. {ECO:0000305}.
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DR EMBL; X82021; CAA57546.1; -; mRNA.
DR EMBL; BC078804; AAH78804.1; -; mRNA.
DR RefSeq; NP_112384.1; NM_031122.1.
DR PDB; 4J8C; X-ray; 1.10 A; A/B=1-44.
DR PDB; 4J8D; X-ray; 2.80 A; A/B/C/D=78-247.
DR PDB; 4J8E; X-ray; 2.60 A; A/B=78-247.
DR PDB; 4J8F; X-ray; 2.70 A; A=77-247.
DR PDBsum; 4J8C; -.
DR PDBsum; 4J8D; -.
DR PDBsum; 4J8E; -.
DR PDBsum; 4J8F; -.
DR AlphaFoldDB; P50503; -.
DR SMR; P50503; -.
DR DIP; DIP-37019N; -.
DR IntAct; P50503; 4.
DR STRING; 10116.ENSRNOP00000025925; -.
DR iPTMnet; P50503; -.
DR PhosphoSitePlus; P50503; -.
DR SwissPalm; P50503; -.
DR jPOST; P50503; -.
DR PaxDb; P50503; -.
DR PRIDE; P50503; -.
DR GeneID; 81800; -.
DR KEGG; rno:81800; -.
DR UCSC; RGD:621312; rat.
DR CTD; 6767; -.
DR RGD; 621312; St13.
DR VEuPathDB; HostDB:ENSRNOG00000018920; -.
DR eggNOG; KOG1308; Eukaryota.
DR HOGENOM; CLU_026202_0_1_1; -.
DR InParanoid; P50503; -.
DR OMA; TVLNMPQ; -.
DR OrthoDB; 1282821at2759; -.
DR PhylomeDB; P50503; -.
DR TreeFam; TF313244; -.
DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR PRO; PR:P50503; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000019070; Expressed in adult mammalian kidney and 19 other tissues.
DR Genevisible; P50503; RN.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0051087; F:chaperone binding; IPI:RGD.
DR GO; GO:0032564; F:dATP binding; IDA:RGD.
DR GO; GO:0030544; F:Hsp70 protein binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0051082; F:unfolded protein binding; IDA:RGD.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IDA:RGD.
DR GO; GO:0061084; P:negative regulation of protein refolding; IDA:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chaperone; Cytoplasm; Direct protein sequencing;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..368
FT /note="Hsc70-interacting protein"
FT /id="PRO_0000190814"
FT REPEAT 113..146
FT /note="TPR 1"
FT REPEAT 147..180
FT /note="TPR 2"
FT REPEAT 181..214
FT /note="TPR 3"
FT DOMAIN 318..357
FT /note="STI1"
FT REGION 38..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 345
FT /note="Phosphoserine; by GRK5"
FT /evidence="ECO:0000250|UniProtKB:P50502"
FT MOD_RES 352
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L47"
FT MOD_RES 359
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L47"
FT HELIX 3..18
FT /evidence="ECO:0007829|PDB:4J8C"
FT HELIX 20..24
FT /evidence="ECO:0007829|PDB:4J8C"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:4J8C"
FT HELIX 29..37
FT /evidence="ECO:0007829|PDB:4J8C"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:4J8F"
FT HELIX 107..124
FT /evidence="ECO:0007829|PDB:4J8E"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:4J8E"
FT HELIX 129..142
FT /evidence="ECO:0007829|PDB:4J8E"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:4J8E"
FT HELIX 163..176
FT /evidence="ECO:0007829|PDB:4J8E"
FT HELIX 182..194
FT /evidence="ECO:0007829|PDB:4J8E"
FT HELIX 197..210
FT /evidence="ECO:0007829|PDB:4J8E"
FT HELIX 214..242
FT /evidence="ECO:0007829|PDB:4J8F"
SQ SEQUENCE 368 AA; 41280 MW; 1AEBFC0526AE5CE1 CRC64;
MDPRKVSELR AFVKMCRQDP SVLHTEEMRF LREWVESMGG KVPPATHKAK SEENTKEEKR
DKTTEDNIKT EEPSSEESDL EIDNEGVIEA DTDAPQEMGD ENAEITEAMM DEANEKKGAA
IDALNDGELQ KAIDLFTDAI KLNPRLAILY AKRASVFVKL QKPNAAIRDC DRAIEINPDS
AQPYKWRGKA HRLLGHWEEA ARDLALACKL DYDEDASAML REVQPRAQKI AEHRRKYERK
REEREIKERI ERVKKAREEH EKAQREEEAR RQSGSQFGSF PGGFPGGMPG NFPGGMPGMG
GAMPGMAGMP GLNEILSDPE VLAAMQDPEV MVAFQDVAQN PSNMSKYQNN PKVMNLISKL
SAKFGGHS
