ID   F10A1_CHICK             Reviewed;         361 AA.
AC   Q5ZLF0;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
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; ORFNames=RCJMB04_6h13;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FAM10 family. {ECO:0000305}.
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DR   EMBL; AJ719784; CAG31443.1; -; mRNA.
DR   RefSeq; NP_001025928.1; NM_001030757.1.
DR   AlphaFoldDB; Q5ZLF0; -.
DR   SMR; Q5ZLF0; -.
DR   STRING; 9031.ENSGALP00000019569; -.
DR   PaxDb; Q5ZLF0; -.
DR   GeneID; 418003; -.
DR   KEGG; gga:418003; -.
DR   CTD; 144106; -.
DR   VEuPathDB; HostDB:geneid_418003; -.
DR   eggNOG; KOG1308; Eukaryota.
DR   InParanoid; Q5ZLF0; -.
DR   OrthoDB; 1282821at2759; -.
DR   PhylomeDB; Q5ZLF0; -.
DR   PRO; PR:Q5ZLF0; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030544; F:Hsp70 protein binding; IBA:GO_Central.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
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   Pfam; PF13181; TPR_8; 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   Chaperone; Cytoplasm; Reference proteome; Repeat; TPR repeat.
FT   CHAIN           1..361
FT                   /note="Hsc70-interacting protein"
FT                   /id="PRO_0000190815"
FT   REPEAT          112..145
FT                   /note="TPR 1"
FT   REPEAT          147..179
FT                   /note="TPR 2"
FT   REPEAT          181..213
FT                   /note="TPR 3"
FT   DOMAIN          311..350
FT                   /note="STI1"
FT   REGION          39..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          254..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..74
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..98
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   361 AA;  40158 MW;  110C1C5031695CE8 CRC64;
     MDSRKLGELR AFVRLCKQNP GLLHTEELGF LREWVESMGG TIPPAPASTS TDETSKGKAE
     EQPEEPVKSP EPESEESDLE IDNEGVIEPD NDDPQEMGDE NVEVTEEMMD QANEKKMEAI
     NALSEGDLQK AVNLFTDAIK LNPCLAILYA KRASVFVKLQ KPNAAIRDCD RAIKINPDSA
     QTYKWRGKAH RLLGHWEEAA HDLALACKLD YDEDASAMLK EVQPRAQKIA EHRRKYERKR
     EEKEIKERME RVKKAREEHE RAQREEEARR QAGGAQFGGF PGGFPGGFPG AMPGGMPGMA
     GMPGLNEILS DPEVLAAMQD PEVMAAFQDV AQNPANMSKY QNNPKVMSLI TKLSAKFGSK
     P