ID   ENPL_BOVIN              Reviewed;         804 AA.
AC   Q95M18; Q3MHX8;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=Endoplasmin;
DE   AltName: Full=94 kDa glucose-regulated protein;
DE            Short=GRP-94;
DE   AltName: Full=Heat shock protein 90 kDa beta member 1;
DE   Flags: Precursor;
GN   Name=HSP90B1; Synonyms=GRP94, TRA1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=11691631; DOI=10.1016/s1096-4959(01)00464-x;
RA   Watanabe A., Uchida I., Nakata K., Fujimoto Y., Oikawa S.;
RT   "Molecular cloning of bovine (Bos taurus) cDNA encoding a 94-kDa glucose-
RT   regulated protein and developmental changes in its mRNA and protein content
RT   in the mammary gland.";
RL   Comp. Biochem. Physiol. 130B:547-557(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Molecular chaperone that functions in the processing and
CC       transport of secreted proteins. When associated with CNPY3, required
CC       for proper folding of Toll-like receptors. Functions in endoplasmic
CC       reticulum associated degradation (ERAD). Has ATPase activity. May
CC       participate in the unfolding of cytosolic leaderless cargos (lacking
CC       the secretion signal sequence) such as the interleukin 1/IL-1 to
CC       facilitate their translocation into the ERGIC (endoplasmic reticulum-
CC       Golgi intermediate compartment) and secretion; the translocation
CC       process is mediated by the cargo receptor TMED10 (By similarity).
CC       {ECO:0000250|UniProtKB:P08113, ECO:0000250|UniProtKB:P14625}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Component of an EIF2 complex at
CC       least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1
CC       and HSPA5 (By similarity). Part of a large chaperone multiprotein
CC       complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6,
CC       PPIB, SDF2L1, UGGT1 and very small amounts of ERP29, but not, or at
CC       very low levels, CALR nor CANX. Interacts with AIMP1; regulates its
CC       retention in the endoplasmic reticulum. Interacts with OS9 (By
CC       similarity). Interacts with CNPY3; this interaction is disrupted in the
CC       presence of ATP. Interacts with several TLRs, including TLR4 and TLR9,
CC       but not with TLR3 (By similarity). Interacts with MZB1 in a calcium-
CC       dependent manner (By similarity). Interacts with METTL23 (By
CC       similarity). Interacts with IL1B; the interaction facilitates cargo
CC       translocation into the ERGIC (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P14625}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000250|UniProtKB:Q66HD0}. Sarcoplasmic reticulum lumen
CC       {ECO:0000250|UniProtKB:P41148}. Melanosome
CC       {ECO:0000250|UniProtKB:P14625}.
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR   EMBL; AB025193; BAB69766.1; -; mRNA.
DR   EMBL; BC104549; AAI04550.1; -; mRNA.
DR   RefSeq; NP_777125.1; NM_174700.2.
DR   AlphaFoldDB; Q95M18; -.
DR   SMR; Q95M18; -.
DR   IntAct; Q95M18; 1.
DR   STRING; 9913.ENSBTAP00000004364; -.
DR   GlyCosmos; Q95M18; 6 sites, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000004364; -.
DR   PeptideAtlas; Q95M18; -.
DR   Ensembl; ENSBTAT00000004364.5; ENSBTAP00000004364.4; ENSBTAG00000003362.5.
DR   GeneID; 282646; -.
DR   KEGG; bta:282646; -.
DR   CTD; 7184; -.
DR   VEuPathDB; HostDB:ENSBTAG00000003362; -.
DR   VGNC; VGNC:49984; HSP90B1.
DR   eggNOG; KOG0020; Eukaryota.
DR   GeneTree; ENSGT01020000230401; -.
DR   HOGENOM; CLU_006684_1_3_1; -.
DR   InParanoid; Q95M18; -.
DR   OMA; YMLQETS; -.
DR   OrthoDB; 547579at2759; -.
DR   TreeFam; TF105969; -.
DR   Reactome; R-BTA-1679131; Trafficking and processing of endosomal TLR.
DR   Reactome; R-BTA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-BTA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR   Reactome; R-BTA-8957275; Post-translational protein phosphorylation.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000003362; Expressed in spermatid and 104 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; ISS:AgBase.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:AgBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:AgBase.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISS:AgBase.
DR   GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; ISS:AgBase.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0031247; P:actin rod assembly; IEA:Ensembl.
DR   GO; GO:0071318; P:cellular response to ATP; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:AgBase.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0001666; P:response to hypoxia; ISS:AgBase.
DR   GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IEA:Ensembl.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR   CDD; cd16927; HATPase_Hsp90-like; 1.
DR   Gene3D; 3.30.230.80; -; 1.
DR   Gene3D; 3.40.50.11260; -; 1.
DR   Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR019805; Heat_shock_protein_90_CS.
DR   InterPro; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   PANTHER; PTHR11528:SF97; ENDOPLASMIN; 1.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Calcium; Chaperone; Disulfide bond;
KW   Endoplasmic reticulum; Glycoprotein; Hydroxylation; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Sarcoplasmic reticulum; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..804
FT                   /note="Endoplasmin"
FT                   /id="PRO_0000013596"
FT   REGION          288..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          750..804
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           801..804
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        290..314
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        754..790
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P41148"
FT   BINDING         149
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P41148"
FT   BINDING         162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P41148"
FT   BINDING         199
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P41148"
FT   SITE            448
FT                   /note="Important for ATP hydrolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P41148"
FT   MOD_RES         64
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P14625"
FT   MOD_RES         168
FT                   /note="N6-(2-hydroxyisobutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P14625"
FT   MOD_RES         172
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q66HD0"
FT   MOD_RES         306
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P14625"
FT   MOD_RES         403
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q66HD0"
FT   MOD_RES         404
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P08113"
FT   MOD_RES         447
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P14625"
FT   MOD_RES         479
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P08113"
FT   MOD_RES         633
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P08113"
FT   MOD_RES         786
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P14625"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        217
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        445
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        481
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        502
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        138
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   804 AA;  92427 MW;  0A204A77E61F1FDE CRC64;
     MRALWVLGLC CVLLTFGSVR ADDEVDVDGT VEEDLGKSRE GSRTDDEVVQ REEEAIQLDG
     LNASQIRELR EKSEKFAFQA EVNRMMKLII NSLYKNKEIF LRELISNASD ALDKIRLISL
     TDENALAGNE ELTVKIKCDK EKNLLHVTDT GVGMTREELV KNLGTIAKSG TSEFLNKMTE
     AQEDGQSTSE LIGQFGVGFY SAFLVADKVI VTSKHNNDTQ HIWESDSNEF SVIADPRGNT
     LGRGTTITLV LKEEASDYLE LDTIKNLVKK YSQFINFPIY VWSSKTETVE EPAEEEEAAK
     EDKEESDDEA AVEEEEDEKK PKTKKVEKTV WDWELMNDIK PIWQRPSKEV EEDEYKAFYK
     SFSKESDDPM AYIHFTAEGE VTFKSILFVP TSAPRGLFDE YGSKKSDYIK LYVRRVFITD
     DFHDMMPKYL NFVKGVVDSD DLPLNVSRET LQQHKLLKVI RKKLVRKTLD MIKKIADEKY
     NDTFWKEFGT NIKLGVIEDH SNRTRLAKLL RFQSSHHPSD MTSLDQYVER MKEKQDKIYF
     MAGASRKEAE SSPFVERLLK KGYEVIYLTE PVDEYCIQAL PEFDGKRFQN VAKEGVKFDE
     SEKSKESREA VEKEFEPLLN WMKDKALKDK IEKAVVSQRL TESPCALVAS QYGWSGNMER
     IMKAQAYQTG KDISTNYYAS QKKTFEINPR HPLIRDMLRR VKEDEDDKTV SDLAVVLFET
     ATLRSGYLLP DTKAYGDRIE RMLRLSLNID PDAKVEEEPE EEPEETTEDT AEDTEQDEEE
     EMDAGTDEEE QETAEKSTAE KDEL
//