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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
 
 
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