ID H2XU53_CIOIN Unreviewed; 643 AA.
AC H2XU53;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Stress-70 protein, mitochondrial {ECO:0000256|ARBA:ARBA00019355};
DE AltName: Full=75 kDa glucose-regulated protein {ECO:0000256|ARBA:ARBA00031419};
DE AltName: Full=Heat shock 70 kDa protein 9 {ECO:0000256|ARBA:ARBA00030055};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000033187.1, ECO:0000313|Proteomes:UP000008144};
RN [1] {ECO:0000313|Proteomes:UP000008144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12481130; DOI=10.1126/science.1080049;
RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA Satoh N., Rokhsar D.S.;
RT "The draft genome of Ciona intestinalis: insights into chordate and
RT vertebrate origins.";
RL Science 298:2157-2167(2002).
RN [2] {ECO:0000313|Ensembl:ENSCINP00000033187.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EAAA01001808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H2XU53; -.
DR STRING; 7719.ENSCINP00000033187; -.
DR Ensembl; ENSCINT00000031556.1; ENSCINP00000033187.1; ENSCING00000019791.1.
DR GeneTree; ENSGT00920000149123; -.
DR HOGENOM; CLU_005965_2_1_1; -.
DR InParanoid; H2XU53; -.
DR OMA; MGTDWKI; -.
DR TreeFam; TF105046; -.
DR Proteomes; UP000008144; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR CDD; cd11733; HSPA9-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR HAMAP; MF_00332; DnaK; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR012725; Chaperone_DnaK.
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 NCBIfam; TIGR02350; prok_dnaK; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000008144}.
FT REGION 618..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 517..564
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 643 AA; 70109 MW; 26E6B896E8455A0D CRC64;
RFIGRSFASE AVRGAVVGID LGTTNSCVAV MDGKQAKVLE NAEGSRTTPS VIAFTPEGER
LAGTPARRQA VTNPGNTFYA TKRLIGRRFD DAEIQKELKT STFKIVKATN GDAWVEGTDG
KRYSPSQIGA FVLTKMKETA ESYLNQPVKN AVVTVPAYFN DSQRQATKDA GQISGLNVLR
VINEPTAAAL AYGMDKSEDK IIAVYDLGGG TFDISLLEIQ KGVFEVKSTN GDTLLGGEDF
DNVLVEHLVK EFLRDQGVDL KKDKMAIQRV KEAAEKAKME LSSSLQTDIN LPYLTMDASG
PKHMNLKMSR SQLEQLVGGL IKRTVQPCEK AIQDAEVSKS DIGEIILVGG MTRMPKVQFT
VQSIFGKQAS KAVNPDEAVA MGAAIQGGVL AGNVTDVLLL DVTPLSLGIE TLGGVFTKLI
TRNTTIPTKK SQVFSTAADG QTQVEIKVHQ GEREMALDNK MLGQFQLVGI PPAPRGVPQV
EVTFDIDANG IVNVSAKDKG TGREQQIVIQ SSGGLSKDEI ENMIKRAEEY AEEDKQRKEK
VEIVNQAENV IHDTETKMEE FKDQLPQDEC EQIKEEITKV REILANKDTQ SVEVIREGFS
GLQQKSLKLF EMAYKKMAAE KEQSGGSSET SSDSSDDQKK QQQ
//
