ID F6SXM4_CIOIN Unreviewed; 659 AA.
AC F6SXM4;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=78 kDa glucose-regulated protein {ECO:0000256|ARBA:ARBA00029695};
DE AltName: Full=Binding-immunoglobulin protein {ECO:0000256|ARBA:ARBA00031291};
DE AltName: Full=Heat shock protein 70 family protein 5 {ECO:0000256|ARBA:ARBA00031035};
DE AltName: Full=Heat shock protein family A member 5 {ECO:0000256|ARBA:ARBA00030223};
DE AltName: Full=Immunoglobulin heavy chain-binding protein {ECO:0000256|ARBA:ARBA00033037};
GN Name=LOC101242470 {ECO:0000313|Ensembl:ENSCINP00000019494.3};
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:ENSCINP00000019494.3, 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:ENSCINP00000019494.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
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DR EMBL; EAAA01002972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F6SXM4; -.
DR STRING; 7719.ENSCINP00000019494; -.
DR Ensembl; ENSCINT00000019494.3; ENSCINP00000019494.3; ENSCING00000009590.3.
DR GeneTree; ENSGT00940000154787; -.
DR HOGENOM; CLU_005965_3_0_1; -.
DR InParanoid; F6SXM4; -.
DR OMA; AYTKNQD; -.
DR TreeFam; TF105044; -.
DR Proteomes; UP000008144; Chromosome 9.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; 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:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR CDD; cd10241; HSPA5-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR042050; BIP_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:SF144; ENDOPLASMIC RETICULUM CHAPERONE BIP; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 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 Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000008144};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..659
FT /note="78 kDa glucose-regulated protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003346693"
FT REGION 636..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 280..307
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 659 AA; 72300 MW; E5032B05F77EF5F8 CRC64;
EMRVFQNILL AIAGFCLVSA VFGDEESKDV GTVIGIDLGT TYSCVGVFKN GRVEIIANDQ
GNRITPSYVA FTAEGDRLIG DAAKNQLTSN PENTVFDAKR LIGRAWSEKG VQSDLKYFPF
TVKNKNSKPH VEVNVKGQKK VFAAEEISAM VLGKMKEIAE AYLGKTVTHA VVTVPAYFND
AQRTATKDAG VIAGLNVMRI INEPTAAAIA YGLDKKEGEK NILVFDLGGG TFDVSMLTID
NGVFEVISTN GDTHLGGEDF DQRVMDYFMK LYKKKRGKDM RRDNRAVQKL RREVEKAKRA
LSSSQVATVE IESFFEGEDF SETLTRAKFE ELNMDLFRST MVPVKKVLED ADLTVKDVDE
VVLVGGSTRI PKIQQLVKDH FKGKEPNRGI NPDEAVAFGA AVQAGVLGGE SDTGDLVLLD
VCPLTLGIET VGGVMTKLIG RNTVVPTKKS QIFSTASDNQ PTVTINVLEG ERAMTKDNHH
LGKFDLTGIP PAPRGVPQIE VTFEIDVNGI LRVSAEDKGT GNKEKITIKN DDNRLSKEDI
ERMVQDAEKF ASEDQKLKEK VDAKNELESY AYSLKNQVGD KEKLGGKLSD EDKETVTKAV
EETIKWLDDH QEGAEKEDYE AQKKKMEEVV QPIVSKIYQG GEGGAPPPPG GETEDKDEL
//
