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Endoplasmin (94 kDa glucose-regulated protein) (GRP-94) (Heat shock protein 90 kDa beta member 1)

 ENPL_BOVIN              Reviewed;         804 AA.
Q95M18; Q3MHX8;
25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
22-NOV-2017, entry version 131.
RecName: Full=Endoplasmin;
AltName: Full=94 kDa glucose-regulated protein;
Short=GRP-94;
AltName: Full=Heat shock protein 90 kDa beta member 1;
Flags: Precursor;
Name=HSP90B1; Synonyms=GRP94, TRA1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary gland;
PubMed=11691631; DOI=10.1016/S1096-4959(01)00464-X;
Watanabe A., Uchida I., Nakata K., Fujimoto Y., Oikawa S.;
"Molecular cloning of bovine (Bos taurus) cDNA encoding a 94-kDa
glucose-regulated protein and developmental changes in its mRNA and
protein content in the mammary gland.";
Comp. Biochem. Physiol. 130B:547-557(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Uterus;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Molecular chaperone that functions in the processing and
transport of secreted proteins. When associated with CNPY3,
required for proper folding of Toll-like receptors. Functions in
endoplasmic reticulum associated degradation (ERAD). Has ATPase
activity (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer; disulfide-linked. Component of an EIF2 complex
at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2,
HSP90B1 and HSPA5 (By similarity). Part of a large chaperone
multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU,
PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts
of ERP29, but not, or at very low levels, CALR nor CANX. Interacts
with AIMP1; regulates its retention in the endoplasmic reticulum.
Interacts with OS9 (By similarity). Interacts with CNPY3; this
interaction is disrupted in the presence of ATP. Interacts with
several TLRs, including TLR4 and TLR9, but not with TLR3 (By
similarity). Interacts with MZB1 in a calcium-dependent manner (By
similarity). Interacts with METTL23 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
Melanosome {ECO:0000250}.
-!- PTM: Phosphorylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the heat shock protein 90 family.
{ECO:0000305}.
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EMBL; AB025193; BAB69766.1; -; mRNA.
EMBL; BC104549; AAI04550.1; -; mRNA.
RefSeq; NP_777125.1; NM_174700.2.
UniGene; Bt.8686; -.
ProteinModelPortal; Q95M18; -.
SMR; Q95M18; -.
IntAct; Q95M18; 1.
STRING; 9913.ENSBTAP00000004364; -.
PaxDb; Q95M18; -.
PeptideAtlas; Q95M18; -.
PRIDE; Q95M18; -.
Ensembl; ENSBTAT00000004364; ENSBTAP00000004364; ENSBTAG00000003362.
GeneID; 282646; -.
KEGG; bta:282646; -.
CTD; 7184; -.
eggNOG; KOG0020; Eukaryota.
eggNOG; COG0326; LUCA.
GeneTree; ENSGT00900000140978; -.
HOGENOM; HOG000031988; -.
HOVERGEN; HBG007374; -.
InParanoid; Q95M18; -.
KO; K09487; -.
OMA; SDHEIFL; -.
OrthoDB; EOG091G0270; -.
TreeFam; TF105969; -.
Reactome; R-BTA-1679131; Trafficking and processing of endosomal TLR.
Reactome; R-BTA-3000480; Scavenging by Class A Receptors.
Reactome; R-BTA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-BTA-8957275; Post-translational protein phosphorylation.
Proteomes; UP000009136; Chromosome 5.
Bgee; ENSBTAG00000003362; -.
GO; GO:0005829; C:cytosol; ISS:AgBase.
GO; GO:0005783; C:endoplasmic reticulum; ISS:AgBase.
GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IEA:Ensembl.
GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0030496; C:midbody; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:AgBase.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISS:AgBase.
GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; ISS:AgBase.
GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
GO; GO:0031247; P:actin rod assembly; IEA:Ensembl.
GO; GO:0071318; P:cellular response to ATP; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:AgBase.
GO; GO:0006457; P:protein folding; IEA:InterPro.
GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; ISS:AgBase.
GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IEA:Ensembl.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
CDD; cd00075; HATPase_c; 1.
Gene3D; 3.30.565.10; -; 1.
HAMAP; MF_00505; HSP90; 1.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR019805; Heat_shock_protein_90_CS.
InterPro; IPR037196; HSP90_C.
InterPro; IPR001404; Hsp90_fam.
InterPro; IPR020575; Hsp90_N.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
PANTHER; PTHR11528; PTHR11528; 1.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF00183; HSP90; 1.
PIRSF; PIRSF002583; Hsp90; 1.
PRINTS; PR00775; HEATSHOCK90.
SMART; SM00387; HATPase_c; 1.
SUPFAM; SSF110942; SSF110942; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF55874; SSF55874; 2.
PROSITE; PS00014; ER_TARGET; 1.
PROSITE; PS00298; HSP90; 1.
2: Evidence at transcript level;
Acetylation; ATP-binding; Calcium; Chaperone; Complete proteome;
Disulfide bond; Endoplasmic reticulum; Glycoprotein;
Nucleotide-binding; Phosphoprotein; Reference proteome; Signal.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 804 Endoplasmin.
/FTId=PRO_0000013596.
MOTIF 801 804 Prevents secretion from ER.
{ECO:0000255}.
BINDING 107 107 ATP. {ECO:0000250}.
BINDING 149 149 ATP. {ECO:0000250}.
BINDING 168 168 ATP. {ECO:0000250}.
BINDING 199 199 ATP; via amide nitrogen. {ECO:0000250}.
BINDING 448 448 ATP. {ECO:0000250}.
MOD_RES 64 64 Phosphoserine.
{ECO:0000250|UniProtKB:P14625}.
MOD_RES 172 172 Phosphoserine.
{ECO:0000250|UniProtKB:Q66HD0}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000250|UniProtKB:P14625}.
MOD_RES 403 403 Phosphoserine.
{ECO:0000250|UniProtKB:Q66HD0}.
MOD_RES 404 404 N6-succinyllysine.
{ECO:0000250|UniProtKB:P08113}.
MOD_RES 447 447 Phosphoserine.
{ECO:0000250|UniProtKB:P14625}.
MOD_RES 479 479 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08113}.
MOD_RES 633 633 N6-succinyllysine.
{ECO:0000250|UniProtKB:P08113}.
MOD_RES 786 786 Phosphothreonine.
{ECO:0000250|UniProtKB:P14625}.
CARBOHYD 62 62 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 107 107 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 217 217 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 445 445 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 481 481 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 502 502 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 138 138 Interchain. {ECO:0000250}.
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


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