LOCUS       NP_112384                368 aa            linear   ROD 03-APR-2024
DEFINITION  hsc70-interacting protein [Rattus norvegicus].
ACCESSION   NP_112384
VERSION     NP_112384.1
DBSOURCE    REFSEQ: accession NM_031122.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Xilouri,M. and Stefanis,L.
  TITLE     Chaperone mediated autophagy to the rescue: A new-fangled target
            for the treatment of neurodegenerative diseases
  JOURNAL   Mol Cell Neurosci 66 (Pt A), 29-36 (2015)
   PUBMED   25724482
  REMARK    Review article
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Li,Z., Hartl,F.U. and Bracher,A.
  TITLE     Structure and function of Hip, an attenuator of the Hsp70 chaperone
            cycle
  JOURNAL   Nat Struct Mol Biol 20 (8), 929-935 (2013)
   PUBMED   23812373
  REMARK    GeneRIF: The tetratricopeptide repeat domain of rat Hip with the
            Hsp70 ATPase domain through an extensive interface, to form a
            bracket that locks ADP in the binding cleft.
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Archambaud,C., Nahori,M.A., Soubigou,G., Becavin,C., Laval,L.,
            Lechat,P., Smokvina,T., Langella,P., Lecuit,M. and Cossart,P.
  TITLE     Impact of lactobacilli on orally acquired listeriosis
  JOURNAL   Proc Natl Acad Sci U S A 109 (41), 16684-16689 (2012)
   PUBMED   23012479
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Zhang,Q.G., Han,D., Wang,R.M., Dong,Y., Yang,F., Vadlamudi,R.K. and
            Brann,D.W.
  TITLE     C terminus of Hsc70-interacting protein (CHIP)-mediated degradation
            of hippocampal estrogen receptor-alpha and the critical period
            hypothesis of estrogen neuroprotection
  JOURNAL   Proc Natl Acad Sci U S A 108 (35), E617-E624 (2011)
   PUBMED   21808025
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Prescott,J. and Coetzee,G.A.
  TITLE     Molecular chaperones throughout the life cycle of the androgen
            receptor
  JOURNAL   Cancer Lett 231 (1), 12-19 (2006)
   PUBMED   16356826
  REMARK    Review article
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Demand,J., Luders,J. and Hohfeld,J.
  TITLE     The carboxy-terminal domain of Hsc70 provides binding sites for a
            distinct set of chaperone cofactors
  JOURNAL   Mol Cell Biol 18 (4), 2023-2028 (1998)
   PUBMED   9528774
REFERENCE   8  (residues 1 to 368)
  AUTHORS   Bruce,B.D. and Churchich,J.
  TITLE     Characterization of the molecular-chaperone function of the
            heat-shock-cognate-70-interacting protein
  JOURNAL   Eur J Biochem 245 (3), 738-744 (1997)
   PUBMED   9183013
REFERENCE   9  (residues 1 to 368)
  AUTHORS   Irmer,H. and Hohfeld,J.
  TITLE     Characterization of functional domains of the eukaryotic
            co-chaperone Hip
  JOURNAL   J Biol Chem 272 (4), 2230-2235 (1997)
   PUBMED   8999928
REFERENCE   10 (residues 1 to 368)
  AUTHORS   Hohfeld,J., Minami,Y. and Hartl,F.U.
  TITLE     Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40
            reaction cycle
  JOURNAL   Cell 83 (4), 589-598 (1995)
   PUBMED   7585962
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X82021.1, FQ212434.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..368
                     /product="hsc70-interacting protein"
                     /note="hip; protein ST13 homolog; suppression of
                     tumorigenicity 13 (colon carcinoma) Hsp70-interacting
                     protein"
                     /calculated_mol_wt=41149
     Region          3..43
                     /region_name="Hip_N"
                     /note="N-terminal dimerization domain of the
                     Hsp70-interacting protein (Hip) and similar proteins;
                     cd14438"
                     /db_xref="CDD:271228"
     Site            order(5..6,8..10,12..13,16..17,23,27,30..31,33..35,37..43)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:271228"
     Region          38..81
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50503.1)"
     Region          113..146
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P50503.1)"
     Region          113..141
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(114,117..118,121..122,124,148,151..152,155..156,
                     158..159,182,185..186,189..190,193)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          <127..221
                     /region_name="NlpI"
                     /note="Lipoprotein NlpI, contains TPR repeats [Cell
                     wall/membrane/envelope biogenesis]; COG4785"
                     /db_xref="CDD:443815"
     Region          146..176
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          147..180
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P50503.1)"
     Region          181..214
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P50503.1)"
     Region          181..209
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          256..299
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50503.1)"
     Region          318..357
                     /region_name="STI1"
                     /note="Heat shock chaperonin-binding motif; smart00727"
                     /db_xref="CDD:128966"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GRK5.
                     /evidence=ECO:0000250|UniProtKB:P50502; propagated from
                     UniProtKB/Swiss-Prot (P50503.1)"
     Site            352
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99L47; propagated from
                     UniProtKB/Swiss-Prot (P50503.1)"
     Site            359
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99L47; propagated from
                     UniProtKB/Swiss-Prot (P50503.1)"
     CDS             1..368
                     /gene="St13"
                     /coded_by="NM_031122.2:60..1166"
                     /db_xref="GeneID:81800"
                     /db_xref="RGD:621312"
ORIGIN      
        1 mdprkvselr afvkmcrqdp svlhteemrf lrewvesmgg kvppathkak seentkeekr
       61 dkttednikt eepsseesdl eidnegviea dtdapqemgd enaeiteamm deanekkgaa
      121 idalndgelq kaidlftdai klnprlaily akrasvfvkl qkpnaairdc draieinpds
      181 aqpykwrgka hrllghweea ardlalackl dydedasaml revqpraqki aehrrkyerk
      241 reereikeri ervkkareeh ekaqreeear rqsgsqfgsf pggfpggmpg nfpggmpgmg
      301 gampgmagmp glneilsdpe vlaamqdpev mvafqdvaqn psnmskyqnn pkvmnliskl
      361 sakfgghs
//
