ID   HSP7C_ICTPU             Reviewed;         649 AA.
AC   P47773;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Heat shock cognate 71 kDa protein;
GN   Name=hsc70;
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8936051; DOI=10.1016/0305-0491(95)02022-5;
RA   Luft J.C., Wilson M.R., Bly J.E., Miller N.W., Clem L.W.;
RT   "Identification and characterization of a heat shock protein 70 family
RT   member in channel catfish (Ictalurus punctatus).";
RL   Comp. Biochem. Physiol. 113B:169-174(1996).
CC   -!- FUNCTION: Molecular chaperone implicated in a wide variety of cellular
CC       processes, including protection of the proteome from stress, folding
CC       and transport of newly synthesized polypeptides, activation of
CC       proteolysis of misfolded proteins and the formation and dissociation of
CC       protein complexes. Plays a pivotal role in the protein quality control
CC       system, ensuring the correct folding of proteins, the re-folding of
CC       misfolded proteins and controlling the targeting of proteins for
CC       subsequent degradation. This is achieved through cycles of ATP binding,
CC       ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity
CC       of HSP70 for polypeptides is regulated by its nucleotide bound state.
CC       In the ATP-bound form, it has a low affinity for substrate proteins.
CC       However, upon hydrolysis of the ATP to ADP, it undergoes a
CC       conformational change that increases its affinity for substrate
CC       proteins. HSP70 goes through repeated cycles of ATP hydrolysis and
CC       nucleotide exchange, which permits cycles of substrate binding and
CC       release. {ECO:0000250|UniProtKB:P11142}.
CC   -!- DOMAIN: The N-terminal nucleotide binding domain (NBD) (also known as
CC       the ATPase domain) is responsible for binding and hydrolyzing ATP. The
CC       C-terminal substrate-binding domain (SBD) (also known as peptide-
CC       binding domain) binds to the client/substrate proteins. The two domains
CC       are allosterically coupled so that, when ATP is bound to the NBD, the
CC       SBD binds relatively weakly to clients. When ADP is bound in the NBD, a
CC       conformational change enhances the affinity of the SBD for client
CC       proteins. {ECO:0000250|UniProtKB:P11142}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; U22460; AAA64872.1; -; mRNA.
DR   RefSeq; NP_001187202.1; NM_001200273.1.
DR   AlphaFoldDB; P47773; -.
DR   SMR; P47773; -.
DR   STRING; 7998.ENSIPUP00000009472; -.
DR   PRIDE; P47773; -.
DR   GeneID; 100305036; -.
DR   KEGG; ipu:100305036; -.
DR   OrthoDB; 288077at2759; -.
DR   Proteomes; UP000221080; Chromosome 16.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding; Stress response.
FT   CHAIN           1..649
FT                   /note="Heat shock cognate 71 kDa protein"
FT                   /id="PRO_0000078277"
FT   REGION          2..386
FT                   /note="Nucleotide-binding domain (NBD)"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   REGION          394..509
FT                   /note="Substrate-binding domain (SBD)"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   REGION          613..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   649 AA;  71340 MW;  D31B8D348D7583CB CRC64;
     MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDSERL IGDAAKNQVA
     MNPTNTIFDA KRLIGRRFED SVVQADMKHW PFKVISDGGR PRLEVEYKGE AKNFYPEEIS
     SMVLVKMKEI AEAYLGKSIN NAVITVPAYF NDSQRQRTKD AGTISGLNVL RIINEPTAAA
     IAYGLDKKVG SERNVLIFDL GGGTFDVSIL TIEDGIFDLK STAGDTHLGG EDFDNRMVNH
     FIAEFKRKHK KDISDNKRAV RRLATACERA KRTLSSSTQA SIEIDSLYEG VDFYTSITRA
     RFEELNADLF RGTLDPVEKA LRDAKMDKAQ VHDIVLVGGS TRIPKMEKLL QDFFNGKELN
     KSINPDEAVA YGAAVQAESS LGDKSENVQD LVLLDVTPLS LGIETAGGVM TVLIKRNTTI
     PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI
     DANGIMNVSA VDKSTGKENK ITITNDKGRL SKEDIERMVQ EAEKYKAEDD VQRDKVSAKN
     GLESYAFNMK STVEDEKLKG KISDEDKHKI LDKCNEVISW LDKNQTAEKD EYEHQQKDLE
     KVCNPIITKL YQSDGGMPGG MPDGMPGGFQ ELGAAPGGGS SGPTIEEVD